2323737
2RQKSFR5
ranish
items
1
0
date
desc
year
1
1
4297
https://ranish.isbscience.org/wp-content/plugins/zotpress/
%7B%22status%22%3A%22success%22%2C%22updateneeded%22%3Afalse%2C%22instance%22%3A%22zotpress-32b7d5d884485732d08c5842ba628450%22%2C%22meta%22%3A%7B%22request_last%22%3A50%2C%22request_next%22%3A50%2C%22used_cache%22%3Atrue%7D%2C%22data%22%3A%5B%7B%22key%22%3A%22L2PM22CC%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Luo%20and%20Ranish%22%2C%22parsedDate%22%3A%222024%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELuo%2C%20J.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282024%29.%20Isobaric%20crosslinking%20mass%20spectrometry%20technology%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20complexes.%20%3Ci%3EELife%3C%5C%2Fi%3E%2C%20%3Ci%3E13%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.7554%5C%2FeLife.99809.2%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.7554%5C%2FeLife.99809.2%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DL2PM22CC%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DWG5NDIAK%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Isobaric%20crosslinking%20mass%20spectrometry%20technology%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20complexes%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Dynamic%20conformational%20and%20structural%20changes%20in%20proteins%20and%20protein%20complexes%20play%20a%20central%20and%20ubiquitous%20role%20in%20the%20regulation%20of%20protein%20function%2C%20yet%20it%20is%20very%20challenging%20to%20study%20these%20changes%2C%20especially%20for%20large%20protein%20complexes%2C%20under%20physiological%20conditions.%20Here%20we%20introduce%20a%20novel%20isobaric%20crosslinker%2C%20Qlinker%2C%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20protein%20complexes%20using%20quantitative%20crosslinking%20mass%20spectrometry%20%28qCLMS%29.%20Qlinkers%20are%20small%20and%20simple%2C%20amine-reactive%20molecules%20with%20an%20optimal%20extended%20distance%20of%20%5Cu223c10%20%5Cu00c5%20which%20use%20MS2%20reporter%20ions%20for%20relative%20quantification%20of%20Qlinker-modified%20peptides%20derived%20from%20different%20samples.%20We%20synthesized%20the%202-plex%20Q2linker%20and%20showed%20that%20the%20Q2linker%20can%20provide%20quantitative%20crosslinking%20data%20that%20pinpoints%20key%20conformational%20and%20structural%20changes%20in%20biosensors%2C%20binary%20and%20ternary%20complexes%20composed%20of%20the%20general%20transcription%20factors%20TBP%2C%20TFIIA%2C%20and%20TFIIB%2C%20and%20RNA%20polymerase%20II%20%28pol%20II%29%20complexes.%22%2C%22date%22%3A%222024%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.7554%5C%2FeLife.99809.2%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Felifesciences.org%5C%2Freviewed-preprints%5C%2F99809%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-10-30T19%3A47%3A24Z%22%7D%7D%2C%7B%22key%22%3A%227R8BDWFW%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kopp%20et%20al.%22%2C%22parsedDate%22%3A%222024%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKopp%2C%20A.%2C%20Nissa%2C%20M.%20U.%2C%20Dollinger%2C%20R.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Brand%2C%20M.%20%282024%29.%203106%20%26%23x2013%3B%20PROTEOMICS%20AND%20GENOMICS%20STUDIES%20REVEALED%20A%20NEW%20ROLE%20FOR%20MLL%20PARTIAL%20TANDEM%20DUPLICATION%20%28PTD%29%20IN%20MYELODYSPLASTIC%20SYNDROME%20%28MDS%29%20AND%20ACUTE%20MYELOID%20LEUKEMIA%20%28AML%29.%20%3Ci%3EExperimental%20Hematology%3C%5C%2Fi%3E%2C%20%3Ci%3E137%3C%5C%2Fi%3E%2C%20104428.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.exphem.2024.104428%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.exphem.2024.104428%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D7R8BDWFW%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%223106%20%5Cu2013%20PROTEOMICS%20AND%20GENOMICS%20STUDIES%20REVEALED%20A%20NEW%20ROLE%20FOR%20MLL%20PARTIAL%20TANDEM%20DUPLICATION%20%28PTD%29%20IN%20MYELODYSPLASTIC%20SYNDROME%20%28MDS%29%20AND%20ACUTE%20MYELOID%20LEUKEMIA%20%28AML%29%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Audrey%22%2C%22lastName%22%3A%22Kopp%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mehar%20Un%22%2C%22lastName%22%3A%22Nissa%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Roberta%22%2C%22lastName%22%3A%22Dollinger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marjorie%22%2C%22lastName%22%3A%22Brand%22%7D%5D%2C%22abstractNote%22%3A%22The%20Mixed%20Lineage%20Leukemia%201%20%28MLL%29%20gene%2C%20a%20histone-3-lysine-4-methyltransferase%2C%20is%20a%20critical%20transcription%20factor%20in%20cell%20fate%20determination%20during%20hematopoiesis%20and%20is%20frequently%20mutated%20in%20patients%20with%20myelodysplastic%20syndrome%20%28MDS%29%20and%20acute%20myeloid%20leukemia%20%28AML%29.%20While%20the%20mechanism%20of%20MLL%20chimeric%20fusion%20proteins%20has%20been%20extensively%20studied%2C%20the%20mechanism%20through%20which%20another%20oncogenic%20mutant%2C%20the%20Partial%20Tandem%20Duplication%20%28PTD%29%20of%20the%20MLL%20N-terminal%20DNA%20binding%20domain%20promotes%20leukemogenesis%2C%20remains%20unknown.%20Most%20commonly%2C%20the%20PTD%20is%20formed%20through%20an%20in-frame%20duplication%20of%20exons%202%20through%206%2C%20although%20other%20rearrangements%20have%20also%20been%20identified.%20However%2C%20MLLPTD%20was%20recently%20recognized%20by%20the%20Molecular%20International%20Prognostic%20Scoring%20System%20Model%20as%20one%20of%20the%20strongest%20predictors%20of%20adverse%20outcomes%20in%20MDS%2C%20pressing%20the%20need%20to%20unravel%20its%20role%20in%20the%20leukemogenic%20process.%20Our%20approach%20to%20understanding%20how%20MLLPTD%20drives%20leukemogenesis%20involved%20different%20techniques.%20We%20did%20targeted%20QconCAT%20mass%20spectrometry%2C%20which%20utilizes%20a%20known%20amount%20of%20peptides%20incorporated%20in%20a%20hybrid%20protein%20named%20QconCAT.%20Once%20it%20is%20included%20in%20the%20nuclear%20extract%2C%20we%20detected%20copy%20numbers%20of%20the%20endogenous%20protein.%20At%20the%20molecular%20level%2C%20we%20demonstrated%20that%20MLL-PTD%20cannot%20interact%20with%20the%20WRAD%20complex%2C%20a%20complex%20of%20proteins%20required%20for%20MLL%20enzymatic%20activity%2C%20suggesting%20a%20defect%20of%20MLL%20function.%20Instead%2C%20MLL-PTD%20associates%20with%20distinct%20chromatin-modifying%20enzymes.%20In%20addition%2C%20to%20further%20study%20MLLPTD%2C%20we%20developed%20and%20validated%20an%20antibody%20that%20recognizes%20the%20exon%206-2%20peptide.%20Using%20this%20antibody%2C%20we%20performed%20CUT%26Tag%20revealing%20for%20the%20first%20time%20the%20genome-wide%20binding%20of%20MLLPTD.%20Taken%20together%20our%20results%20provide%20critical%20insights%20into%20the%20mechanism%20through%20which%20MLL-PTD%20leads%20to%20the%20deregulation%20of%20gene%20expression%20contributing%20to%20the%20progression%20of%20MDS%20to%20AML.%22%2C%22date%22%3A%222024%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.exphem.2024.104428%22%2C%22ISSN%22%3A%220301-472X%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.sciencedirect.com%5C%2Fscience%5C%2Farticle%5C%2Fpii%5C%2FS0301472X2400287X%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-10-28T17%3A00%3A29Z%22%7D%7D%2C%7B%22key%22%3A%22QLW4ZUUZ%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Yang%20et%20al.%22%2C%22parsedDate%22%3A%222024%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EYang%2C%20Z.%2C%20Mameri%2C%20A.%2C%20Cattoglio%2C%20C.%2C%20Lachance%2C%20C.%2C%20Florez%20Ariza%2C%20A.%20J.%2C%20Luo%2C%20J.%2C%20Humbert%2C%20J.%2C%20Sudarshan%2C%20D.%2C%20Banerjea%2C%20A.%2C%20Galloy%2C%20M.%2C%20Fradet-Turcotte%2C%20A.%2C%20Lambert%2C%20J.-P.%2C%20Ranish%2C%20J.%20A.%2C%20C%26%23xF4%3Bt%26%23xE9%3B%2C%20J.%2C%20%26amp%3B%20Nogales%2C%20E.%20%282024%29.%20Structural%20insights%20into%20the%20human%20NuA4%5C%2FTIP60%20acetyltransferase%20and%20chromatin%20remodeling%20complex.%20%3Ci%3EScience%20%28New%20York%2C%20N.Y.%29%3C%5C%2Fi%3E%2C%20eadl5816.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1126%5C%2Fscience.adl5816%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1126%5C%2Fscience.adl5816%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DQLW4ZUUZ%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structural%20insights%20into%20the%20human%20NuA4%5C%2FTIP60%20acetyltransferase%20and%20chromatin%20remodeling%20complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Zhenlin%22%2C%22lastName%22%3A%22Yang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Amel%22%2C%22lastName%22%3A%22Mameri%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Claudia%22%2C%22lastName%22%3A%22Cattoglio%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Catherine%22%2C%22lastName%22%3A%22Lachance%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alfredo%20Jose%22%2C%22lastName%22%3A%22Florez%20Ariza%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jonathan%22%2C%22lastName%22%3A%22Humbert%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Deepthi%22%2C%22lastName%22%3A%22Sudarshan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arul%22%2C%22lastName%22%3A%22Banerjea%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Maxime%22%2C%22lastName%22%3A%22Galloy%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Am%5Cu00e9lie%22%2C%22lastName%22%3A%22Fradet-Turcotte%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jean-Philippe%22%2C%22lastName%22%3A%22Lambert%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jacques%22%2C%22lastName%22%3A%22C%5Cu00f4t%5Cu00e9%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Eva%22%2C%22lastName%22%3A%22Nogales%22%7D%5D%2C%22abstractNote%22%3A%22The%20human%20NuA4%5C%2FTIP60%20co-activator%20complex%2C%20a%20fusion%20of%20the%20yeast%20SWR1%20and%20NuA4%20complexes%2C%20both%20incorporates%20the%20histone%20variant%20H2A.Z%20into%20nucleosomes%20and%20acetylates%20histones%20H4%5C%2FH2A%5C%2FH2A.Z%20to%20regulate%20gene%20expression%20and%20maintain%20genome%20stability.%20Our%20cryo-electron%20microscopy%20studies%20show%20that%2C%20within%20the%20NuA4%5C%2FTIP60%20complex%2C%20the%20EP400%20subunit%20serves%20as%20a%20scaffold%20holding%20the%20different%20functional%20modules%20in%20specific%20positions%2C%20creating%20a%20unique%20arrangement%20of%20the%20ARP%20module.%20EP400%20interacts%20with%20the%20TRRAP%20subunit%20using%20a%20footprint%20that%20overlaps%20with%20that%20of%20the%20SAGA%20acetyltransferase%20complex%2C%20preventing%20the%20formation%20of%20a%20hybrid%20complex.%20Loss%20of%20the%20TRRAP%20subunit%20leads%20to%20mislocalization%20of%20NuA4%5C%2FTIP60%2C%20resulting%20in%20the%20redistribution%20of%20H2A.Z%20and%20its%20acetylation%20across%20the%20genome%2C%20emphasizing%20the%20dual%20functionality%20of%20NuA4%5C%2FTIP60%20as%20a%20single%20macromolecular%20assembly.%22%2C%22date%22%3A%222024%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1126%5C%2Fscience.adl5816%22%2C%22ISSN%22%3A%221095-9203%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-08-12T18%3A02%3A59Z%22%7D%7D%2C%7B%22key%22%3A%22RFXK8S4J%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Saha%20et%20al.%22%2C%22parsedDate%22%3A%222023%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ESaha%2C%20D.%2C%20Hailu%2C%20S.%2C%20Hada%2C%20A.%2C%20Lee%2C%20J.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%20A.%2C%20Lin%2C%20Y.-C.%2C%20Feola%2C%20K.%2C%20Persinger%2C%20J.%2C%20Jain%2C%20A.%2C%20Liu%2C%20B.%2C%20Lu%2C%20Y.%2C%20Sen%2C%20P.%2C%20%26amp%3B%20Bartholomew%2C%20B.%20%282023%29.%20The%20AT-hook%20is%20an%20evolutionarily%20conserved%20auto-regulatory%20domain%20of%20SWI%5C%2FSNF%20required%20for%20cell%20lineage%20priming.%20%3Ci%3ENature%20Communications%3C%5C%2Fi%3E%2C%20%3Ci%3E14%3C%5C%2Fi%3E%281%29%2C%204682.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-023-40386-8%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-023-40386-8%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DRFXK8S4J%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3D6EVQM65M%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20AT-hook%20is%20an%20evolutionarily%20conserved%20auto-regulatory%20domain%20of%20SWI%5C%2FSNF%20required%20for%20cell%20lineage%20priming%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dhurjhoti%22%2C%22lastName%22%3A%22Saha%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Solomon%22%2C%22lastName%22%3A%22Hailu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arjan%22%2C%22lastName%22%3A%22Hada%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Junwoo%22%2C%22lastName%22%3A%22Lee%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuan-Chi%22%2C%22lastName%22%3A%22Lin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kyle%22%2C%22lastName%22%3A%22Feola%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jim%22%2C%22lastName%22%3A%22Persinger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Abhinav%22%2C%22lastName%22%3A%22Jain%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Bin%22%2C%22lastName%22%3A%22Liu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yue%22%2C%22lastName%22%3A%22Lu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Payel%22%2C%22lastName%22%3A%22Sen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Blaine%22%2C%22lastName%22%3A%22Bartholomew%22%7D%5D%2C%22abstractNote%22%3A%22The%20SWI%5C%2FSNF%20ATP-dependent%20chromatin%20remodeler%20is%20a%20master%20regulator%20of%20the%20epigenome%2C%20controlling%20pluripotency%20and%20differentiation.%20Towards%20the%20C-terminus%20of%20the%20catalytic%20subunit%20of%20SWI%5C%2FSNF%20is%20a%20motif%20called%20the%20AT-hook%20that%20is%20evolutionary%20conserved.%20The%20AT-hook%20is%20present%20in%20many%20chromatin%20modifiers%20and%20generally%20thought%20to%20help%20anchor%20them%20to%20DNA.%20We%20observe%20however%20that%20the%20AT-hook%20regulates%20the%20intrinsic%20DNA-stimulated%20ATPase%20activity%20aside%20from%20promoting%20SWI%5C%2FSNF%20recruitment%20to%20DNA%20or%20nucleosomes%20by%20increasing%20the%20reaction%20velocity%20a%20factor%20of%2013%20with%20no%20accompanying%20change%20in%20substrate%20affinity%20%28KM%29.%20The%20changes%20in%20ATP%20hydrolysis%20causes%20an%20equivalent%20change%20in%20nucleosome%20movement%2C%20confirming%20they%20are%20tightly%20coupled.%20The%20catalytic%20subunit%27s%20AT-hook%20is%20required%20in%20vivo%20for%20SWI%5C%2FSNF%20remodeling%20activity%20in%20yeast%20and%20mouse%20embryonic%20stem%20cells.%20The%20AT-hook%20in%20SWI%5C%2FSNF%20is%20required%20for%20transcription%20regulation%20and%20activation%20of%20stage-specific%20enhancers%20critical%20in%20cell%20lineage%20priming.%20Similarly%2C%20growth%20assays%20suggest%20the%20AT-hook%20is%20required%20in%20yeast%20SWI%5C%2FSNF%20for%20activation%20of%20genes%20involved%20in%20amino%20acid%20biosynthesis%20and%20metabolizing%20ethanol.%20Our%20findings%20highlight%20the%20importance%20of%20studying%20SWI%5C%2FSNF%20attenuation%20versus%20eliminating%20the%20catalytic%20subunit%20or%20completely%20shutting%20down%20its%20enzymatic%20activity.%22%2C%22date%22%3A%222023%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fs41467-023-40386-8%22%2C%22ISSN%22%3A%222041-1723%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222023-10-24T15%3A47%3A06Z%22%7D%7D%2C%7B%22key%22%3A%22SP6M3L8T%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Luo%20and%20Ranish%22%2C%22parsedDate%22%3A%222022%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELuo%2C%20J.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282022%29.%20%3Ci%3EIsobaric%20crosslinking%20mass%20spectrometry%20technology%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20complexes%3C%5C%2Fi%3E.%20bioRxiv.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1101%5C%2F2022.12.02.518925%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1101%5C%2F2022.12.02.518925%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DSP6M3L8T%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DILNX64ZS%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22preprint%22%2C%22title%22%3A%22Isobaric%20crosslinking%20mass%20spectrometry%20technology%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20complexes%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Dynamic%20conformational%20and%20structural%20changes%20in%20proteins%20and%20protein%20complexes%20play%20a%20central%20and%20ubiquitous%20role%20in%20the%20regulation%20of%20protein%20function%2C%20yet%20it%20is%20very%20challenging%20to%20study%20these%20changes%2C%20especially%20for%20large%20protein%20complexes%2C%20under%20physiological%20conditions.%20Here%20we%20introduce%20a%20novel%20isobaric%20crosslinker%2C%20Qlinker%2C%20for%20studying%20conformational%20and%20structural%20changes%20in%20proteins%20and%20protein%20complexes%20using%20quantitative%20crosslinking%20mass%20spectrometry%20%28qCLMS%29.%20Qlinkers%20are%20small%20and%20simple%2C%20amine-reactive%20molecules%20with%20an%20optimal%20extended%20distance%20of%20%5Cu223c10%20%5Cu00c5%20and%20use%20MS2%20reporter%20ions%20for%20relative%20quantification%20of%20Qlinker-modified%20peptides.%20We%20synthesized%20the%202-plex%20Q2linker%20and%20showed%20that%20the%20Q2linker%20can%20provide%20quantitative%20crosslinking%20data%20that%20pinpoints%20the%20key%20conformational%20and%20structural%20changes%20in%20biosensors%20and%20the%20RNA%20polymerase%20II%20%28pol%20II%29%20complex.%22%2C%22genre%22%3A%22%22%2C%22repository%22%3A%22bioRxiv%22%2C%22archiveID%22%3A%22%22%2C%22date%22%3A%222022%22%2C%22DOI%22%3A%2210.1101%5C%2F2022.12.02.518925%22%2C%22citationKey%22%3A%22%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.biorxiv.org%5C%2Fcontent%5C%2F10.1101%5C%2F2022.12.02.518925v1%22%2C%22language%22%3A%22en%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222023-01-18T22%3A27%3A29Z%22%7D%7D%2C%7B%22key%22%3A%22ZUBGWGXR%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Bassett%20et%20al.%22%2C%22parsedDate%22%3A%222022%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EBassett%2C%20J.%2C%20Rimel%2C%20J.%20K.%2C%20Basu%2C%20S.%2C%20Basnet%2C%20P.%2C%20Luo%2C%20J.%2C%20Engel%2C%20K.%20L.%2C%20Nagel%2C%20M.%2C%20Woyciehowsky%2C%20A.%2C%20Ebmeier%2C%20C.%20C.%2C%20Kaplan%2C%20C.%20D.%2C%20Taatjes%2C%20D.%20J.%2C%20%26amp%3B%20Ranish%2C%20J.%20A.%20%282022%29.%20Systematic%20mutagenesis%20of%20TFIIH%20subunit%20p52%5C%2FTfb2%20identifies%20residues%20required%20for%20XPB%5C%2FSsl2%20subunit%20function%20and%20genetic%20interactions%20with%20TFB6.%20%3Ci%3EThe%20Journal%20of%20Biological%20Chemistry%3C%5C%2Fi%3E%2C%20%3Ci%3E298%3C%5C%2Fi%3E%2810%29%2C%20102433.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jbc.2022.102433%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jbc.2022.102433%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DZUBGWGXR%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DSUD9V59U%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Systematic%20mutagenesis%20of%20TFIIH%20subunit%20p52%5C%2FTfb2%20identifies%20residues%20required%20for%20XPB%5C%2FSsl2%20subunit%20function%20and%20genetic%20interactions%20with%20TFB6%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jacob%22%2C%22lastName%22%3A%22Bassett%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jenna%20K.%22%2C%22lastName%22%3A%22Rimel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shrabani%22%2C%22lastName%22%3A%22Basu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Pratik%22%2C%22lastName%22%3A%22Basnet%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Krysta%20L.%22%2C%22lastName%22%3A%22Engel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Michael%22%2C%22lastName%22%3A%22Nagel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexander%22%2C%22lastName%22%3A%22Woyciehowsky%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christopher%20C.%22%2C%22lastName%22%3A%22Ebmeier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Craig%20D.%22%2C%22lastName%22%3A%22Kaplan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dylan%20J.%22%2C%22lastName%22%3A%22Taatjes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22TFIIH%20is%20an%20evolutionarily%20conserved%20complex%20that%20plays%20central%20roles%20in%20both%20RNA%20polymerase%20II%20%28pol%20II%29%20transcription%20and%20DNA%20repair.%20As%20an%20integral%20component%20of%20the%20pol%20II%20preinitiation%20complex%2C%20TFIIH%20regulates%20pol%20II%20enzyme%20activity%20in%5Cu00a0numerous%20ways.%20The%20TFIIH%20subunit%20XPB%5C%2FSsl2%20is%20an%20ATP-dependent%20DNA%20translocase%20that%20stimulates%20promoter%20opening%20prior%20to%20transcription%20initiation.%20Crosslinking-mass%20spectrometry%20and%20cryo-EM%20results%20have%20shown%20a%20conserved%20interaction%20network%20involving%20XPB%5C%2FSsl2%20and%20the%20C-terminal%20Hub%20region%20of%20the%20TFIIH%20p52%5C%2FTfb2%20subunit%2C%20but%20the%20functional%20significance%20of%20specific%20residues%20is%20unclear.%20Here%2C%20we%20systematically%20mutagenized%20the%20HubA%20region%20of%20Tfb2%20and%20screened%20for%20growth%20phenotypes%20in%20a%20TFB6%20deletion%20background%20in%20Saccharomyces%20cerevisiae.%20We%20identified%20six%20lethal%20and%2012%20conditional%20mutants.%20Slow%20growth%20phenotypes%20of%20all%20but%20three%20conditional%20mutants%20were%20relieved%20in%20the%20presence%20of%20TFB6%2C%20thus%20identifying%20a%20functional%20interaction%20between%20Tfb2%20HubA%20mutants%20and%20Tfb6%2C%20a%20protein%20that%20dissociates%20Ssl2%20from%20TFIIH.%20Our%20biochemical%20analysis%20of%20Tfb2%20mutants%20with%20severe%20growth%20phenotypes%20revealed%20defects%20in%20Ssl2%20association%2C%20with%20similar%20results%20in%20human%20cells.%20Further%20characterization%20of%20these%20tfb2%20mutant%20cells%20revealed%20defects%20in%20GAL%20gene%20induction%2C%20and%20reduced%20occupancy%20of%20TFIIH%20and%20pol%20II%20at%20GAL%20gene%20promoters%2C%20suggesting%20that%20functionally%20competent%20TFIIH%20is%20required%20for%20proper%20pol%20II%20recruitment%20to%20preinitiation%20complexes%20in%5Cu00a0vivo.%20Consistent%20with%20recent%20structural%20models%20of%20TFIIH%2C%20our%20results%20identify%20key%20residues%20in%20the%20p52%5C%2FTfb2%20HubA%20domain%20that%20are%20required%20for%20stable%20incorporation%20of%20XPB%5C%2FSsl2%20into%20TFIIH%20and%20for%20pol%20II%20transcription.%22%2C%22date%22%3A%222022%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.jbc.2022.102433%22%2C%22ISSN%22%3A%221083-351X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222022-12-07T00%3A05%3A49Z%22%7D%7D%2C%7B%22key%22%3A%22K97PBNIT%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Danileviciute%20et%20al.%22%2C%22parsedDate%22%3A%222022%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EDanileviciute%2C%20E.%2C%20Zeng%2C%20N.%2C%20Capelle%2C%20C.%20M.%2C%20Paczia%2C%20N.%2C%20Gillespie%2C%20M.%20A.%2C%20Kurniawan%2C%20H.%2C%20Benzarti%2C%20M.%2C%20Merz%2C%20M.%20P.%2C%20Coowar%2C%20D.%2C%20Fritah%2C%20S.%2C%20Vogt%20Weisenhorn%2C%20D.%20M.%2C%20Gomez%20Giro%2C%20G.%2C%20Grusdat%2C%20M.%2C%20Baron%2C%20A.%2C%20Guerin%2C%20C.%2C%20Franchina%2C%20D.%20G.%2C%20L%26%23xE9%3Bonard%2C%20C.%2C%20Domingues%2C%20O.%2C%20Delhalle%2C%20S.%2C%20%26%23x2026%3B%20Hefeng%2C%20F.%20Q.%20%282022%29.%20PARK7%5C%2FDJ-1%20promotes%20pyruvate%20dehydrogenase%20activity%20and%20maintains%20Treg%20homeostasis%20during%20ageing.%20%3Ci%3ENature%20Metabolism%3C%5C%2Fi%3E%2C%20%3Ci%3E4%3C%5C%2Fi%3E%285%29%2C%20589%26%23x2013%3B607.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs42255-022-00576-y%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs42255-022-00576-y%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DK97PBNIT%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22PARK7%5C%2FDJ-1%20promotes%20pyruvate%20dehydrogenase%20activity%20and%20maintains%20Treg%20homeostasis%20during%20ageing%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Egle%22%2C%22lastName%22%3A%22Danileviciute%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ni%22%2C%22lastName%22%3A%22Zeng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%20M.%22%2C%22lastName%22%3A%22Capelle%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nicole%22%2C%22lastName%22%3A%22Paczia%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Henry%22%2C%22lastName%22%3A%22Kurniawan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mohaned%22%2C%22lastName%22%3A%22Benzarti%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Myriam%20P.%22%2C%22lastName%22%3A%22Merz%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Djalil%22%2C%22lastName%22%3A%22Coowar%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sabrina%22%2C%22lastName%22%3A%22Fritah%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniela%20Maria%22%2C%22lastName%22%3A%22Vogt%20Weisenhorn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Gemma%22%2C%22lastName%22%3A%22Gomez%20Giro%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Melanie%22%2C%22lastName%22%3A%22Grusdat%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexandre%22%2C%22lastName%22%3A%22Baron%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Coralie%22%2C%22lastName%22%3A%22Guerin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Davide%20G.%22%2C%22lastName%22%3A%22Franchina%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cathy%22%2C%22lastName%22%3A%22L%5Cu00e9onard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Olivia%22%2C%22lastName%22%3A%22Domingues%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sylvie%22%2C%22lastName%22%3A%22Delhalle%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Wolfgang%22%2C%22lastName%22%3A%22Wurst%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jonathan%20D.%22%2C%22lastName%22%3A%22Turner%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jens%20Christian%22%2C%22lastName%22%3A%22Schwamborn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Johannes%22%2C%22lastName%22%3A%22Meiser%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rejko%22%2C%22lastName%22%3A%22Kr%5Cu00fcger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dirk%22%2C%22lastName%22%3A%22Brenner%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Carole%20L.%22%2C%22lastName%22%3A%22Linster%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rudi%22%2C%22lastName%22%3A%22Balling%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Markus%22%2C%22lastName%22%3A%22Ollert%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Feng%20Q.%22%2C%22lastName%22%3A%22Hefeng%22%7D%5D%2C%22abstractNote%22%3A%22Pyruvate%20dehydrogenase%20%28PDH%29%20is%20the%20gatekeeper%20enzyme%20of%20the%20tricarboxylic%20acid%20%28TCA%29%20cycle.%20Here%20we%20show%20that%20the%20deglycase%20DJ-1%20%28encoded%20by%20PARK7%2C%20a%20key%20familial%20Parkinson%27s%20disease%20gene%29%20is%20a%20pacemaker%20regulating%20PDH%20activity%20in%20CD4%2B%20regulatory%20T%20cells%20%28Treg%20cells%29.%20DJ-1%20binds%20to%20PDHE1-%5Cu03b2%20%28PDHB%29%2C%20inhibiting%20phosphorylation%20of%20PDHE1-%5Cu03b1%20%28PDHA%29%2C%20thus%20promoting%20PDH%20activity%20and%20oxidative%20phosphorylation%20%28OXPHOS%29.%20Park7%20%28Dj-1%29%20deletion%20impairs%20Treg%20survival%20starting%20in%20young%20mice%20and%20reduces%20Treg%20homeostatic%20proliferation%20and%20cellularity%20only%20in%20aged%20mice.%20This%20leads%20to%20increased%20severity%20in%20aged%20mice%20during%20the%20remission%20of%20experimental%20autoimmune%20encephalomyelitis%20%28EAE%29.%20Dj-1%20deletion%20also%20compromises%20differentiation%20of%20inducible%20Treg%20cells%20especially%20in%20aged%20mice%2C%20and%20the%20impairment%20occurs%20via%20regulation%20of%20PDHB.%20These%20findings%20provide%20unforeseen%20insight%20into%20the%20complicated%20regulatory%20machinery%20of%20the%20PDH%20complex.%20As%20Treg%20homeostasis%20is%20dysregulated%20in%20many%20complex%20diseases%2C%20the%20DJ-1-PDHB%20axis%20represents%20a%20potential%20target%20to%20maintain%20or%20re-establish%20Treg%20homeostasis.%22%2C%22date%22%3A%222022%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fs42255-022-00576-y%22%2C%22ISSN%22%3A%222522-5812%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222022-07-05T18%3A07%3A22Z%22%7D%7D%2C%7B%22key%22%3A%22YGR959FT%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Scheer%20et%20al.%22%2C%22parsedDate%22%3A%222021%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EScheer%2C%20E.%2C%20Luo%2C%20J.%2C%20Bernardini%2C%20A.%2C%20Ruffenach%2C%20F.%2C%20Garnier%2C%20J.-M.%2C%20Kolb-Cheynel%2C%20I.%2C%20Gupta%2C%20K.%2C%20Berger%2C%20I.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Tora%2C%20L.%20%282021%29.%20TAF8%20regions%20important%20for%20TFIID%20lobe%20B%20assembly%20or%20for%20TAF2%20interactions%20are%20required%20for%20embryonic%20stem%20cell%20survival.%20%3Ci%3EThe%20Journal%20of%20Biological%20Chemistry%3C%5C%2Fi%3E%2C%20101288.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jbc.2021.101288%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jbc.2021.101288%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DYGR959FT%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22TAF8%20regions%20important%20for%20TFIID%20lobe%20B%20assembly%20or%20for%20TAF2%20interactions%20are%20required%20for%20embryonic%20stem%20cell%20survival%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Elisabeth%22%2C%22lastName%22%3A%22Scheer%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrea%22%2C%22lastName%22%3A%22Bernardini%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Frank%22%2C%22lastName%22%3A%22Ruffenach%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jean-Marie%22%2C%22lastName%22%3A%22Garnier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%22%2C%22lastName%22%3A%22Kolb-Cheynel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kapil%22%2C%22lastName%22%3A%22Gupta%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Imre%22%2C%22lastName%22%3A%22Berger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22L%5Cu00e1szl%5Cu00f3%22%2C%22lastName%22%3A%22Tora%22%7D%5D%2C%22abstractNote%22%3A%22The%20human%20general%20transcription%20factor%20TFIID%20is%20composed%20of%20the%20TATA-binding%20protein%20%28TBP%29%20and%2013%20TBP-associated%20factors%20%28TAFs%29.%20In%20eukaryotic%20cells%2C%20TFIID%20is%20thought%20to%20nucleate%20RNA%20polymerase%20II%20%28Pol%20II%29%20preinitiation%20complex%20formation%20on%20all%20protein%20coding%20gene%20promoters%20and%20thus%2C%20be%20crucial%20for%20Pol%20II%20transcription.%20TFIID%20is%20composed%20of%20three%20lobes%2C%20named%20A%2C%20B%20and%20C.%20A%205TAF%20core%20complex%20can%20be%20assembled%20in%20vitro%20constituting%20a%20building%20block%20for%20the%20further%20assembly%20of%20either%20lobe%20A%20or%20B%20in%20TFIID.%20Structural%20studies%20showed%20that%20TAF8%20forms%20a%20histone%20fold%20pair%20with%20TAF10%20in%20lobe%20B%20and%20participates%20in%20connecting%20lobe%20B%20to%20lobe%20C.%20To%20better%20understand%20the%20role%20of%20TAF8%20in%20TFIID%2C%20we%20have%20investigated%20the%20requirement%20of%20the%20different%20regions%20of%20TAF8%20for%20the%20in%20vitro%20assembly%20of%20lobe%20B%20and%20C%2C%20and%20the%20importance%20of%20certain%20TAF8%20regions%20for%20mouse%20embryonic%20stem%20cell%20%28ESC%29%20viability.%20We%20have%20identified%20a%20region%20of%20TAF8%20distinct%20from%20the%20histone%20fold%20domain%20important%20for%20assembling%20with%20the%205TAF%20core%20complex%20in%20lobe%20B.%20We%20also%20delineated%20four%20more%20regions%20of%20TAF8%20each%20individually%20required%20for%20interacting%20with%20TAF2%20in%20lobe%20C.%20Moreover%2C%20CRISPR%5C%2FCas9-mediated%20gene%20editing%20indicated%20that%20the%205TAF%20core-interacting%20TAF8%20domain%20and%20the%20proline-rich%20domain%20of%20TAF8%20that%20interacts%20with%20TAF2%20are%20both%20required%20for%20mouse%20embryonic%20stem%20cell%20survival.%20Thus%2C%20our%20study%20defines%20distinct%20TAF8%20regions%20involved%20in%20connecting%20TFIID%20lobe%20B%20to%20lobe%20C%20that%20appear%20crucial%20for%20TFIID%20function%20and%20consequent%20ESC%20survival.%22%2C%22date%22%3A%222021%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.jbc.2021.101288%22%2C%22ISSN%22%3A%221083-351X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222021-10-14T23%3A34%3A19Z%22%7D%7D%2C%7B%22key%22%3A%22NHEPRX4Q%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Brand%20and%20Ranish%22%2C%22parsedDate%22%3A%222021%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EBrand%2C%20M.%2C%20%26amp%3B%20Ranish%2C%20J.%20A.%20%282021%29.%20Proteomic%5C%2Ftranscriptomic%20analysis%20of%20erythropoiesis.%20%3Ci%3ECurrent%20Opinion%20in%20Hematology%3C%5C%2Fi%3E%2C%20%3Ci%3E28%3C%5C%2Fi%3E%283%29%2C%20150%26%23x2013%3B157.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1097%5C%2FMOH.0000000000000647%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1097%5C%2FMOH.0000000000000647%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DNHEPRX4Q%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Proteomic%5C%2Ftranscriptomic%20analysis%20of%20erythropoiesis%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marjorie%22%2C%22lastName%22%3A%22Brand%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22PURPOSE%20OF%20REVIEW%3A%20Erythropoiesis%20is%20a%20hierarchical%20process%20by%20which%20hematopoietic%20stem%20cells%20give%20rise%20to%20red%20blood%20cells%20through%20gradual%20cell%20fate%20restriction%20and%20maturation.%20Deciphering%20this%20process%20requires%20the%20establishment%20of%20dynamic%20gene%20regulatory%20networks%20%28GRNs%29%20that%20predict%20the%20response%20of%20hematopoietic%20cells%20to%20signals%20from%20the%20environment.%20Although%20GRNs%20have%20historically%20been%20derived%20from%20transcriptomic%20data%2C%20recent%20proteomic%20studies%20have%20revealed%20a%20major%20role%20for%20posttranscriptional%20mechanisms%20in%20regulating%20gene%20expression%20during%20erythropoiesis.%20These%20new%20findings%20highlight%20the%20need%20to%20integrate%20proteomic%20data%20into%20GRNs%20for%20a%20refined%20understanding%20of%20erythropoiesis.%5CnRECENT%20FINDINGS%3A%20Here%2C%20we%20review%20recent%20proteomic%20studies%20that%20have%20furthered%20our%20understanding%20of%20erythropoiesis%20with%20a%20focus%20on%20quantitative%20mass%20spectrometry%20approaches%20to%20measure%20the%20abundance%20of%20transcription%20factors%20and%20cofactors%20during%20differentiation.%20Furthermore%2C%20we%20highlight%20challenges%20that%20remain%20in%20integrating%20transcriptomic%2C%20proteomic%2C%20and%20other%20omics%20data%20into%20a%20predictive%20model%20of%20erythropoiesis%2C%20and%20discuss%20the%20future%20prospect%20of%20single-cell%20proteomics.%5CnSUMMARY%3A%20Recent%20proteomic%20studies%20have%20considerably%20expanded%20our%20knowledge%20of%20erythropoiesis%20beyond%20the%20traditional%20transcriptomic-centric%20perspective.%20These%20findings%20have%20both%20opened%20up%20new%20avenues%20of%20research%20to%20increase%20our%20understanding%20of%20erythroid%20differentiation%2C%20while%20at%20the%20same%20time%20presenting%20new%20challenges%20in%20integrating%20multiple%20layers%20of%20information%20into%20a%20comprehensive%20gene%20regulatory%20model.%22%2C%22date%22%3A%222021%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1097%5C%2FMOH.0000000000000647%22%2C%22ISSN%22%3A%221531-7048%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222021-06-04T19%3A17%3A10Z%22%7D%7D%2C%7B%22key%22%3A%226UR4CYCM%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Jensen%20et%20al.%22%2C%22parsedDate%22%3A%222021%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EJensen%2C%20B.%20C.%2C%20Phan%2C%20I.%20Q.%2C%20McDonald%2C%20J.%20R.%2C%20Sur%2C%20A.%2C%20Gillespie%2C%20M.%20A.%2C%20Ranish%2C%20J.%20A.%2C%20Parsons%2C%20M.%2C%20%26amp%3B%20Myler%2C%20P.%20J.%20%282021%29.%20Chromatin-Associated%20Protein%20Complexes%20Link%20DNA%20Base%20J%20and%20Transcription%20Termination%20in%20Leishmania.%20%3Ci%3EMSphere%3C%5C%2Fi%3E%2C%20%3Ci%3E6%3C%5C%2Fi%3E%281%29.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FmSphere.01204-20%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FmSphere.01204-20%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D6UR4CYCM%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Chromatin-Associated%20Protein%20Complexes%20Link%20DNA%20Base%20J%20and%20Transcription%20Termination%20in%20Leishmania%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Bryan%20C.%22%2C%22lastName%22%3A%22Jensen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%20Q.%22%2C%22lastName%22%3A%22Phan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jacquelyn%20R.%22%2C%22lastName%22%3A%22McDonald%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Aakash%22%2C%22lastName%22%3A%22Sur%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marilyn%22%2C%22lastName%22%3A%22Parsons%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Peter%20J.%22%2C%22lastName%22%3A%22Myler%22%7D%5D%2C%22abstractNote%22%3A%22Unlike%20most%20other%20eukaryotes%2C%20Leishmania%20and%20other%20trypanosomatid%20protozoa%20have%20largely%20eschewed%20transcriptional%20control%20of%20gene%20expression%2C%20relying%20instead%20on%20posttranscriptional%20regulation%20of%20mRNAs%20derived%20from%20polycistronic%20transcription%20units%20%28PTUs%29.%20In%20these%20parasites%2C%20a%20novel%20modified%20nucleotide%20base%20%28%5Cu03b2-d-glucopyranosyloxymethyluracil%29%20known%20as%20J%20plays%20a%20critical%20role%20in%20ensuring%20that%20transcription%20termination%20occurs%20only%20at%20the%20end%20of%20each%20PTU%2C%20rather%20than%20at%20the%20polyadenylation%20sites%20of%20individual%20genes.%20To%20further%20understand%20the%20biology%20of%20J-associated%20processes%2C%20we%20used%20tandem%20affinity%20purification%20%28TAP%29%20tagging%20and%20mass%20spectrometry%20to%20reveal%20proteins%20that%20interact%20with%20the%20glucosyltransferase%20performing%20the%20final%20step%20in%20J%20synthesis.%20These%20studies%20identified%20four%20proteins%20reminiscent%20of%20subunits%20in%20the%20PTW%5C%2FPP1%20complex%20that%20controls%20transcription%20termination%20in%20higher%20eukaryotes.%20Moreover%2C%20bioinformatic%20analyses%20identified%20the%20DNA-binding%20subunit%20of%20Leishmania%20PTW%5C%2FPP1%20as%20a%20novel%20J-binding%20protein%20%28JBP3%29%2C%20which%20is%20also%20part%20of%20another%20complex%20containing%20proteins%20with%20domains%20suggestive%20of%20a%20role%20in%20chromatin%20modification%5C%2Fremodeling.%20Additionally%2C%20JBP3%20associates%20%28albeit%20transiently%20and%5C%2For%20indirectly%29%20with%20the%20trypanosomatid%20equivalent%20of%20the%20PAF1%20complex%20involved%20in%20the%20regulation%20of%20transcription%20in%20other%20eukaryotes.%20The%20downregulation%20of%20JBP3%20expression%20levels%20in%20Leishmania%20resulted%20in%20a%20substantial%20increase%20in%20transcriptional%20readthrough%20at%20the%203%27%20end%20of%20most%20PTUs.%20We%20propose%20that%20JBP3%20recruits%20one%20or%20more%20of%20these%20complexes%20to%20the%20J-containing%20regions%20at%20the%20end%20of%20PTUs%2C%20where%20they%20halt%20the%20progression%20of%20the%20RNA%20polymerase.%20This%20decoupling%20of%20transcription%20termination%20from%20the%20splicing%20of%20individual%20genes%20enables%20the%20parasites%27%20unique%20reliance%20on%20polycistronic%20transcription%20and%20posttranscriptional%20regulation%20of%20gene%20expression.IMPORTANCELeishmania%20parasites%20cause%20a%20variety%20of%20serious%20human%20diseases%2C%20with%20no%20effective%20vaccine%20and%20emerging%20resistance%20to%20current%20drug%20therapy.%20We%20have%20previously%20shown%20that%20a%20novel%20DNA%20base%20called%20J%20is%20critical%20for%20transcription%20termination%20at%20the%20ends%20of%20the%20polycistronic%20gene%20clusters%20that%20are%20a%20hallmark%20of%20Leishmania%20and%20related%20trypanosomatids.%20Here%2C%20we%20describe%20a%20new%20J-binding%20protein%20%28JBP3%29%20associated%20with%20three%20different%20protein%20complexes%20that%20are%20reminiscent%20of%20those%20involved%20in%20the%20control%20of%20transcription%20in%20other%20eukaryotes.%20However%2C%20the%20parasite%20complexes%20have%20been%20reprogrammed%20to%20regulate%20transcription%20and%20gene%20expression%20in%20trypanosomatids%20differently%20than%20in%20the%20mammalian%20hosts%2C%20providing%20new%20opportunities%20to%20develop%20novel%20chemotherapeutic%20treatments%20against%20these%20important%20pathogens.%22%2C%22date%22%3A%222021%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1128%5C%2FmSphere.01204-20%22%2C%22ISSN%22%3A%222379-5042%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222021-03-05T20%3A21%3A31Z%22%7D%7D%2C%7B%22key%22%3A%22XEB92V5R%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kim%20et%20al.%22%2C%22parsedDate%22%3A%222020%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKim%2C%20M.%20K.%2C%20Tranvo%2C%20A.%2C%20Hurlburt%2C%20A.%20M.%2C%20Verma%2C%20N.%2C%20Phan%2C%20P.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Stumph%2C%20W.%20E.%20%282020%29.%20Assembly%20of%20SNAPc%2C%20Bdp1%2C%20and%20TBP%20on%20the%20U6%20snRNA%20Gene%20Promoter%20in%20Drosophila%20melanogaster.%20%3Ci%3EMolecular%20and%20Cellular%20Biology%3C%5C%2Fi%3E%2C%20%3Ci%3E40%3C%5C%2Fi%3E%2812%29.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00641-19%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00641-19%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DXEB92V5R%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Assembly%20of%20SNAPc%2C%20Bdp1%2C%20and%20TBP%20on%20the%20U6%20snRNA%20Gene%20Promoter%20in%20Drosophila%20melanogaster%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mun%20Kyoung%22%2C%22lastName%22%3A%22Kim%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22An%22%2C%22lastName%22%3A%22Tranvo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ann%20Marie%22%2C%22lastName%22%3A%22Hurlburt%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Neha%22%2C%22lastName%22%3A%22Verma%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Phuc%22%2C%22lastName%22%3A%22Phan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22William%20E.%22%2C%22lastName%22%3A%22Stumph%22%7D%5D%2C%22abstractNote%22%3A%22U6%20snRNA%20is%20transcribed%20by%20RNA%20polymerase%20III%20%28Pol%20III%29%20and%20has%20an%20external%20upstream%20promoter%20that%20consists%20of%20a%20TATA%20sequence%20recognized%20by%20the%20TBP%20subunit%20of%20the%20Pol%20III%20basal%20transcription%20factor%20IIIB%20and%20a%20proximal%20sequence%20element%20%28PSE%29%20recognized%20by%20the%20small%20nuclear%20RNA%20activating%20protein%20complex%20%28SNAPc%29.%20Previously%2C%20we%20found%20that%20Drosophila%20melanogaster%20SNAPc%20%28DmSNAPc%29%20bound%20to%20the%20U6%20PSE%20can%20recruit%20the%20Pol%20III%20general%20transcription%20factor%20Bdp1%20to%20form%20a%20stable%20complex%20with%20the%20DNA.%20Here%2C%20we%20show%20that%20DmSNAPc-Bdp1%20can%20recruit%20TBP%20to%20the%20U6%20promoter%2C%20and%20we%20identify%20a%20region%20of%20Bdp1%20that%20is%20sufficient%20for%20TBP%20recruitment.%20Moreover%2C%20we%20find%20that%20this%20same%20region%20of%20Bdp1%20cross-links%20to%20nucleotides%20within%20the%20U6%20PSE%20at%20positions%20that%20also%20cross-link%20to%20DmSNAPc.%20Finally%2C%20cross-linking%20mass%20spectrometry%20reveals%20likely%20interactions%20of%20specific%20DmSNAPc%20subunits%20with%20Bdp1%20and%20TBP.%20These%20data%2C%20together%20with%20previous%20findings%2C%20have%20allowed%20us%20to%20build%20a%20more%20comprehensive%20model%20of%20the%20DmSNAPc-Bdp1-TBP%20complex%20on%20the%20U6%20promoter%20that%20includes%20nearly%20all%20of%20DmSNAPc%2C%20a%20portion%20of%20Bdp1%2C%20and%20the%20conserved%20region%20of%20TBP.%22%2C%22date%22%3A%2205%2028%2C%202020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1128%5C%2FMCB.00641-19%22%2C%22ISSN%22%3A%221098-5549%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-07-09T02%3A10%3A01Z%22%7D%7D%2C%7B%22key%22%3A%22M6DHB9YQ%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Gillespie%20et%20al.%22%2C%22parsedDate%22%3A%222020%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EGillespie%2C%20M.%20A.%2C%20Palii%2C%20C.%20G.%2C%20Sanchez-Taltavull%2C%20D.%2C%20Perkins%2C%20T.%20J.%2C%20Brand%2C%20M.%2C%20%26amp%3B%20Ranish%2C%20J.%20A.%20%282020%29.%20Absolute%20quantification%20of%20transcription%20factors%20in%20human%20erythropoiesis%20using%20selected%20reaction%20monitoring%20mass%20spectrometry.%20%3Ci%3ESTAR%20Protocols%3C%5C%2Fi%3E%2C%20%3Ci%3E1%3C%5C%2Fi%3E%283%29%2C%20100216.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.xpro.2020.100216%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.xpro.2020.100216%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DM6DHB9YQ%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Absolute%20quantification%20of%20transcription%20factors%20in%20human%20erythropoiesis%20using%20selected%20reaction%20monitoring%20mass%20spectrometry%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Carmen%20G.%22%2C%22lastName%22%3A%22Palii%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniel%22%2C%22lastName%22%3A%22Sanchez-Taltavull%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Theodore%20J.%22%2C%22lastName%22%3A%22Perkins%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marjorie%22%2C%22lastName%22%3A%22Brand%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Quantitative%20changes%20in%20transcription%20factor%20%28TF%29%20abundance%20regulate%20dynamic%20cellular%20processes%2C%20including%20cell%20fate%20decisions.%20Protein%20copy%20number%20provides%20information%20about%20the%20relative%20stoichiometry%20of%20TFs%20that%20can%20be%20used%20to%20determine%20how%20quantitative%20changes%20in%20TF%20abundance%20influence%20gene%20regulatory%20networks.%20In%20this%20protocol%2C%20we%20describe%20a%20targeted%20selected%20reaction%20monitoring%20%28SRM%29-based%20mass-spectrometry%20method%20to%20systematically%20measure%20the%20absolute%20protein%20concentration%20of%20nuclear%20TFs%20as%20human%20hematopoietic%20stem%20and%20progenitor%20cells%20differentiate%20along%20the%20erythropoietic%20lineage.%20For%20complete%20details%20on%20the%20use%20and%20execution%20of%20this%20protocol%2C%20please%20refer%20to%20Gillespie%20et%5Cu00a0al.%20%282020%29.%22%2C%22date%22%3A%222020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.xpro.2020.100216%22%2C%22ISSN%22%3A%222666-1667%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222021-01-04T19%3A37%3A25Z%22%7D%7D%2C%7B%22key%22%3A%22XNHICNBU%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wenderski%20et%20al.%22%2C%22parsedDate%22%3A%222020%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWenderski%2C%20W.%2C%20Wang%2C%20L.%2C%20Krokhotin%2C%20A.%2C%20Walsh%2C%20J.%20J.%2C%20Li%2C%20H.%2C%20Shoji%2C%20H.%2C%20Ghosh%2C%20S.%2C%20George%2C%20R.%20D.%2C%20Miller%2C%20E.%20L.%2C%20Elias%2C%20L.%2C%20Gillespie%2C%20M.%20A.%2C%20Son%2C%20E.%20Y.%2C%20Staahl%2C%20B.%20T.%2C%20Baek%2C%20S.%20T.%2C%20Stanley%2C%20V.%2C%20Moncada%2C%20C.%2C%20Shipony%2C%20Z.%2C%20Linker%2C%20S.%20B.%2C%20Marchetto%2C%20M.%20C.%20N.%2C%20%26%23x2026%3B%20Gleeson%2C%20J.%20G.%20%282020%29.%20Loss%20of%20the%20neural-specific%20BAF%20subunit%20ACTL6B%20relieves%20repression%20of%20early%20response%20genes%20and%20causes%20recessive%20autism.%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1908238117%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1908238117%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DXNHICNBU%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DXYJLU794%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Loss%20of%20the%20neural-specific%20BAF%20subunit%20ACTL6B%20relieves%20repression%20of%20early%20response%20genes%20and%20causes%20recessive%20autism%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Wendy%22%2C%22lastName%22%3A%22Wenderski%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Lu%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrey%22%2C%22lastName%22%3A%22Krokhotin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jessica%20J.%22%2C%22lastName%22%3A%22Walsh%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hongjie%22%2C%22lastName%22%3A%22Li%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hirotaka%22%2C%22lastName%22%3A%22Shoji%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shereen%22%2C%22lastName%22%3A%22Ghosh%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Renee%20D.%22%2C%22lastName%22%3A%22George%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Erik%20L.%22%2C%22lastName%22%3A%22Miller%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Laura%22%2C%22lastName%22%3A%22Elias%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Esther%20Y.%22%2C%22lastName%22%3A%22Son%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Brett%20T.%22%2C%22lastName%22%3A%22Staahl%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seung%20Tae%22%2C%22lastName%22%3A%22Baek%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Valentina%22%2C%22lastName%22%3A%22Stanley%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cynthia%22%2C%22lastName%22%3A%22Moncada%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Zohar%22%2C%22lastName%22%3A%22Shipony%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sara%20B.%22%2C%22lastName%22%3A%22Linker%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Maria%20C.%20N.%22%2C%22lastName%22%3A%22Marchetto%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Fred%20H.%22%2C%22lastName%22%3A%22Gage%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dillon%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Tipu%22%2C%22lastName%22%3A%22Sultan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Maha%20S.%22%2C%22lastName%22%3A%22Zaki%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Tsuyoshi%22%2C%22lastName%22%3A%22Miyakawa%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Liqun%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Robert%20C.%22%2C%22lastName%22%3A%22Malenka%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Gerald%20R.%22%2C%22lastName%22%3A%22Crabtree%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Joseph%20G.%22%2C%22lastName%22%3A%22Gleeson%22%7D%5D%2C%22abstractNote%22%3A%22Synaptic%20activity%20in%20neurons%20leads%20to%20the%20rapid%20activation%20of%20genes%20involved%20in%20mammalian%20behavior.%20ATP-dependent%20chromatin%20remodelers%20such%20as%20the%20BAF%20complex%20contribute%20to%20these%20responses%20and%20are%20generally%20thought%20to%20activate%20transcription.%20However%2C%20the%20mechanisms%20keeping%20such%20%5C%22early%20activation%5C%22%20genes%20silent%20have%20been%20a%20mystery.%20In%20the%20course%20of%20investigating%20Mendelian%20recessive%20autism%2C%20we%20identified%20six%20families%20with%20segregating%20loss-of-function%20mutations%20in%20the%20neuronal%20BAF%20%28nBAF%29%20subunit%20ACTL6B%20%28originally%20named%20BAF53b%29.%20Accordingly%2C%20ACTL6B%20was%20the%20most%20significantly%20mutated%20gene%20in%20the%20Simons%20Recessive%20Autism%20Cohort.%20At%20least%2014%20subunits%20of%20the%20nBAF%20complex%20are%20mutated%20in%20autism%2C%20collectively%20making%20it%20a%20major%20contributor%20to%20autism%20spectrum%20disorder%20%28ASD%29.%20Patient%20mutations%20destabilized%20ACTL6B%20protein%20in%20neurons%20and%20rerouted%20dendrites%20to%20the%20wrong%20glomerulus%20in%20the%20fly%20olfactory%20system.%20Humans%20and%20mice%20lacking%20ACTL6B%20showed%20corpus%20callosum%20hypoplasia%2C%20indicating%20a%20conserved%20role%20for%20ACTL6B%20in%20facilitating%20neural%20connectivity.%20Actl6b%20knockout%20mice%20on%20two%20genetic%20backgrounds%20exhibited%20ASD-related%20behaviors%2C%20including%20social%20and%20memory%20impairments%2C%20repetitive%20behaviors%2C%20and%20hyperactivity.%20Surprisingly%2C%20mutation%20of%20Actl6b%20relieved%20repression%20of%20early%20response%20genes%20including%20AP1%20transcription%20factors%20%28Fos%2C%20Fosl2%2C%20Fosb%2C%20and%20Junb%29%2C%20increased%20chromatin%20accessibility%20at%20AP1%20binding%20sites%2C%20and%20transcriptional%20changes%20in%20late%20response%20genes%20associated%20with%20early%20response%20transcription%20factor%20activity.%20ACTL6B%20loss%20is%20thus%20an%20important%20cause%20of%20recessive%20ASD%2C%20with%20impaired%20neuron-specific%20chromatin%20repression%20indicated%20as%20a%20potential%20mechanism.%22%2C%22date%22%3A%222020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1073%5C%2Fpnas.1908238117%22%2C%22ISSN%22%3A%221091-6490%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222020-11-18T18%3A21%3A53Z%22%7D%7D%2C%7B%22key%22%3A%22VHPX4KH8%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Gillespie%20et%20al.%22%2C%22parsedDate%22%3A%222020%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EGillespie%2C%20M.%20A.%2C%20Palii%2C%20C.%20G.%2C%20Sanchez-Taltavull%2C%20D.%2C%20Shannon%2C%20P.%2C%20Longabaugh%2C%20W.%20J.%20R.%2C%20Downes%2C%20D.%20J.%2C%20Sivaraman%2C%20K.%2C%20Espinoza%2C%20H.%20M.%2C%20Hughes%2C%20J.%20R.%2C%20Price%2C%20N.%20D.%2C%20Perkins%2C%20T.%20J.%2C%20Ranish%2C%20J.%20A.%2C%20%26amp%3B%20Brand%2C%20M.%20%282020%29.%20Absolute%20Quantification%20of%20Transcription%20Factors%20Reveals%20Principles%20of%20Gene%20Regulation%20in%20Erythropoiesis.%20%3Ci%3EMolecular%20Cell%3C%5C%2Fi%3E%2C%20%3Ci%3E78%3C%5C%2Fi%3E%285%29%2C%20960-974.e11.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.molcel.2020.03.031%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.molcel.2020.03.031%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DVHPX4KH8%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DW3R56RWP%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Absolute%20Quantification%20of%20Transcription%20Factors%20Reveals%20Principles%20of%20Gene%20Regulation%20in%20Erythropoiesis%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Carmen%20G.%22%2C%22lastName%22%3A%22Palii%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniel%22%2C%22lastName%22%3A%22Sanchez-Taltavull%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paul%22%2C%22lastName%22%3A%22Shannon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22William%20J.%20R.%22%2C%22lastName%22%3A%22Longabaugh%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Damien%20J.%22%2C%22lastName%22%3A%22Downes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Karthi%22%2C%22lastName%22%3A%22Sivaraman%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Herbert%20M.%22%2C%22lastName%22%3A%22Espinoza%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jim%20R.%22%2C%22lastName%22%3A%22Hughes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nathan%20D.%22%2C%22lastName%22%3A%22Price%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Theodore%20J.%22%2C%22lastName%22%3A%22Perkins%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marjorie%22%2C%22lastName%22%3A%22Brand%22%7D%5D%2C%22abstractNote%22%3A%22Dynamic%20cellular%20processes%20such%20as%20differentiation%20are%20driven%20by%20changes%20in%20the%20abundances%20of%20transcription%20factors%20%28TFs%29.%20However%2C%20despite%20years%20of%20studies%2C%20our%20knowledge%20about%20the%20protein%20copy%20number%20of%20TFs%20in%20the%20nucleus%20is%20limited.%20Here%2C%20by%20determining%20the%20absolute%20abundances%20of%20103%20TFs%20and%20co-factors%20during%20the%20course%20of%20human%20erythropoiesis%2C%20we%20provide%20a%20dynamic%20and%20quantitative%20scale%20for%20TFs%20in%20the%20nucleus.%20Furthermore%2C%20we%20establish%20the%20first%20gene%20regulatory%20network%20of%20cell%20fate%20commitment%20that%20integrates%20temporal%20protein%20stoichiometry%20data%20with%20mRNA%20measurements.%20The%20model%20revealed%20quantitative%20imbalances%20in%20TFs%27%20cross-antagonistic%20relationships%20that%20underlie%20lineage%20determination.%20Finally%2C%20we%20made%20the%20surprising%20discovery%20that%2C%20in%20the%20nucleus%2C%20co-repressors%20are%20dramatically%20more%20abundant%20than%20co-activators%20at%20the%20protein%20level%2C%20but%20not%20at%20the%20RNA%20level%2C%20with%20profound%20implications%20for%20understanding%20transcriptional%20regulation.%20These%20analyses%20provide%20a%20unique%20quantitative%20framework%20to%20understand%20transcriptional%20regulation%20of%20cell%20differentiation%20in%20a%20dynamic%20context.%22%2C%22date%22%3A%222020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.molcel.2020.03.031%22%2C%22ISSN%22%3A%221097-4164%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222020-11-18T18%3A18%3A16Z%22%7D%7D%2C%7B%22key%22%3A%222FQPB6CN%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Mashtalir%20et%20al.%22%2C%22parsedDate%22%3A%222020%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EMashtalir%2C%20N.%2C%20Suzuki%2C%20H.%2C%20Farrell%2C%20D.%20P.%2C%20Sankar%2C%20A.%2C%20Luo%2C%20J.%2C%20Filipovski%2C%20M.%2C%20D%26%23x2019%3BAvino%2C%20A.%20R.%2C%20St%20Pierre%2C%20R.%2C%20Valencia%2C%20A.%20M.%2C%20Onikubo%2C%20T.%2C%20Roeder%2C%20R.%20G.%2C%20Han%2C%20Y.%2C%20He%2C%20Y.%2C%20Ranish%2C%20J.%20A.%2C%20DiMaio%2C%20F.%2C%20Walz%2C%20T.%2C%20%26amp%3B%20Kadoch%2C%20C.%20%282020%29.%20A%20Structural%20Model%20of%20the%20Endogenous%20Human%20BAF%20Complex%20Informs%20Disease%20Mechanisms.%20%3Ci%3ECell%3C%5C%2Fi%3E%2C%20%3Ci%3E183%3C%5C%2Fi%3E%283%29%2C%20802-817.e24.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cell.2020.09.051%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cell.2020.09.051%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D2FQPB6CN%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22A%20Structural%20Model%20of%20the%20Endogenous%20Human%20BAF%20Complex%20Informs%20Disease%20Mechanisms%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nazar%22%2C%22lastName%22%3A%22Mashtalir%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hiroshi%22%2C%22lastName%22%3A%22Suzuki%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniel%20P.%22%2C%22lastName%22%3A%22Farrell%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Akshay%22%2C%22lastName%22%3A%22Sankar%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Martin%22%2C%22lastName%22%3A%22Filipovski%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrew%20R.%22%2C%22lastName%22%3A%22D%27Avino%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Roodolph%22%2C%22lastName%22%3A%22St%20Pierre%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alfredo%20M.%22%2C%22lastName%22%3A%22Valencia%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Takashi%22%2C%22lastName%22%3A%22Onikubo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Robert%20G.%22%2C%22lastName%22%3A%22Roeder%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yan%22%2C%22lastName%22%3A%22Han%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuan%22%2C%22lastName%22%3A%22He%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Frank%22%2C%22lastName%22%3A%22DiMaio%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Thomas%22%2C%22lastName%22%3A%22Walz%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cigall%22%2C%22lastName%22%3A%22Kadoch%22%7D%5D%2C%22abstractNote%22%3A%22Mammalian%20SWI%5C%2FSNF%20complexes%20are%20ATP-dependent%20chromatin%20remodeling%20complexes%20that%20regulate%20genomic%20architecture.%20Here%2C%20we%20present%20a%20structural%20model%20of%20the%20endogenously%20purified%20human%20canonical%20BAF%20complex%20bound%20to%20the%20nucleosome%2C%20generated%20using%20cryoelectron%20microscopy%20%28cryo-EM%29%2C%20cross-linking%20mass%20spectrometry%2C%20and%20homology%20modeling.%20BAF%20complexes%20bilaterally%20engage%20the%20nucleosome%20H2A%5C%2FH2B%20acidic%20patch%20regions%20through%20the%20SMARCB1%20C-terminal%20%5Cu03b1-helix%20and%20the%20SMARCA4%5C%2F2%20C-terminal%20SnAc%5C%2Fpost-SnAc%20regions%2C%20with%20disease-associated%20mutations%20in%20either%20causing%20attenuated%20chromatin%20remodeling%20activities.%20Further%2C%20we%20define%20changes%20in%20BAF%20complex%20architecture%20upon%20nucleosome%20engagement%20and%20compare%20the%20structural%20model%20of%20endogenous%20BAF%20to%20those%20of%20related%20SWI%5C%2FSNF-family%20complexes.%20Finally%2C%20we%20assign%20and%20experimentally%20interrogate%20cancer-associated%20hot-spot%20mutations%20localizing%20within%20the%20endogenous%20human%20BAF%20complex%2C%20identifying%20those%20that%20disrupt%20BAF%20subunit-subunit%20and%20subunit-nucleosome%20interfaces%20in%20the%20nucleosome-bound%20conformation.%20Taken%20together%2C%20this%20integrative%20structural%20approach%20provides%20important%20biophysical%20foundations%20for%20understanding%20the%20mechanisms%20of%20BAF%20complex%20function%20in%20normal%20and%20disease%20states.%22%2C%22date%22%3A%222020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.cell.2020.09.051%22%2C%22ISSN%22%3A%221097-4172%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222020-11-18T18%3A18%3A08Z%22%7D%7D%2C%7B%22key%22%3A%228FV3RIX8%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Patel%20et%20al.%22%2C%22parsedDate%22%3A%222019%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EPatel%2C%20A.%20B.%2C%20Moore%2C%20C.%20M.%2C%20Greber%2C%20B.%20J.%2C%20Luo%2C%20J.%2C%20Zukin%2C%20S.%20A.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Nogales%2C%20E.%20%282019%29.%20Architecture%20of%20the%20chromatin%20remodeler%20RSC%20and%20insights%20into%20its%20nucleosome%20engagement.%20%3Ci%3EELife%3C%5C%2Fi%3E%2C%20%3Ci%3E8%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.7554%5C%2FeLife.54449%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.7554%5C%2FeLife.54449%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D8FV3RIX8%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DLAZWGD9U%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Architecture%20of%20the%20chromatin%20remodeler%20RSC%20and%20insights%20into%20its%20nucleosome%20engagement%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Avinash%20B.%22%2C%22lastName%22%3A%22Patel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Camille%20M.%22%2C%22lastName%22%3A%22Moore%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Basil%20J.%22%2C%22lastName%22%3A%22Greber%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Stefan%20A.%22%2C%22lastName%22%3A%22Zukin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Eva%22%2C%22lastName%22%3A%22Nogales%22%7D%5D%2C%22abstractNote%22%3A%22Eukaryotic%20DNA%20is%20packaged%20into%20nucleosome%20arrays%2C%20which%20are%20repositioned%20by%20chromatin%20remodeling%20complexes%20to%20control%20DNA%20accessibility.%20The%20Saccharomyces%20cerevisiae%20RSC%20%28Remodeling%20the%20Structure%20of%20Chromatin%29%20complex%2C%20a%20member%20of%20the%20SWI%5C%2FSNF%20chromatin%20remodeler%20family%2C%20plays%20critical%20roles%20in%20genome%20maintenance%2C%20transcription%2C%20and%20DNA%20repair.%20Here%2C%20we%20report%20cryo-electron%20microscopy%20%28cryo-EM%29%20and%20crosslinking%20mass%20spectrometry%20%28CLMS%29%20studies%20of%20yeast%20RSC%20complex%20and%20show%20that%20RSC%20is%20composed%20of%20a%20rigid%20tripartite%20core%20and%20two%20flexible%20lobes.%20The%20core%20structure%20is%20scaffolded%20by%20an%20asymmetric%20Rsc8%20dimer%20and%20built%20with%20the%20evolutionarily%20conserved%20subunits%20Sfh1%2C%20Rsc6%2C%20Rsc9%20and%20Sth1.%20The%20flexible%20ATPase%20lobe%2C%20composed%20of%20helicase%20subunit%20Sth1%2C%20Arp7%2C%20Arp9%20and%20Rtt102%2C%20is%20anchored%20to%20this%20core%20by%20the%20N-terminus%20of%20Sth1.%20Our%20cryo-EM%20analysis%20of%20RSC%20bound%20to%20a%20nucleosome%20core%20particle%20shows%20that%20in%20addition%20to%20the%20expected%20nucleosome-Sth1%20interactions%2C%20RSC%20engages%20histones%20and%20nucleosomal%20DNA%20through%20one%20arm%20of%20the%20core%20structure%2C%20composed%20of%20the%20Rsc8%20SWIRM%20domains%2C%20Sfh1%20and%20Npl6.%20Our%20findings%20provide%20structural%20insights%20into%20the%20conserved%20assembly%20process%20for%20all%20members%20of%20the%20SWI%5C%2FSNF%20family%20of%20remodelers%2C%20and%20illustrate%20how%20RSC%20selects%2C%20engages%2C%20and%20remodels%20nucleosomes.%22%2C%22date%22%3A%222019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.7554%5C%2FeLife.54449%22%2C%22ISSN%22%3A%222050-084X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222020-01-25T00%3A32%3A03Z%22%7D%7D%2C%7B%22key%22%3A%228M2Y4CGW%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Hada%20et%20al.%22%2C%22parsedDate%22%3A%222019%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EHada%2C%20A.%2C%20Hota%2C%20S.%20K.%2C%20Luo%2C%20J.%2C%20Lin%2C%20Y.-C.%2C%20Kale%2C%20S.%2C%20Shaytan%2C%20A.%20K.%2C%20Bhardwaj%2C%20S.%20K.%2C%20Persinger%2C%20J.%2C%20Ranish%2C%20J.%2C%20Panchenko%2C%20A.%20R.%2C%20%26amp%3B%20Bartholomew%2C%20B.%20%282019%29.%20Histone%20Octamer%20Structure%20Is%20Altered%20Early%20in%20ISW2%20ATP-Dependent%20Nucleosome%20Remodeling.%20%3Ci%3ECell%20Reports%3C%5C%2Fi%3E%2C%20%3Ci%3E28%3C%5C%2Fi%3E%281%29%2C%20282-294.e6.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2019.05.106%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2019.05.106%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D8M2Y4CGW%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DW8AXCYID%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Histone%20Octamer%20Structure%20Is%20Altered%20Early%20in%20ISW2%20ATP-Dependent%20Nucleosome%20Remodeling%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arjan%22%2C%22lastName%22%3A%22Hada%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Swetansu%20K.%22%2C%22lastName%22%3A%22Hota%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuan-Chi%22%2C%22lastName%22%3A%22Lin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seyit%22%2C%22lastName%22%3A%22Kale%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexey%20K.%22%2C%22lastName%22%3A%22Shaytan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Saurabh%20K.%22%2C%22lastName%22%3A%22Bhardwaj%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jim%22%2C%22lastName%22%3A%22Persinger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Anna%20R.%22%2C%22lastName%22%3A%22Panchenko%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Blaine%22%2C%22lastName%22%3A%22Bartholomew%22%7D%5D%2C%22abstractNote%22%3A%22Nucleosomes%20are%20the%20fundamental%20building%20blocks%20of%5Cu00a0chromatin%20that%20regulate%20DNA%20access%20and%20are%20composed%20of%20histone%20octamers.%20ATP-dependent%20chromatin%20remodelers%20like%20ISW2%20regulate%20chromatin%20access%20by%20translationally%20moving%20nucleosomes%20to%20different%20DNA%20regions.%20We%20find%20that%20histone%20octamers%20are%20more%20pliable%20than%20previously%20assumed%20and%20distorted%20by%20ISW2%20early%20in%20remodeling%20before%20DNA%20enters%20nucleosomes%20and%20the%20ATPase%20motor%20moves%20processively%20on%20nucleosomal%20DNA.%20Uncoupling%20the%20ATPase%20activity%20of%20ISW2%20from%20nucleosome%20movement%20with%20deletion%20of%20the%20SANT%20domain%20from%20the%20C%20terminus%20of%20the%20Isw2%20catalytic%20subunit%20traps%20remodeling%20intermediates%20in%20which%20the%20histone%20octamer%20structure%20is%20changed.%20We%20find%20restricting%20histone%20movement%20by%20chemical%20crosslinking%20also%20traps%20remodeling%20intermediates%20resembling%20those%20seen%20early%20in%20ISW2%20remodeling%20with%20loss%20of%20the%20SANT%20domain.%20Other%20evidence%20shows%20histone%20octamers%20are%20intrinsically%20prone%20to%20changing%20their%20conformation%20and%20can%20be%20distorted%20merely%20by%20H3-H4%20tetramer%20disulfide%20crosslinking.%22%2C%22date%22%3A%222019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.celrep.2019.05.106%22%2C%22ISSN%22%3A%222211-1247%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222019-10-18T23%3A28%3A06Z%22%7D%7D%2C%7B%22key%22%3A%228WI73W9C%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Luo%20et%20al.%22%2C%22parsedDate%22%3A%222019%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELuo%2C%20J.%2C%20Bassett%2C%20J.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282019%29.%20Identification%20of%20Cross-linked%20Peptides%20Using%20Isotopomeric%20Cross-linkers.%20%3Ci%3EJournal%20of%20the%20American%20Society%20for%20Mass%20Spectrometry%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1007%5C%2Fs13361-019-02253-z%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1007%5C%2Fs13361-019-02253-z%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D8WI73W9C%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Identification%20of%20Cross-linked%20Peptides%20Using%20Isotopomeric%20Cross-linkers%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jacob%22%2C%22lastName%22%3A%22Bassett%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Chemical%20cross-linking%20combined%20with%20mass%20spectrometry%20%28CL-MS%29%20is%20a%20powerful%20method%20for%20characterizing%20the%20architecture%20of%20protein%20assemblies%20and%20for%20mapping%20protein-protein%20interactions.%20Despite%20its%20proven%20utility%2C%20confident%20identification%20of%20cross-linked%20peptides%20remains%20a%20formidable%20challenge%2C%20especially%20when%20the%20peptides%20are%20derived%20from%20complex%20mixtures.%20MS%20cleavable%20cross-linkers%20are%20gaining%20importance%20for%20CL-MS%20as%20they%20permit%20reliable%20identification%20of%20cross-linked%20peptides%20by%20whole%20proteome%20database%20searching%20using%20MS%5C%2FMS%20information.%20Here%20we%20introduce%20a%20novel%20class%20of%20MS%20cleavable%20cross-linkers%20called%20isotopomeric%20cross-linkers%20%28ICLs%29%2C%20which%20allow%20for%20confident%20and%20efficient%20identification%20of%20cross-linked%20peptides%20by%20whole%20proteome%20database%20searching.%20ICLs%20are%20simple%2C%20symmetrical%20molecules%20that%20asymmetrically%20incorporate%20heavy%20and%20light%20stable%20isotopes%20into%20the%20two%20arms%20of%20the%20cross-linker.%20As%20a%20result%20of%20this%20property%2C%20ICLs%20automatically%20generate%20pairs%20of%20isotopomeric%20cross-linked%20peptides%2C%20which%20differ%20only%20by%20the%20positions%20of%20the%20heavy%20and%20light%20isotopes.%20Upon%20fragmentation%20during%20MS%20analysis%2C%20these%20isotopomeric%20cross-linked%20peptides%20generate%20unique%20isotopic%20doublet%20ions%20that%20correspond%20to%20the%20individual%20peptides%20in%20the%20cross-link.%20The%20doublet%20ion%20information%20is%20used%20to%20determine%20the%20masses%20of%20the%20two%20cross-linked%20peptides%20from%20the%20same%20MS2%20spectrum%20that%20is%20also%20used%20for%20peptide%20spectrum%20matching%20%28PSM%29%20by%20sequence%20database%20searching.%20Here%20we%20present%20the%20rationale%20for%20and%20mechanism%20of%20cross-linked%20peptide%20identification%20by%20ICL-MS.%20We%20describe%20the%20synthesis%20of%20the%20ICL-1%20reagent%2C%20the%20ICL-MS%20workflow%2C%20and%20the%20performance%20characteristics%20of%20ICL-MS%20for%20identifying%20cross-linked%20peptides%20derived%20from%20increasingly%20complex%20mixtures%20by%20whole%20proteome%20database%20searching.%22%2C%22date%22%3A%222019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1007%5C%2Fs13361-019-02253-z%22%2C%22ISSN%22%3A%221879-1123%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222019-06-21T20%3A45%3A39Z%22%7D%7D%2C%7B%22key%22%3A%224P9SB8BR%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Palii%20et%20al.%22%2C%22parsedDate%22%3A%222019%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EPalii%2C%20C.%20G.%2C%20Cheng%2C%20Q.%2C%20Gillespie%2C%20M.%20A.%2C%20Shannon%2C%20P.%2C%20Mazurczyk%2C%20M.%2C%20Napolitani%2C%20G.%2C%20Price%2C%20N.%20D.%2C%20Ranish%2C%20J.%20A.%2C%20Morrissey%2C%20E.%2C%20Higgs%2C%20D.%20R.%2C%20%26amp%3B%20Brand%2C%20M.%20%282019%29.%20Single-Cell%20Proteomics%20Reveal%20that%20Quantitative%20Changes%20in%20Co-expressed%20Lineage-Specific%20Transcription%20Factors%20Determine%20Cell%20Fate.%20%3Ci%3ECell%20Stem%20Cell%3C%5C%2Fi%3E%2C%20%3Ci%3E24%3C%5C%2Fi%3E%285%29%2C%20812-820.e5.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.stem.2019.02.006%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.stem.2019.02.006%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D4P9SB8BR%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Single-Cell%20Proteomics%20Reveal%20that%20Quantitative%20Changes%20in%20Co-expressed%20Lineage-Specific%20Transcription%20Factors%20Determine%20Cell%20Fate%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Carmen%20G.%22%2C%22lastName%22%3A%22Palii%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Qian%22%2C%22lastName%22%3A%22Cheng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paul%22%2C%22lastName%22%3A%22Shannon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Michalina%22%2C%22lastName%22%3A%22Mazurczyk%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Giorgio%22%2C%22lastName%22%3A%22Napolitani%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nathan%20D.%22%2C%22lastName%22%3A%22Price%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Edward%22%2C%22lastName%22%3A%22Morrissey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Douglas%20R.%22%2C%22lastName%22%3A%22Higgs%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marjorie%22%2C%22lastName%22%3A%22Brand%22%7D%5D%2C%22abstractNote%22%3A%22Hematopoiesis%20provides%20an%20accessible%20system%20for%20studying%20the%20principles%20underlying%20cell-fate%20decisions%20in%20stem%20cells.%20Proposed%20models%20of%20hematopoiesis%20suggest%20that%20quantitative%20changes%20in%20lineage-specific%20transcription%20factors%20%28LS-TFs%29%20underlie%20cell-fate%20decisions.%20However%2C%20evidence%20for%20such%20models%20is%20lacking%20as%20TF%20levels%20are%20typically%20measured%20via%20RNA%20expression%20rather%20than%20by%20analyzing%20temporal%20changes%20in%20protein%20abundance.%20Here%2C%20we%20used%20single-cell%20mass%20cytometry%20and%20absolute%20quantification%20by%20mass%20spectrometry%20to%20capture%20the%20temporal%20dynamics%20of%20TF%20protein%20expression%20in%20individual%20cells%20during%20human%20erythropoiesis.%20We%20found%20that%20LS-TFs%20from%20alternate%20lineages%20are%20co-expressed%2C%20as%20proteins%2C%20in%20individual%20early%20progenitor%20cells%20and%20quantitative%20changes%20of%20LS-TFs%20occur%20gradually%20rather%20than%20abruptly%20to%20direct%20cell-fate%20decisions.%20Importantly%2C%20upregulation%20of%20a%20megakaryocytic%20TF%20in%20early%20progenitors%20is%20sufficient%20to%20deviate%20cells%20from%20an%20erythroid%20to%20a%20megakaryocyte%20trajectory%2C%20showing%20that%20quantitative%20changes%20in%20protein%20abundance%20of%20LS-TFs%20in%20progenitors%20can%20determine%20alternate%20cell%20fates.%22%2C%22date%22%3A%222019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.stem.2019.02.006%22%2C%22ISSN%22%3A%221875-9777%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222019-05-10T16%3A29%3A07Z%22%7D%7D%2C%7B%22key%22%3A%22TL3FPZUQ%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Patel%20et%20al.%22%2C%22parsedDate%22%3A%222018%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EPatel%2C%20A.%20B.%2C%20Louder%2C%20R.%20K.%2C%20Greber%2C%20B.%20J.%2C%20Gr%26%23xFC%3Bnberg%2C%20S.%2C%20Luo%2C%20J.%2C%20Fang%2C%20J.%2C%20Liu%2C%20Y.%2C%20Ranish%2C%20J.%2C%20Hahn%2C%20S.%2C%20%26amp%3B%20Nogales%2C%20E.%20%282018%29.%20Structure%20of%20human%20TFIID%20and%20mechanism%20of%20TBP%20loading%20onto%20promoter%20DNA.%20%3Ci%3EScience%20%28New%20York%2C%20N.Y.%29%3C%5C%2Fi%3E%2C%20%3Ci%3E362%3C%5C%2Fi%3E%286421%29.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1126%5C%2Fscience.aau8872%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1126%5C%2Fscience.aau8872%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DTL3FPZUQ%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structure%20of%20human%20TFIID%20and%20mechanism%20of%20TBP%20loading%20onto%20promoter%20DNA%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Avinash%20B.%22%2C%22lastName%22%3A%22Patel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Robert%20K.%22%2C%22lastName%22%3A%22Louder%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Basil%20J.%22%2C%22lastName%22%3A%22Greber%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sebastian%22%2C%22lastName%22%3A%22Gr%5Cu00fcnberg%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Fang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yutong%22%2C%22lastName%22%3A%22Liu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steve%22%2C%22lastName%22%3A%22Hahn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Eva%22%2C%22lastName%22%3A%22Nogales%22%7D%5D%2C%22abstractNote%22%3A%22The%20general%20transcription%20factor%20IID%20%28TFIID%29%20is%20a%20critical%20component%20of%20the%20eukaryotic%20transcription%20preinitiation%20complex%20%28PIC%29%20and%20is%20responsible%20for%20recognizing%20the%20core%20promoter%20DNA%20and%20initiating%20PIC%20assembly.%20We%20used%20cryo-electron%20microscopy%2C%20chemical%20cross-linking%20mass%20spectrometry%2C%20and%20biochemical%20reconstitution%20to%20determine%20the%20complete%20molecular%20architecture%20of%20TFIID%20and%20define%20the%20conformational%20landscape%20of%20TFIID%20in%20the%20process%20of%20TATA%20box-binding%20protein%20%28TBP%29%20loading%20onto%20promoter%20DNA.%20Our%20structural%20analysis%20revealed%20five%20structural%20states%20of%20TFIID%20in%20the%20presence%20of%20TFIIA%20and%20promoter%20DNA%2C%20showing%20that%20the%20initial%20binding%20of%20TFIID%20to%20the%20downstream%20promoter%20positions%20the%20upstream%20DNA%20and%20facilitates%20scanning%20of%20TBP%20for%20a%20TATA%20box%20and%20the%20subsequent%20engagement%20of%20the%20promoter.%20Our%20findings%20provide%20a%20mechanistic%20model%20for%20the%20specific%20loading%20of%20TBP%20by%20TFIID%20onto%20the%20promoter.%22%2C%22date%22%3A%222018%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1126%5C%2Fscience.aau8872%22%2C%22ISSN%22%3A%221095-9203%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222019-05-10T16%3A26%3A59Z%22%7D%7D%2C%7B%22key%22%3A%22XBDCM6QS%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kolesnikova%20et%20al.%22%2C%22parsedDate%22%3A%222018%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKolesnikova%2C%20O.%2C%20Ben-Shem%2C%20A.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20Schultz%2C%20P.%2C%20%26amp%3B%20Papai%2C%20G.%20%282018%29.%20Molecular%20structure%20of%20promoter-bound%20yeast%20TFIID.%20%3Ci%3ENature%20Communications%3C%5C%2Fi%3E%2C%20%3Ci%3E9%3C%5C%2Fi%3E%281%29%2C%204666.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-018-07096-y%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-018-07096-y%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DXBDCM6QS%27%3ECite%3C%5C%2Fa%3E%20%20%3Ca%20title%3D%27Download%27%20class%3D%27zp-DownloadURL%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.dl.php%3Fapi_user_id%3D2323737%26amp%3Bdlkey%3DN5LYWLZ3%26amp%3Bcontent_type%3Dapplication%5C%2Fpdf%27%3EDownload%3C%5C%2Fa%3E%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Molecular%20structure%20of%20promoter-bound%20yeast%20TFIID%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Olga%22%2C%22lastName%22%3A%22Kolesnikova%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Adam%22%2C%22lastName%22%3A%22Ben-Shem%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Patrick%22%2C%22lastName%22%3A%22Schultz%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Gabor%22%2C%22lastName%22%3A%22Papai%22%7D%5D%2C%22abstractNote%22%3A%22Transcription%20preinitiation%20complex%20assembly%20on%20the%20promoters%20of%20protein%20encoding%20genes%20is%20nucleated%20in%20vivo%20by%20TFIID%20composed%20of%20the%20TATA-box%20Binding%20Protein%20%28TBP%29%20and%2013%20TBP-associate%20factors%20%28Tafs%29%20providing%20regulatory%20and%20chromatin%20binding%20functions.%20Here%20we%20present%20the%20cryo-electron%20microscopy%20structure%20of%20promoter-bound%20yeast%20TFIID%20at%20a%20resolution%20better%20than%205%5Cu2009%5Cu00c5%2C%20except%20for%20a%20flexible%20domain.%20We%20position%20the%20crystal%20structures%20of%20several%20subunits%20and%2C%20in%20combination%20with%20cross-linking%20studies%2C%20describe%20the%20quaternary%20organization%20of%20TFIID.%20The%20compact%20tri%20lobed%20architecture%20is%20stabilized%20by%20a%20topologically%20closed%20Taf5-Taf6%20tetramer.%20We%20confirm%20the%20unique%20subunit%20stoichiometry%20prevailing%20in%20TFIID%20and%20uncover%20a%20hexameric%20arrangement%20of%20Tafs%20containing%20a%20histone%20fold%20domain%20in%20the%20Twin%20lobe.%22%2C%22date%22%3A%222018%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fs41467-018-07096-y%22%2C%22ISSN%22%3A%222041-1723%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-12-21T17%3A39%3A46Z%22%7D%7D%2C%7B%22key%22%3A%22HJ3P8V2L%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Mashtalir%20et%20al.%22%2C%22parsedDate%22%3A%222018%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EMashtalir%2C%20N.%2C%20D%26%23x2019%3BAvino%2C%20A.%20R.%2C%20Michel%2C%20B.%20C.%2C%20Luo%2C%20J.%2C%20Pan%2C%20J.%2C%20Otto%2C%20J.%20E.%2C%20Zullow%2C%20H.%20J.%2C%20McKenzie%2C%20Z.%20M.%2C%20Kubiak%2C%20R.%20L.%2C%20Pierre%2C%20R.%20S.%2C%20Valencia%2C%20A.%20M.%2C%20Poynter%2C%20S.%20J.%2C%20Cassel%2C%20S.%20H.%2C%20Ranish%2C%20J.%20A.%2C%20%26amp%3B%20Kadoch%2C%20C.%20%282018%29.%20Modular%20Organization%20and%20Assembly%20of%20SWI%5C%2FSNF%20Family%20Chromatin%20Remodeling%20Complexes.%20%3Ci%3ECell%3C%5C%2Fi%3E%2C%20%3Ci%3E175%3C%5C%2Fi%3E%285%29%2C%201272-1288.e20.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cell.2018.09.032%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cell.2018.09.032%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DHJ3P8V2L%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Modular%20Organization%20and%20Assembly%20of%20SWI%5C%2FSNF%20Family%20Chromatin%20Remodeling%20Complexes%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nazar%22%2C%22lastName%22%3A%22Mashtalir%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrew%20R.%22%2C%22lastName%22%3A%22D%5Cu2019Avino%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Brittany%20C.%22%2C%22lastName%22%3A%22Michel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Joshua%22%2C%22lastName%22%3A%22Pan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jordan%20E.%22%2C%22lastName%22%3A%22Otto%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hayley%20J.%22%2C%22lastName%22%3A%22Zullow%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Zachary%20M.%22%2C%22lastName%22%3A%22McKenzie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rachel%20L.%22%2C%22lastName%22%3A%22Kubiak%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Roodolph%20St%22%2C%22lastName%22%3A%22Pierre%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alfredo%20M.%22%2C%22lastName%22%3A%22Valencia%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%20J.%22%2C%22lastName%22%3A%22Poynter%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seth%20H.%22%2C%22lastName%22%3A%22Cassel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cigall%22%2C%22lastName%22%3A%22Kadoch%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222018%22%2C%22language%22%3A%22English%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.cell.2018.09.032%22%2C%22ISSN%22%3A%220092-8674%2C%201097-4172%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.cell.com%5C%2Fcell%5C%2Fabstract%5C%2FS0092-8674%2818%2931244-3%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-12-21T17%3A40%3A06Z%22%7D%7D%2C%7B%22key%22%3A%22VT7XG4KB%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Tuttle%20et%20al.%22%2C%22parsedDate%22%3A%222018%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ETuttle%2C%20L.%20M.%2C%20Pacheco%2C%20D.%2C%20Warfield%2C%20L.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20Hahn%2C%20S.%2C%20%26amp%3B%20Klevit%2C%20R.%20E.%20%282018%29.%20Gcn4-Mediator%20Specificity%20Is%20Mediated%20by%20a%20Large%20and%20Dynamic%20Fuzzy%20Protein-Protein%20Complex.%20%3Ci%3ECell%20Reports%3C%5C%2Fi%3E%2C%20%3Ci%3E22%3C%5C%2Fi%3E%2812%29%2C%203251%26%23x2013%3B3264.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2018.02.097%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2018.02.097%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DVT7XG4KB%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Gcn4-Mediator%20Specificity%20Is%20Mediated%20by%20a%20Large%20and%20Dynamic%20Fuzzy%20Protein-Protein%20Complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Lisa%20M.%22%2C%22lastName%22%3A%22Tuttle%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Derek%22%2C%22lastName%22%3A%22Pacheco%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Linda%22%2C%22lastName%22%3A%22Warfield%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Hahn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rachel%20E.%22%2C%22lastName%22%3A%22Klevit%22%7D%5D%2C%22abstractNote%22%3A%22Transcription%20activation%20domains%20%28ADs%29%20are%20inherently%20disordered%20proteins%20that%20often%20target%20multiple%20coactivator%20complexes%2C%20but%20the%20specificity%20of%20these%20interactions%20is%20not%20understood.%20Efficient%20transcription%20activation%20by%20yeast%20Gcn4%20requires%20its%20tandem%20ADs%20and%20four%20activator-binding%20domains%20%28ABDs%29%20on%20its%20target%2C%20the%20Mediator%20subunit%20Med15.%20Multiple%20ABDs%20are%20a%20common%20feature%20of%20coactivator%20complexes.%20We%20find%20that%20the%20large%20Gcn4-Med15%20complex%20is%20heterogeneous%20and%20contains%20nearly%20all%20possible%20AD-ABD%20interactions.%20Gcn4-Med15%20forms%20via%20a%20dynamic%20fuzzy%20protein-protein%20interface%2C%20where%20ADs%20bind%20the%20ABDs%20in%20multiple%20orientations%20via%20hydrophobic%20regions%20that%20gain%20helicity.%20This%20combinatorial%20mechanism%20allows%20individual%20low-affinity%20and%20specificity%20interactions%20to%5Cu00a0generate%20a%20biologically%20functional%2C%20specific%2C%20and%20higher%20affinity%20complex%20despite%20lacking%20a%20defined%20protein-protein%20interface.%20This%20binding%20strategy%20is%20likely%20representative%20of%20many%20activators%20that%20target%20multiple%20coactivators%2C%20as%20it%20allows%20great%20flexibility%20in%20combinations%20of%20activators%20that%20can%20cooperate%20to%20regulate%20genes%20with%20variable%20coactivator%20requirements.%22%2C%22date%22%3A%222018%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.celrep.2018.02.097%22%2C%22ISSN%22%3A%222211-1247%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-03-29T20%3A01%3A58Z%22%7D%7D%2C%7B%22key%22%3A%22X8A32K59%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Pacheco%20et%20al.%22%2C%22parsedDate%22%3A%222018%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EPacheco%2C%20D.%2C%20Warfield%2C%20L.%2C%20Brajcich%2C%20M.%2C%20Robbins%2C%20H.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Hahn%2C%20S.%20%282018%29.%20Transcription%20activation%20domains%20of%20the%20yeast%20factors%20Met4%20and%20Ino2%3A%20tandem%20activation%20domains%20with%20properties%20similar%20to%20the%20yeast%20Gcn4%20activator.%20%3Ci%3EMolecular%20and%20Cellular%20Biology%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00038-18%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00038-18%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DX8A32K59%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Transcription%20activation%20domains%20of%20the%20yeast%20factors%20Met4%20and%20Ino2%3A%20tandem%20activation%20domains%20with%20properties%20similar%20to%20the%20yeast%20Gcn4%20activator%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Derek%22%2C%22lastName%22%3A%22Pacheco%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Linda%22%2C%22lastName%22%3A%22Warfield%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Michelle%22%2C%22lastName%22%3A%22Brajcich%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hannah%22%2C%22lastName%22%3A%22Robbins%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Hahn%22%7D%5D%2C%22abstractNote%22%3A%22Eukaryotic%20transcription%20activation%20domains%20%28ADs%29%20are%20intrinsically%20disordered%20polypeptides%20that%20typically%20interact%20with%20coactivator%20complexes%2C%20leading%20to%20stimulation%20of%20transcription%20initiation%2C%20elongation%20and%20chromatin%20modifications.%20Here%20we%20examine%20the%20properties%20of%20two%20strong%20and%20conserved%20yeast%20ADs%3A%20Met4%20and%20Ino2.%20Both%20factors%20have%20tandem%20ADs%20that%20were%20identified%20by%20conserved%20sequence%20and%20functional%20studies.%20While%20AD%20function%20from%20both%20factors%20depends%20on%20hydrophobic%20residues%2C%20Ino2%20further%20requires%20key%20conserved%20acidic%20and%20polar%20residues%20for%20optimal%20function.%20Binding%20studies%20show%20that%20the%20ADs%20bind%20multiple%20Med15%20activator%20binding%20domains%20%28ABDs%29%20with%20a%20similar%20order%20of%20micromolar%20affinity%2C%20and%20similar%20but%20distinct%20thermodynamic%20properties.%20Protein%20crosslinking%20shows%20that%20no%20unique%20complex%20is%20formed%20upon%20Met4-Med15%20binding.%20Rather%2C%20we%20observed%20heterogeneous%20AD-ABD%20contacts%20with%20nearly%20every%20possible%20AD-ABD%20combination.%20Many%20of%20these%20properties%20are%20similar%20to%20those%20observed%20with%20the%20yeast%20activator%20Gcn4%2C%20which%20forms%20a%20large%20heterogeneous%2C%20dynamic%2C%20and%20fuzzy%20complex%20with%20Med15.%20We%20suggest%20that%20this%20molecular%20behavior%20is%20common%20among%20eukaryotic%20activators.%22%2C%22date%22%3A%222018%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1128%5C%2FMCB.00038-18%22%2C%22ISSN%22%3A%221098-5549%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-03-19T17%3A28%3A41Z%22%7D%7D%2C%7B%22key%22%3A%22VADMF6D5%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Turkarslan%20et%20al.%22%2C%22parsedDate%22%3A%222017%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ETurkarslan%2C%20S.%2C%20Raman%2C%20A.%20V.%2C%20Thompson%2C%20A.%20W.%2C%20Arens%2C%20C.%20E.%2C%20Gillespie%2C%20M.%20A.%2C%20von%20Netzer%2C%20F.%2C%20Hillesland%2C%20K.%20L.%2C%20Stolyar%2C%20S.%2C%20L%26%23xF3%3Bpez%20Garc%26%23xED%3Ba%20de%20Lomana%2C%20A.%2C%20Reiss%2C%20D.%20J.%2C%20Gorman-Lewis%2C%20D.%2C%20Zane%2C%20G.%20M.%2C%20Ranish%2C%20J.%20A.%2C%20Wall%2C%20J.%20D.%2C%20Stahl%2C%20D.%20A.%2C%20%26amp%3B%20Baliga%2C%20N.%20S.%20%282017%29.%20Mechanism%20for%20microbial%20population%20collapse%20in%20a%20fluctuating%20resource%20environment.%20%3Ci%3EMolecular%20Systems%20Biology%3C%5C%2Fi%3E%2C%20%3Ci%3E13%3C%5C%2Fi%3E%283%29%2C%20919.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DVADMF6D5%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Mechanism%20for%20microbial%20population%20collapse%20in%20a%20fluctuating%20resource%20environment%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Serdar%22%2C%22lastName%22%3A%22Turkarslan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arjun%20V.%22%2C%22lastName%22%3A%22Raman%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Anne%20W.%22%2C%22lastName%22%3A%22Thompson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christina%20E.%22%2C%22lastName%22%3A%22Arens%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Frederick%22%2C%22lastName%22%3A%22von%20Netzer%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kristina%20L.%22%2C%22lastName%22%3A%22Hillesland%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sergey%22%2C%22lastName%22%3A%22Stolyar%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Adrian%22%2C%22lastName%22%3A%22L%5Cu00f3pez%20Garc%5Cu00eda%20de%20Lomana%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22David%20J.%22%2C%22lastName%22%3A%22Reiss%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Drew%22%2C%22lastName%22%3A%22Gorman-Lewis%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Grant%20M.%22%2C%22lastName%22%3A%22Zane%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Judy%20D.%22%2C%22lastName%22%3A%22Wall%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22David%20A.%22%2C%22lastName%22%3A%22Stahl%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nitin%20S.%22%2C%22lastName%22%3A%22Baliga%22%7D%5D%2C%22abstractNote%22%3A%22Managing%20trade-offs%20through%20gene%20regulation%20is%20believed%20to%20confer%20resilience%20to%20a%20microbial%20community%20in%20a%20fluctuating%20resource%20environment.%20To%20investigate%20this%20hypothesis%2C%20we%20imposed%20a%20fluctuating%20environment%20that%20required%20the%20sulfate-reducer%20Desulfovibrio%20vulgaris%20to%20undergo%20repeated%20ecologically%20relevant%20shifts%20between%20retaining%20metabolic%20independence%20%28active%20capacity%20for%20sulfate%20respiration%29%20and%20becoming%20metabolically%20specialized%20to%20a%20mutualistic%20association%20with%20the%20hydrogen-consuming%20Methanococcus%20maripaludis%20Strikingly%2C%20the%20microbial%20community%20became%20progressively%20less%20proficient%20at%20restoring%20the%20environmentally%20relevant%20physiological%20state%20after%20each%20perturbation%20and%20most%20cultures%20collapsed%20within%203-7%20shifts.%20Counterintuitively%2C%20the%20collapse%20phenomenon%20was%20prevented%20by%20a%20single%20regulatory%20mutation.%20We%20have%20characterized%20the%20mechanism%20for%20collapse%20by%20conducting%20RNA-seq%20analysis%2C%20proteomics%2C%20microcalorimetry%2C%20and%20single-cell%20transcriptome%20analysis.%20We%20demonstrate%20that%20the%20collapse%20was%20caused%20by%20conditional%20gene%20regulation%2C%20which%20drove%20precipitous%20decline%20in%20intracellular%20abundance%20of%20essential%20transcripts%20and%20proteins%2C%20imposing%20greater%20energetic%20burden%20of%20regulation%20to%20restore%20function%20in%20a%20fluctuating%20environment.%22%2C%22date%22%3A%222017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%221744-4292%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-12-21T17%3A41%3A41Z%22%7D%7D%2C%7B%22key%22%3A%22MA6M3T48%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Sen%20et%20al.%22%2C%22parsedDate%22%3A%222017%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ESen%2C%20P.%2C%20Luo%2C%20J.%2C%20Hada%2C%20A.%2C%20Hailu%2C%20S.%20G.%2C%20Dechassa%2C%20M.%20L.%2C%20Persinger%2C%20J.%2C%20Brahma%2C%20S.%2C%20Paul%2C%20S.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Bartholomew%2C%20B.%20%282017%29.%20Loss%20of%20Snf5%20Induces%20Formation%20of%20an%20Aberrant%20SWI%5C%2FSNF%20Complex.%20%3Ci%3ECell%20Reports%3C%5C%2Fi%3E%2C%20%3Ci%3E18%3C%5C%2Fi%3E%289%29%2C%202135%26%23x2013%3B2147.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2017.02.017%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.celrep.2017.02.017%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DMA6M3T48%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Loss%20of%20Snf5%20Induces%20Formation%20of%20an%20Aberrant%20SWI%5C%2FSNF%20Complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Payel%22%2C%22lastName%22%3A%22Sen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arjan%22%2C%22lastName%22%3A%22Hada%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Solomon%20G.%22%2C%22lastName%22%3A%22Hailu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mekonnen%20Lemma%22%2C%22lastName%22%3A%22Dechassa%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jim%22%2C%22lastName%22%3A%22Persinger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sandipan%22%2C%22lastName%22%3A%22Brahma%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Somnath%22%2C%22lastName%22%3A%22Paul%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Blaine%22%2C%22lastName%22%3A%22Bartholomew%22%7D%5D%2C%22abstractNote%22%3A%22The%20SWI%5C%2FSNF%20chromatin%20remodeling%20complex%20is%20highly%20conserved%20from%20yeast%20to%20human%2C%20and%20aberrant%20SWI%5C%2FSNF%20complexes%20contribute%20to%20human%20disease.%20The%20Snf5%5C%2FSMARCB1%5C%2FINI1%20subunit%20of%20SWI%5C%2FSNF%20is%20a%20tumor%20suppressor%20frequently%20lost%20in%20pediatric%20rhabdoid%20cancers.%20We%20examined%20the%20effects%20of%20Snf5%20loss%20on%20the%20composition%2C%20nucleosome%20binding%2C%20recruitment%2C%20and%20remodeling%20activities%20of%20yeast%20SWI%5C%2FSNF.%20The%20Snf5%20subunit%20is%20shown%20by%20crosslinking-mass%20spectrometry%20%28CX-MS%29%20and%20subunit%20deletion%20analysis%20to%20interact%20with%20the%20ATPase%20domain%20of%20Snf2%20and%20to%20form%20a%20submodule%20consisting%20of%20Snf5%2C%20Swp82%2C%20and%20Taf14.%20Snf5%20promotes%20binding%20of%20the%20Snf2%20ATPase%20domain%20to%20nucleosomal%20DNA%20and%20enhances%20the%20catalytic%20and%20nucleosome%20remodeling%20activities%20of%20SWI%5C%2FSNF.%20Snf5%20is%20also%20required%20for%20SWI%5C%2FSNF%20recruitment%20by%20acidic%20transcription%20factors.%20RNA-seq%20analysis%20suggests%20that%20both%20the%20recruitment%20and%20remodeling%20functions%20of%20Snf5%20are%20required%20in%5Cu00a0vivo%20for%20SWI%5C%2FSNF%20regulation%20of%20gene%20expression.%20Thus%2C%20loss%20of%20SNF5%20alters%20the%20structure%20and%20function%20of%20SWI%5C%2FSNF.%22%2C%22date%22%3A%222017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.celrep.2017.02.017%22%2C%22ISSN%22%3A%222211-1247%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222018-12-21T17%3A41%3A25Z%22%7D%7D%2C%7B%22key%22%3A%22IKG72TKW%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Nakayama%20et%20al.%22%2C%22parsedDate%22%3A%222017%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ENakayama%2C%20R.%20T.%2C%20Pulice%2C%20J.%20L.%2C%20Valencia%2C%20A.%20M.%2C%20McBride%2C%20M.%20J.%2C%20McKenzie%2C%20Z.%20M.%2C%20Gillespie%2C%20M.%20A.%2C%20Ku%2C%20W.%20L.%2C%20Teng%2C%20M.%2C%20Cui%2C%20K.%2C%20Williams%2C%20R.%20T.%2C%20Cassel%2C%20S.%20H.%2C%20Qing%2C%20H.%2C%20Widmer%2C%20C.%20J.%2C%20Demetri%2C%20G.%20D.%2C%20Irizarry%2C%20R.%20A.%2C%20Zhao%2C%20K.%2C%20Ranish%2C%20J.%20A.%2C%20%26amp%3B%20Kadoch%2C%20C.%20%282017%29.%20SMARCB1%20is%20required%20for%20widespread%20BAF%20complex-mediated%20activation%20of%20enhancers%20and%20bivalent%20promoters.%20%3Ci%3ENature%20Genetics%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fng.3958%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fng.3958%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DIKG72TKW%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22SMARCB1%20is%20required%20for%20widespread%20BAF%20complex-mediated%20activation%20of%20enhancers%20and%20bivalent%20promoters%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Robert%20T.%22%2C%22lastName%22%3A%22Nakayama%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22John%20L.%22%2C%22lastName%22%3A%22Pulice%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alfredo%20M.%22%2C%22lastName%22%3A%22Valencia%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Matthew%20J.%22%2C%22lastName%22%3A%22McBride%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Zachary%20M.%22%2C%22lastName%22%3A%22McKenzie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Wai%20Lim%22%2C%22lastName%22%3A%22Ku%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mingxiang%22%2C%22lastName%22%3A%22Teng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kairong%22%2C%22lastName%22%3A%22Cui%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Robert%20T.%22%2C%22lastName%22%3A%22Williams%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seth%20H.%22%2C%22lastName%22%3A%22Cassel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22He%22%2C%22lastName%22%3A%22Qing%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christian%20J.%22%2C%22lastName%22%3A%22Widmer%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22George%20D.%22%2C%22lastName%22%3A%22Demetri%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rafael%20A.%22%2C%22lastName%22%3A%22Irizarry%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Keji%22%2C%22lastName%22%3A%22Zhao%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cigall%22%2C%22lastName%22%3A%22Kadoch%22%7D%5D%2C%22abstractNote%22%3A%22Perturbations%20to%20mammalian%20SWI%5C%2FSNF%20%28mSWI%5C%2FSNF%20or%20BAF%29%20complexes%20contribute%20to%20more%20than%2020%25%20of%20human%20cancers%2C%20with%20driving%20roles%20first%20identified%20in%20malignant%20rhabdoid%20tumor%2C%20an%20aggressive%20pediatric%20cancer%20characterized%20by%20biallelic%20inactivation%20of%20the%20core%20BAF%20complex%20subunit%20SMARCB1%20%28BAF47%29.%20However%2C%20the%20mechanism%20by%20which%20this%20alteration%20contributes%20to%20tumorigenesis%20remains%20poorly%20understood.%20We%20find%20that%20BAF47%20loss%20destabilizes%20BAF%20complexes%20on%20chromatin%2C%20absent%20significant%20changes%20in%20complex%20assembly%20or%20integrity.%20Rescue%20of%20BAF47%20in%20BAF47-deficient%20sarcoma%20cell%20lines%20results%20in%20increased%20genome-wide%20BAF%20complex%20occupancy%2C%20facilitating%20widespread%20enhancer%20activation%20and%20opposition%20of%20Polycomb-mediated%20repression%20at%20bivalent%20promoters.%20We%20demonstrate%20differential%20regulation%20by%20two%20distinct%20mSWI%5C%2FSNF%20assemblies%2C%20BAF%20and%20PBAF%20complexes%2C%20enhancers%20and%20promoters%2C%20respectively%2C%20suggesting%20that%20each%20complex%20has%20distinct%20functions%20that%20are%20perturbed%20upon%20BAF47%20loss.%20Our%20results%20demonstrate%20collaborative%20mechanisms%20of%20mSWI%5C%2FSNF-mediated%20gene%20activation%2C%20identifying%20functions%20that%20are%20co-opted%20or%20abated%20to%20drive%20human%20cancers%20and%20developmental%20disorders.%22%2C%22date%22%3A%222017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fng.3958%22%2C%22ISSN%22%3A%221546-1718%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222017-10-03T21%3A13%3A48Z%22%7D%7D%2C%7B%22key%22%3A%22F4D4GWC6%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22McDermott%20et%20al.%22%2C%22parsedDate%22%3A%222016%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EMcDermott%2C%20S.%20M.%2C%20Luo%2C%20J.%2C%20Carnes%2C%20J.%2C%20Ranish%2C%20J.%20A.%2C%20%26amp%3B%20Stuart%2C%20K.%20%282016%29.%20The%20Architecture%20of%20Trypanosoma%20brucei%20editosomes.%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America%3C%5C%2Fi%3E%2C%20%3Ci%3E113%3C%5C%2Fi%3E%2842%29%2C%20E6476%26%23x2013%3BE6485.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1610177113%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1610177113%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DF4D4GWC6%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20Architecture%20of%20Trypanosoma%20brucei%20editosomes%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Suzanne%20M.%22%2C%22lastName%22%3A%22McDermott%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jason%22%2C%22lastName%22%3A%22Carnes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kenneth%22%2C%22lastName%22%3A%22Stuart%22%7D%5D%2C%22abstractNote%22%3A%22Uridine%20insertion%20and%20deletion%20RNA%20editing%20generates%20functional%20mitochondrial%20mRNAs%20in%20Trypanosoma%20brucei%20Editing%20is%20catalyzed%20by%20three%20distinct%20%5Cu223c20S%20editosomes%20that%20have%20a%20common%20set%20of%2012%20proteins%2C%20but%20are%20typified%20by%20mutually%20exclusive%20RNase%20III%20endonucleases%20with%20distinct%20cleavage%20specificities%20and%20unique%20partner%20proteins.%20Previous%20studies%20identified%20a%20network%20of%20protein-protein%20interactions%20among%20a%20subset%20of%20common%20editosome%20proteins%2C%20but%20interactions%20among%20the%20endonucleases%20and%20their%20partner%20proteins%2C%20and%20their%20interactions%20with%20common%20subunits%20were%20not%20identified.%20Here%2C%20chemical%20cross-linking%20and%20mass%20spectrometry%2C%20comparative%20structural%20modeling%2C%20and%20genetic%20and%20biochemical%20analyses%20were%20used%20to%20define%20the%20molecular%20architecture%20and%20subunit%20organization%20of%20purified%20editosomes.%20We%20identified%20intra-%20and%20interprotein%20cross-links%20for%20all%20editosome%20subunits%20that%20are%20fully%20consistent%20with%20editosome%20protein%20structures%20and%20previously%20identified%20interactions%2C%20which%20we%20validated%20by%20genetic%20and%20biochemical%20studies.%20The%20results%20were%20used%20to%20create%20a%20highly%20detailed%20map%20of%20editosome%20protein%20domain%20proximities%2C%20leading%20to%20identification%20of%20molecular%20interactions%20between%20subunits%2C%20insights%20into%20the%20functions%20of%20noncatalytic%20editosome%20proteins%2C%20and%20a%20global%20understanding%20of%20editosome%20architecture.%22%2C%22date%22%3A%222016%22%2C%22language%22%3A%22ENG%22%2C%22DOI%22%3A%2210.1073%5C%2Fpnas.1610177113%22%2C%22ISSN%22%3A%221091-6490%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-11-01T16%3A14%3A44Z%22%7D%7D%2C%7B%22key%22%3A%227QUTT8WP%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Warfield%20et%20al.%22%2C%22parsedDate%22%3A%222016%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWarfield%2C%20L.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Hahn%2C%20S.%20%282016%29.%20Function%20of%20conserved%20topological%20regions%20within%20the%20S.%20cerevisiae%20basal%20transcription%20factor%20TFIIH.%20%3Ci%3EMolecular%20and%20Cellular%20Biology%3C%5C%2Fi%3E.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00182-16%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1128%5C%2FMCB.00182-16%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D7QUTT8WP%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Function%20of%20conserved%20topological%20regions%20within%20the%20S.%20cerevisiae%20basal%20transcription%20factor%20TFIIH%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Linda%22%2C%22lastName%22%3A%22Warfield%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Hahn%22%7D%5D%2C%22abstractNote%22%3A%22TFIIH%20is%20a%2010%20subunit%20RNA%20polymerase%20II%20basal%20transcription%20factor%20with%20a%20dual%20role%20in%20DNA%20repair.%20TFIIH%20contains%20three%20enzymatic%20functions%20and%20over%2030%20conserved%20subdomains%20and%20topological%20regions.%20We%20systematically%20tested%20the%20function%20of%20these%20regions%20in%20three%20TFIIH%20core%20module%20subunits%3A%20Ssl1%2C%20Tfb4%2C%20and%20Tfb2%2C%20in%20the%20DNA%20translocase%20subunit%20Ssl2%2C%20and%20in%20the%20kinase%20module%20subunit%20Tfb3.%20Our%20results%20are%20consistent%20with%20previously%20predicted%20roles%20for%20the%20Tfb2%20Hub%2C%20Ssl2%20Lock%20and%20Tfb3%20Latch%20regions%2C%20with%20mutations%20in%20these%20elements%20typically%20having%20severe%20defects%20in%20TFIIH%20subunit%20association.%20We%20also%20found%20unexpected%20roles%20for%20other%20domains%20whose%20function%20had%20not%20previously%20been%20defined.%20First%2C%20the%20Ssl1-Tfb4%20Ring%20domains%20are%20important%20for%20TFIIH%20assembly.%20Second%2C%20the%20Tfb2%20Hub%20and%20HEAT%20domains%20have%20an%20unexpected%20role%20in%20association%20with%20Tfb3.%20Third%2C%20the%20Tfb3%20Ring%20domain%20is%20important%20for%20association%20with%20many%20other%20TFIIH%20subunits.%20Fourth%2C%20a%20partial%20deletion%20of%20the%20Ssl1%20NTE%20domain%20inhibits%20TFIIH%20function%20without%20affecting%20subunit%20association.%20Finally%2C%20we%20used%20site-specific%20crosslinking%20to%20localize%20the%20Tfb3-binding%20surface%20on%20the%20Rad3%20Arch%20domain.%20Our%20crosslinking%20results%20suggest%20that%20Tfb3%20and%20Rad3%20have%20an%20unusual%20interface%20with%20Tfb3%20binding%20on%20two%20opposite%20faces%20of%20the%20Arch.%22%2C%22date%22%3A%222016%22%2C%22language%22%3A%22ENG%22%2C%22DOI%22%3A%2210.1128%5C%2FMCB.00182-16%22%2C%22ISSN%22%3A%221098-5549%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-09-12T19%3A25%3A49Z%22%7D%7D%2C%7B%22key%22%3A%22PE46R632%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Luo%20et%20al.%22%2C%22parsedDate%22%3A%222015-09-03%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELuo%2C%20J.%2C%20Cimermancic%2C%20P.%2C%20Viswanath%2C%20S.%2C%20Ebmeier%2C%20C.%20C.%2C%20Kim%2C%20B.%2C%20Dehecq%2C%20M.%2C%20Raman%2C%20V.%2C%20Greenberg%2C%20C.%20H.%2C%20Pellarin%2C%20R.%2C%20Sali%2C%20A.%2C%20Taatjes%2C%20D.%20J.%2C%20Hahn%2C%20S.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282015%29.%20Architecture%20of%20the%20Human%20and%20Yeast%20General%20Transcription%20and%20DNA%20Repair%20Factor%20TFIIH.%20%3Ci%3EMolecular%20Cell%3C%5C%2Fi%3E%2C%20%3Ci%3E59%3C%5C%2Fi%3E%2C%20794%26%23x2013%3B806.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.molcel.2015.07.016%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.molcel.2015.07.016%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DPE46R632%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Architecture%20of%20the%20Human%20and%20Yeast%20General%20Transcription%20and%20DNA%20Repair%20Factor%20TFIIH%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22P.%22%2C%22lastName%22%3A%22Cimermancic%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Viswanath%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20C.%22%2C%22lastName%22%3A%22Ebmeier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Kim%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Dehecq%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22V.%22%2C%22lastName%22%3A%22Raman%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20H.%22%2C%22lastName%22%3A%22Greenberg%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22R.%22%2C%22lastName%22%3A%22Pellarin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%22%2C%22lastName%22%3A%22Sali%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22D.%20J.%22%2C%22lastName%22%3A%22Taatjes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Hahn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22TFIIH%20is%20essential%20for%20both%20RNA%20polymerase%20II%20transcription%20and%20DNA%20repair%2C%20and%20mutations%20in%20TFIIH%20can%20result%20in%20human%20disease.%20Here%2C%20we%20determine%20the%20molecular%20architecture%20of%20human%20and%20yeast%20TFIIH%20by%20an%20integrative%20approach%20using%20chemical%20crosslinking%5C%2Fmass%20spectrometry%20%28CXMS%29%20data%2C%20biochemical%20analyses%2C%20and%20previously%20published%20electron%20microscopy%20maps.%20We%20identified%20four%20new%20conserved%20%5C%22topological%20regions%5C%22%20that%20function%20as%20hubs%20for%20TFIIH%20assembly%20and%20more%20than%2035%20conserved%20topological%20features%20within%20TFIIH%2C%20illuminating%20a%20network%20of%20interactions%20involved%20in%20TFIIH%20assembly%20and%20regulation%20of%20its%20activities.%20We%20show%20that%20one%20of%20these%20conserved%20regions%2C%20the%20p62%5C%2FTfb1%20Anchor%20region%2C%20directly%20interacts%20with%20the%20DNA%20helicase%20subunit%20XPD%5C%2FRad3%20in%20native%20TFIIH%20and%20is%20required%20for%20the%20integrity%20and%20function%20of%20TFIIH.%20We%20also%20reveal%20the%20structural%20basis%20for%20defects%20in%20patients%20with%20xeroderma%20pigmentosum%20and%20trichothiodystrophy%2C%20with%20mutations%20found%20at%20the%20interface%20between%20the%20p62%20Anchor%20region%20and%20the%20XPD%20subunit.%22%2C%22date%22%3A%222015-9-3%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.molcel.2015.07.016%22%2C%22ISSN%22%3A%221097-4164%20%28Electronic%29%201097-2765%20%28Linking%29%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-08T18%3A58%3A51Z%22%7D%7D%2C%7B%22key%22%3A%22B79ZKW59%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Gillespie%20et%20al.%22%2C%22parsedDate%22%3A%222015-05-05%22%2C%22numChildren%22%3A3%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EGillespie%2C%20M.%20A.%2C%20Gold%2C%20E.%20S.%2C%20Ramsey%2C%20S.%20A.%2C%20Podolsky%2C%20I.%2C%20Aderem%2C%20A.%2C%20%26amp%3B%20Ranish%2C%20J.%20A.%20%282015%29.%20An%20LXR-NCOA5%20gene%20regulatory%20complex%20directs%20inflammatory%20crosstalk-dependent%20repression%20of%20macrophage%20cholesterol%20efflux.%20%3Ci%3EThe%20EMBO%20Journal%3C%5C%2Fi%3E%2C%20%3Ci%3E34%3C%5C%2Fi%3E%289%29%2C%201244%26%23x2013%3B1258.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.15252%5C%2Fembj.201489819%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.15252%5C%2Fembj.201489819%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DB79ZKW59%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22An%20LXR-NCOA5%20gene%20regulatory%20complex%20directs%20inflammatory%20crosstalk-dependent%20repression%20of%20macrophage%20cholesterol%20efflux%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mark%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Elizabeth%20S.%22%2C%22lastName%22%3A%22Gold%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Stephen%20A.%22%2C%22lastName%22%3A%22Ramsey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Irina%22%2C%22lastName%22%3A%22Podolsky%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alan%22%2C%22lastName%22%3A%22Aderem%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22LXR-cofactor%20complexes%20activate%20the%20gene%20expression%20program%20responsible%20for%20cholesterol%20efflux%20in%20macrophages.%20Inflammation%20antagonizes%20this%20program%2C%20resulting%20in%20foam%20cell%20formation%20and%20atherosclerosis%3B%20however%2C%20the%20molecular%20mechanisms%20underlying%20this%20antagonism%20remain%20to%20be%20fully%20elucidated.%20We%20use%20promoter%20enrichment-quantitative%20mass%20spectrometry%20%28PE-QMS%29%20to%20characterize%20the%20composition%20of%20gene%20regulatory%20complexes%20assembled%20at%20the%20promoter%20of%20the%20lipid%20transporter%20Abca1%20following%20downregulation%20of%20its%20expression.%20We%20identify%20a%20subset%20of%20proteins%20that%20show%20LXR%20ligand-%20and%20binding-dependent%20association%20with%20the%20Abca1%20promoter%20and%20demonstrate%20they%20differentially%20control%20Abca1%20expression.%20We%20determine%20that%20NCOA5%20is%20linked%20to%20inflammatory%20Toll-like%20receptor%20%28TLR%29%20signaling%20and%20establish%20that%20NCOA5%20functions%20as%20an%20LXR%20corepressor%20to%20attenuate%20Abca1%20expression.%20Importantly%2C%20TLR3-LXR%20signal%20crosstalk%20promotes%20recruitment%20of%20NCOA5%20to%20the%20Abca1%20promoter%20together%20with%20loss%20of%20RNA%20polymerase%20II%20and%20reduced%20cholesterol%20efflux.%20Together%2C%20these%20data%20significantly%20expand%20our%20knowledge%20of%20regulatory%20inputs%20impinging%20on%20the%20Abca1%20promoter%20and%20indicate%20a%20central%20role%20for%20NCOA5%20in%20mediating%20crosstalk%20between%20pro-inflammatory%20and%20anti-inflammatory%20pathways%20that%20results%20in%20repression%20of%20macrophage%20cholesterol%20efflux.%22%2C%22date%22%3A%222015-5-5%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.15252%5C%2Fembj.201489819%22%2C%22ISSN%22%3A%221460-2075%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-07-09T02%3A07%3A09Z%22%7D%7D%2C%7B%22key%22%3A%22EJ7CQ7DM%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kapoor%20et%20al.%22%2C%22parsedDate%22%3A%222015-03-15%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKapoor%2C%20P.%2C%20Bao%2C%20Y.%2C%20Xiao%2C%20J.%2C%20Luo%2C%20J.%2C%20Shen%2C%20J.%2C%20Persinger%2C%20J.%2C%20Peng%2C%20G.%2C%20Ranish%2C%20J.%2C%20Bartholomew%2C%20B.%2C%20%26amp%3B%20Shen%2C%20X.%20%282015%29.%20Regulation%20of%20Mec1%20kinase%20activity%20by%20the%20SWI%5C%2FSNF%20chromatin%20remodeling%20complex.%20%3Ci%3EGenes%20%26amp%3B%20Development%3C%5C%2Fi%3E%2C%20%3Ci%3E29%3C%5C%2Fi%3E%286%29%2C%20591%26%23x2013%3B602.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1101%5C%2Fgad.257626.114%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1101%5C%2Fgad.257626.114%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DEJ7CQ7DM%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Regulation%20of%20Mec1%20kinase%20activity%20by%20the%20SWI%5C%2FSNF%20chromatin%20remodeling%20complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Prabodh%22%2C%22lastName%22%3A%22Kapoor%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yunhe%22%2C%22lastName%22%3A%22Bao%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jing%22%2C%22lastName%22%3A%22Xiao%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jianfeng%22%2C%22lastName%22%3A%22Shen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jim%22%2C%22lastName%22%3A%22Persinger%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Guang%22%2C%22lastName%22%3A%22Peng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Blaine%22%2C%22lastName%22%3A%22Bartholomew%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Xuetong%22%2C%22lastName%22%3A%22Shen%22%7D%5D%2C%22abstractNote%22%3A%22ATP-dependent%20chromatin%20remodeling%20complexes%20alter%20chromatin%20structure%20through%20interactions%20with%20chromatin%20substrates%20such%20as%20DNA%2C%20histones%2C%20and%20nucleosomes.%20However%2C%20whether%20chromatin%20remodeling%20complexes%20have%20the%20ability%20to%20regulate%20nonchromatin%20substrates%20remains%20unclear.%20Saccharomyces%20cerevisiae%20checkpoint%20kinase%20Mec1%20%28ATR%20in%20mammals%29%20is%20an%20essential%20master%20regulator%20of%20genomic%20integrity.%20Here%20we%20found%20that%20the%20SWI%5C%2FSNF%20chromatin%20remodeling%20complex%20is%20capable%20of%20regulating%20Mec1%20kinase%20activity.%20In%20vivo%2C%20Mec1%20activity%20is%20reduced%20by%20the%20deletion%20of%20Snf2%2C%20the%20core%20ATPase%20subunit%20of%20the%20SWI%5C%2FSNF%20complex.%20SWI%5C%2FSNF%20interacts%20with%20Mec1%2C%20and%20cross-linking%20studies%20revealed%20that%20the%20Snf2%20ATPase%20is%20the%20main%20interaction%20partner%20for%20Mec1.%20In%20vitro%2C%20SWI%5C%2FSNF%20can%20activate%20Mec1%20kinase%20activity%20in%20the%20absence%20of%20chromatin%20or%20known%20activators%20such%20as%20Dpb11.%20The%20subunit%20requirement%20of%20SWI%5C%2FSNF-mediated%20Mec1%20regulation%20differs%20from%20that%20of%20SWI%5C%2FSNF-mediated%20chromatin%20remodeling.%20Functionally%2C%20SWI%5C%2FSNF-mediated%20Mec1%20regulation%20specifically%20occurs%20in%20S%20phase%20of%20the%20cell%20cycle.%20Together%2C%20these%20findings%20identify%20a%20novel%20regulator%20of%20Mec1%20kinase%20activity%20and%20suggest%20that%20ATP-dependent%20chromatin%20remodeling%20complexes%20can%20regulate%20nonchromatin%20substrates%20such%20as%20a%20checkpoint%20kinase.%22%2C%22date%22%3A%222015-3-15%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1101%5C%2Fgad.257626.114%22%2C%22ISSN%22%3A%221549-5477%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22QCWWWSRR%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222014-12-30%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20L.%2C%20Limbo%2C%20O.%2C%20Fei%2C%20J.%2C%20Chen%2C%20L.%2C%20Kim%2C%20B.%2C%20Luo%2C%20J.%2C%20Chong%2C%20J.%2C%20Conaway%2C%20R.%20C.%2C%20Conaway%2C%20J.%20W.%2C%20Ranish%2C%20J.%20A.%2C%20Kadonaga%2C%20J.%20T.%2C%20Russell%2C%20P.%2C%20%26amp%3B%20Wang%2C%20D.%20%282014%29.%20Regulation%20of%20the%20Rhp26ERCC6%5C%2FCSB%20chromatin%20remodeler%20by%20a%20novel%20conserved%20leucine%20latch%20motif.%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America%3C%5C%2Fi%3E%2C%20%3Ci%3E111%3C%5C%2Fi%3E%2852%29%2C%2018566%26%23x2013%3B18571.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1420227112%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1420227112%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DQCWWWSRR%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Regulation%20of%20the%20Rhp26ERCC6%5C%2FCSB%20chromatin%20remodeler%20by%20a%20novel%20conserved%20leucine%20latch%20motif%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Lanfeng%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Oliver%22%2C%22lastName%22%3A%22Limbo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jia%22%2C%22lastName%22%3A%22Fei%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Lu%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Bong%22%2C%22lastName%22%3A%22Kim%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jenny%22%2C%22lastName%22%3A%22Chong%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ronald%20C.%22%2C%22lastName%22%3A%22Conaway%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Joan%20W.%22%2C%22lastName%22%3A%22Conaway%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeff%20A.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22James%20T.%22%2C%22lastName%22%3A%22Kadonaga%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paul%22%2C%22lastName%22%3A%22Russell%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dong%22%2C%22lastName%22%3A%22Wang%22%7D%5D%2C%22abstractNote%22%3A%22CSB%5C%2FERCC6%20%28Cockayne%20syndrome%20B%20protein%5C%2Fexcision%20repair%20cross-complementation%20group%206%29%2C%20a%20member%20of%20a%20subfamily%20of%20SWI2%5C%2FSNF2%20%28SWItch%5C%2Fsucrose%20nonfermentable%29-related%20chromatin%20remodelers%2C%20plays%20crucial%20roles%20in%20gene%20expression%20and%20the%20maintenance%20of%20genome%20integrity.%20Here%2C%20we%20report%20the%20mechanism%20of%20the%20autoregulation%20of%20Rhp26%2C%20which%20is%20the%20homolog%20of%20CSB%5C%2FERCC6%20in%20Schizosaccharomyces%20pombe.%20We%20identified%20a%20novel%20conserved%20protein%20motif%2C%20termed%20the%20%5C%22leucine%20latch%2C%5C%22%20at%20the%20N%20terminus%20of%20Rhp26.%20The%20leucine%20latch%20motif%20mediates%20the%20autoinhibition%20of%20the%20ATPase%20and%20chromatin-remodeling%20activities%20of%20Rhp26%20via%20its%20interaction%20with%20the%20core%20ATPase%20domain.%20Moreover%2C%20we%20found%20that%20the%20C%20terminus%20of%20the%20protein%20counteracts%20this%20autoinhibition%20and%20that%20both%20the%20N-%20and%20C-terminal%20regions%20of%20Rhp26%20are%20needed%20for%20its%20proper%20function%20in%20DNA%20repair%20in%20vivo.%20The%20presence%20of%20the%20leucine%20latch%20motif%20in%20organisms%20ranging%20from%20yeast%20to%20humans%20suggests%20a%20conserved%20mechanism%20for%20the%20autoregulation%20of%20CSB%5C%2FERCC6%20despite%20the%20otherwise%20highly%20divergent%20nature%20of%20the%20N-%20and%20C-terminal%20regions.%22%2C%22date%22%3A%222014-12-30%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1073%5C%2Fpnas.1420227112%22%2C%22ISSN%22%3A%221091-6490%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-05T23%3A15%3A38Z%22%7D%7D%2C%7B%22key%22%3A%22FTMS8TUJ%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Han%20et%20al.%22%2C%22parsedDate%22%3A%222014-11-03%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EHan%2C%20Y.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Hahn%2C%20S.%20%282014%29.%20Architecture%20of%20the%20Saccharomyces%20cerevisiae%20SAGA%20transcription%20coactivator%20complex.%20%3Ci%3EThe%20EMBO%20Journal%3C%5C%2Fi%3E%2C%20%3Ci%3E33%3C%5C%2Fi%3E%2821%29%2C%202534%26%23x2013%3B2546.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.15252%5C%2Fembj.201488638%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.15252%5C%2Fembj.201488638%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DFTMS8TUJ%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Architecture%20of%20the%20Saccharomyces%20cerevisiae%20SAGA%20transcription%20coactivator%20complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yan%22%2C%22lastName%22%3A%22Han%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Hahn%22%7D%5D%2C%22abstractNote%22%3A%22The%20conserved%20transcription%20coactivator%20SAGA%20is%20comprised%20of%20several%20modules%20that%20are%20involved%20in%20activator%20binding%2C%20TBP%20binding%2C%20histone%20acetylation%20%28HAT%29%20and%20deubiquitination%20%28DUB%29.%20Crosslinking%20and%20mass%20spectrometry%2C%20together%20with%20genetic%20and%20biochemical%20analyses%2C%20were%20used%20to%20determine%20the%20molecular%20architecture%20of%20the%20SAGA-TBP%20complex.%20We%20find%20that%20the%20SAGA%20Taf%20and%20Taf-like%20subunits%20form%20a%20TFIID-like%20core%20complex%20at%20the%20center%20of%20SAGA%20that%20makes%20extensive%20interactions%20with%20all%20other%20SAGA%20modules.%20SAGA-TBP%20binding%20involves%20a%20network%20of%20interactions%20between%20subunits%20Spt3%2C%20Spt8%2C%20Spt20%2C%20and%20Spt7.%20The%20HAT%20and%20DUB%20modules%20are%20in%20close%20proximity%2C%20and%20the%20DUB%20module%20modestly%20stimulates%20HAT%20function.%20The%20large%20activator-binding%20subunit%20Tra1%20primarily%20connects%20to%20the%20TFIID-like%20core%20via%20its%20FAT%20domain.%20These%20combined%20results%20were%20used%20to%20derive%20a%20model%20for%20the%20arrangement%20of%20the%20SAGA%20subunits%20and%20its%20interactions%20with%20TBP.%20Our%20results%20provide%20new%20insight%20into%20SAGA%20function%20in%20gene%20regulation%2C%20its%20structural%20similarity%20with%20TFIID%2C%20and%20functional%20interactions%20between%20the%20SAGA%20modules.%22%2C%22date%22%3A%222014-11-3%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.15252%5C%2Fembj.201488638%22%2C%22ISSN%22%3A%221460-2075%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-05T23%3A03%3A33Z%22%7D%7D%2C%7B%22key%22%3A%22DXVS5JBW%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Taylor%20et%20al.%22%2C%22parsedDate%22%3A%222014-10-23%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ETaylor%2C%20A.%20F.%2C%20Amundsen%2C%20S.%20K.%2C%20Guttman%2C%20M.%2C%20Lee%2C%20K.%20K.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Smith%2C%20G.%20R.%20%282014%29.%20Control%20of%20RecBCD%20enzyme%20activity%20by%20DNA%20binding-%20and%20Chi%20hotspot-dependent%20conformational%20changes.%20%3Ci%3EJournal%20of%20Molecular%20Biology%3C%5C%2Fi%3E%2C%20%3Ci%3E426%3C%5C%2Fi%3E%2821%29%2C%203479%26%23x2013%3B3499.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jmb.2014.07.017%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jmb.2014.07.017%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DDXVS5JBW%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Control%20of%20RecBCD%20enzyme%20activity%20by%20DNA%20binding-%20and%20Chi%20hotspot-dependent%20conformational%20changes%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrew%20F.%22%2C%22lastName%22%3A%22Taylor%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Susan%20K.%22%2C%22lastName%22%3A%22Amundsen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Miklos%22%2C%22lastName%22%3A%22Guttman%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kelly%20K.%22%2C%22lastName%22%3A%22Lee%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Gerald%20R.%22%2C%22lastName%22%3A%22Smith%22%7D%5D%2C%22abstractNote%22%3A%22Faithful%20repair%20of%20DNA%20double-strand%20breaks%20by%20homologous%20recombination%20is%20crucial%20to%20maintain%20functional%20genomes.%20The%20major%20Escherichia%20coli%20pathway%20of%20DNA%20break%20repair%20requires%20RecBCD%20enzyme%2C%20a%20complex%20protein%20machine%20with%20multiple%20activities.%20Upon%20encountering%20a%20Chi%20recombination%20hotspot%20%285%27%20GCTGGTGG%203%27%29%20during%20DNA%20unwinding%2C%20RecBCD%27s%20unwinding%2C%20nuclease%2C%20and%20RecA-loading%20activities%20change%20dramatically%2C%20but%20the%20physical%20basis%20for%20these%20changes%20is%20unknown.%20Here%2C%20we%20identify%2C%20during%20RecBCD%27s%20DNA%20unwinding%2C%20two%20Chi-stimulated%20conformational%20changes%20involving%20RecC.%20One%20produced%20a%20marked%2C%20long-lasting%2C%20Chi-dependent%20increase%20in%20protease%20sensitivity%20of%20a%20small%20patch%2C%20near%20the%20Chi%20recognition%20domain%2C%20on%20the%20solvent-exposed%20RecC%20surface.%20The%20other%20change%20was%20identified%20by%20crosslinking%20of%20an%20artificial%20amino%20acid%20inserted%20in%20this%20RecC%20patch%20to%20RecB.%20Small-angle%20X-ray%20scattering%20analysis%20confirmed%20a%20major%20conformational%20change%20upon%20binding%20of%20DNA%20to%20the%20enzyme%20and%20is%20consistent%20with%20these%20two%20changes.%20We%20propose%20that%2C%20upon%20DNA%20binding%2C%20the%20RecB%20nuclease%20domain%20swings%20from%20one%20side%20of%20RecC%20to%20the%20other%3B%20when%20RecBCD%20encounters%20Chi%2C%20the%20nuclease%20domain%20returns%20to%20its%20initial%20position%20determined%20by%20crystallography%2C%20where%20it%20nicks%20DNA%20exiting%20from%20RecC%20and%20loads%20RecA%20onto%20the%20newly%20generated%203%27-ended%20single-stranded%20DNA%20during%20continued%20unwinding%3B%20a%20crevice%20between%20RecB%20and%20RecC%20increasingly%20narrows%20during%20these%20steps.%20This%20model%20provides%20a%20physical%20basis%20for%20the%20intramolecular%20%5C%22signal%20transduction%5C%22%20from%20Chi%20to%20RecC%20to%20RecD%20to%20RecB%20inferred%20previously%20from%20genetic%20and%20enzymatic%20analyses%2C%20and%20it%20accounts%20for%20the%20enzymatic%20changes%20that%20accompany%20Chi%27s%20stimulation%20of%20recombination.%22%2C%22date%22%3A%222014-10-23%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.jmb.2014.07.017%22%2C%22ISSN%22%3A%221089-8638%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-05T23%3A15%3A19Z%22%7D%7D%2C%7B%22key%22%3A%22GA6K7G3I%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Knutson%20et%20al.%22%2C%22parsedDate%22%3A%222014-09%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKnutson%2C%20B.%20A.%2C%20Luo%2C%20J.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Hahn%2C%20S.%20%282014%29.%20Architecture%20of%20the%20Saccharomyces%20cerevisiae%20RNA%20polymerase%20I%20Core%20Factor%20complex.%20%3Ci%3ENature%20Structural%20%26amp%3B%20Molecular%20Biology%3C%5C%2Fi%3E%2C%20%3Ci%3E21%3C%5C%2Fi%3E%289%29%2C%20810%26%23x2013%3B816.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fnsmb.2873%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fnsmb.2873%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DGA6K7G3I%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Architecture%20of%20the%20Saccharomyces%20cerevisiae%20RNA%20polymerase%20I%20Core%20Factor%20complex%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Bruce%20A.%22%2C%22lastName%22%3A%22Knutson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jie%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jeffrey%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Hahn%22%7D%5D%2C%22abstractNote%22%3A%22Core%20Factor%20%28CF%29%20is%20a%20conserved%20RNA%20polymerase%20%28Pol%29%20I%20general%20transcription%20factor%20comprising%20Rrn6%2C%20Rrn11%20and%20the%20TFIIB-related%20subunit%20Rrn7.%20CF%20binds%20TATA-binding%20protein%20%28TBP%29%2C%20Pol%20I%20and%20the%20regulatory%20factors%20Rrn3%20and%20upstream%20activation%20factor.%20We%20used%20chemical%20cross-linking-MS%20to%20determine%20the%20molecular%20architecture%20of%20CF%20and%20its%20interactions%20with%20TBP.%20The%20CF%20subunits%20assemble%20through%20an%20interconnected%20network%20of%20interactions%20between%20five%20structural%20domains%20that%20are%20conserved%20in%20orthologous%20subunits%20of%20the%20human%20Pol%20I%20factor%20SL1.%20We%20validated%20the%20cross-linking-derived%20model%20through%20a%20series%20of%20genetic%20and%20biochemical%20assays.%20Our%20combined%20results%20show%20the%20architecture%20of%20CF%20and%20the%20functions%20of%20the%20CF%20subunits%20in%20assembly%20of%20the%20complex.%20We%20extend%20these%20findings%20to%20model%20how%20CF%20assembles%20into%20the%20Pol%20I%20preinitiation%20complex%2C%20providing%20new%20insight%20into%20the%20roles%20of%20CF%2C%20TBP%20and%20Rrn3.%22%2C%22date%22%3A%222014-9%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fnsmb.2873%22%2C%22ISSN%22%3A%221545-9985%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-05T23%3A13%3A04Z%22%7D%7D%2C%7B%22key%22%3A%22BD4IAIBB%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kadoch%20et%20al.%22%2C%22parsedDate%22%3A%222013-05-05%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKadoch%2C%20C.%2C%20Hargreaves%2C%20D.%20C.%2C%20Hodges%2C%20C.%2C%20Elias%2C%20L.%2C%20Ho%2C%20L.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Crabtree%2C%20G.%20R.%20%282013%29.%20Proteomic%20and%20bioinformatic%20analysis%20of%20mammalian%20SWI%5C%2FSNF%20complexes%20identifies%20extensive%20roles%20in%20human%20malignancy.%20%3Ci%3ENat%20Genet%3C%5C%2Fi%3E.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DBD4IAIBB%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Proteomic%20and%20bioinformatic%20analysis%20of%20mammalian%20SWI%5C%2FSNF%20complexes%20identifies%20extensive%20roles%20in%20human%20malignancy%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%22%2C%22lastName%22%3A%22Kadoch%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22D.%20C.%22%2C%22lastName%22%3A%22Hargreaves%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%22%2C%22lastName%22%3A%22Hodges%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22L.%22%2C%22lastName%22%3A%22Elias%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22L.%22%2C%22lastName%22%3A%22Ho%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22G.%20R.%22%2C%22lastName%22%3A%22Crabtree%22%7D%5D%2C%22abstractNote%22%3A%22Subunits%20of%20mammalian%20SWI%5C%2FSNF%20%28mSWI%5C%2FSNF%20or%20BAF%29%20complexes%20have%20recently%20been%20implicated%20as%20tumor%20suppressors%20in%20human%20malignancies.%20To%20understand%20the%20full%20extent%20of%20their%20involvement%2C%20we%20conducted%20a%20proteomic%20analysis%20of%20endogenous%20mSWI%5C%2FSNF%20complexes%2C%20which%20identified%20several%20new%20dedicated%2C%20stable%20subunits%20not%20found%20in%20yeast%20SWI%5C%2FSNF%20complexes%2C%20including%20BCL7A%2C%20BCL7B%20and%20BCL7C%2C%20BCL11A%20and%20BCL11B%2C%20BRD9%20and%20SS18.%20Incorporating%20these%20new%20members%2C%20we%20determined%20mSWI%5C%2FSNF%20subunit%20mutation%20frequency%20in%20exome%20and%20whole-genome%20sequencing%20studies%20of%20primary%20human%20tumors.%20Notably%2C%20mSWI%5C%2FSNF%20subunits%20are%20mutated%20in%2019.6%25%20of%20all%20human%20tumors%20reported%20in%2044%20studies.%20Our%20analysis%20suggests%20that%20specific%20subunits%20protect%20against%20cancer%20in%20specific%20tissues.%20In%20addition%2C%20mutations%20affecting%20more%20than%20one%20subunit%2C%20defined%20here%20as%20compound%20heterozygosity%2C%20are%20prevalent%20in%20certain%20cancers.%20Our%20studies%20demonstrate%20that%20mSWI%5C%2FSNF%20is%20the%20most%20frequently%20mutated%20chromatin-regulatory%20complex%20%28CRC%29%20in%20human%20cancer%2C%20exhibiting%20a%20broad%20mutation%20pattern%2C%20similar%20to%20that%20of%20TP53.%20Thus%2C%20proper%20functioning%20of%20polymorphic%20BAF%20complexes%20may%20constitute%20a%20major%20mechanism%20of%20tumor%20suppression.%22%2C%22date%22%3A%222013%20May%205%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22SU8SWDAD%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Sun%20et%20al.%22%2C%22parsedDate%22%3A%222013-03-29%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ESun%2C%20B.%2C%20Utleg%2C%20A.%20G.%2C%20Hu%2C%20Z.%2C%20Qin%2C%20S.%2C%20Keller%2C%20A.%2C%20Lorang%2C%20C.%2C%20Gray%2C%20L.%2C%20Brightman%2C%20A.%2C%20Lee%2C%20D.%2C%20Alexander%2C%20V.%2C%20Ranish%2C%20J.%2C%20Moritz%2C%20R.%20L.%2C%20%26amp%3B%20Hood%2C%20L.%20%282013%29.%20Glycocapture-Assisted%20Global%20Quantitative%20Proteomics%20%28gagQP%29%20Reveals%20Multiorgan%20Responses%20in%20Serum%20Toxicoproteome.%20%3Ci%3EJournal%20of%20Proteome%20Research%3C%5C%2Fi%3E.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DSU8SWDAD%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Glycocapture-Assisted%20Global%20Quantitative%20Proteomics%20%28gagQP%29%20Reveals%20Multiorgan%20Responses%20in%20Serum%20Toxicoproteome%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Sun%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%20G.%22%2C%22lastName%22%3A%22Utleg%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Z.%22%2C%22lastName%22%3A%22Hu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Qin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%22%2C%22lastName%22%3A%22Keller%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%22%2C%22lastName%22%3A%22Lorang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22L.%22%2C%22lastName%22%3A%22Gray%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%22%2C%22lastName%22%3A%22Brightman%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22D.%22%2C%22lastName%22%3A%22Lee%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22V.%22%2C%22lastName%22%3A%22Alexander%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22R.%20L.%22%2C%22lastName%22%3A%22Moritz%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22L.%22%2C%22lastName%22%3A%22Hood%22%7D%5D%2C%22abstractNote%22%3A%22Blood%20is%20an%20ideal%20window%20for%20viewing%20our%20health%20and%20disease%20status.%20Because%20blood%20circulates%20the%20entire%20body%20and%20carries%20secreted%2C%20shed%20and%20excreted%20signature%20proteins%20from%20every%20organ%20and%20tissue%20type%2C%20it%20is%20thus%20possible%20of%20using%20blood%20proteome%20to%20achieve%20a%20comprehensive%20assessment%20of%20multiple-organ%20physiology%20and%20pathology.%20To%20date%2C%20blood%20proteome%20has%20been%20frequently%20examined%20for%20diseases%20of%20individual%20organs%3B%20studies%20on%20compound%20insults%20impacting%20multiple%20organs%20are%2C%20however%2C%20elusive.%20We%20believe%20that%20a%20characterization%20of%20peripheral%20blood%20for%20organ-specific%20proteins%20affords%20a%20powerful%20strategy%20to%20allow%20early%20detection%2C%20staging%20and%20monitoring%20of%20diseases%20and%20their%20treatments%20at%20a%20whole-body%20level.%20In%20this%20paper%20we%20test%20this%20hypothesis%20by%20examining%20a%20mouse%20model%20of%20acetaminophen%20%28APAP%29-induced%20hepatic%20and%20extrahepatic%20toxicity.%20We%20used%20glycocapture-assisted%20global%20quantitative%20proteomics%20%28gagQP%29%20approach%20to%20study%20serum%20proteins%20and%20validated%20our%20results%20using%20Western%20blot.%20We%20discovered%20in%20mouse%20sera%20both%20hepatic%20and%20extrahepatic%20organ-specific%20proteins.%20From%20our%20validation%2C%20selected%20organ-specific%20proteins%20had%20changed%20their%20blood%20concentration%20during%20the%20course%20of%20toxicity%20development%20and%20recovery.%20Interestingly%2C%20the%20peak%20responding%20time%20of%20proteins%20specific%20to%20different%20organs%20varied%20in%20a%20time-course%20study.%20The%20collected%20molecular%20information%20shed%20light%20on%20a%20complex%2C%20dynamic%20yet%20interweaving%2C%20multiorgan-enrolled%20APAP%20toxicity.%20The%20developed%20technique%20as%20well%20as%20the%20identified%20protein%20markers%20is%20translational%20to%20human%20studies.%20We%20hope%20our%20work%20can%20broaden%20the%20utility%20of%20blood%20proteomics%20in%20diagnosis%20and%20research%20of%20the%20whole-body%20response%20to%20pathogenic%20cues.%22%2C%22date%22%3A%222013%20March%2029%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22A5PGIBCS%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Mirzaei%20et%20al.%22%2C%22parsedDate%22%3A%222013-02-26%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EMirzaei%2C%20H.%2C%20Knijnenburg%2C%20T.%20A.%2C%20Kim%2C%20B.%2C%20Robinson%2C%20M.%2C%20Picotti%2C%20P.%2C%20Carter%2C%20G.%20W.%2C%20Li%2C%20S.%2C%20Dilworth%2C%20D.%20J.%2C%20Eng%2C%20J.%20K.%2C%20Aitchison%2C%20J.%20D.%2C%20Shmulevich%2C%20I.%2C%20Galitski%2C%20T.%2C%20Aebersold%2C%20R.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282013%29.%20Systematic%20measurement%20of%20transcription%20factor-DNA%20interactions%20by%20targeted%20mass%20spectrometry%20identifies%20candidate%20gene%20regulatory%20proteins.%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America%3C%5C%2Fi%3E%2C%20%3Ci%3E110%3C%5C%2Fi%3E%289%29%2C%203645%26%23x2013%3B3650.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DA5PGIBCS%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Systematic%20measurement%20of%20transcription%20factor-DNA%20interactions%20by%20targeted%20mass%20spectrometry%20identifies%20candidate%20gene%20regulatory%20proteins%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22H.%22%2C%22lastName%22%3A%22Mirzaei%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22T.%20A.%22%2C%22lastName%22%3A%22Knijnenburg%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Kim%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Robinson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22P.%22%2C%22lastName%22%3A%22Picotti%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22G.%20W.%22%2C%22lastName%22%3A%22Carter%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Li%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22D.%20J.%22%2C%22lastName%22%3A%22Dilworth%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%20K.%22%2C%22lastName%22%3A%22Eng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%20D.%22%2C%22lastName%22%3A%22Aitchison%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22I.%22%2C%22lastName%22%3A%22Shmulevich%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22T.%22%2C%22lastName%22%3A%22Galitski%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22R.%22%2C%22lastName%22%3A%22Aebersold%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Regulation%20of%20gene%20expression%20involves%20the%20orchestrated%20interaction%20of%20a%20large%20number%20of%20proteins%20with%20transcriptional%20regulatory%20elements%20in%20the%20context%20of%20chromatin.%20Our%20understanding%20of%20gene%20regulation%20is%20limited%20by%20the%20lack%20of%20a%20protein%20measurement%20technology%20that%20can%20systematically%20detect%20and%20quantify%20the%20ensemble%20of%20proteins%20associated%20with%20the%20transcriptional%20regulatory%20elements%20of%20specific%20genes.%20Here%2C%20we%20introduce%20a%20set%20of%20selected%20reaction%20monitoring%20%28SRM%29%20assays%20for%20the%20systematic%20measurement%20of%20464%20proteins%20with%20known%20or%20suspected%20roles%20in%20transcriptional%20regulation%20at%20RNA%20polymerase%20II%20transcribed%20promoters%20in%20Saccharomyces%20cerevisiae.%20Measurement%20of%20these%20proteins%20in%20nuclear%20extracts%20by%20SRM%20permitted%20the%20reproducible%20quantification%20of%2042%25%20of%20the%20proteins%20over%20a%20wide%20range%20of%20abundances.%20By%20deploying%20the%20assay%20to%20systematically%20identify%20DNA%20binding%20transcriptional%20regulators%20that%20interact%20with%20the%20environmentally%20regulated%20FLO11%20promoter%20in%20cell%20extracts%2C%20we%20identified%2015%20regulators%20that%20bound%20specifically%20to%20distinct%20regions%20along%20approximately%20600%20bp%20of%20the%20regulatory%20sequence.%20Importantly%2C%20the%20dataset%20includes%20a%20number%20of%20regulators%20that%20have%20been%20shown%20to%20either%20control%20FLO11%20expression%20or%20localize%20to%20these%20regulatory%20regions%20in%20vivo.%20We%20further%20validated%20the%20utility%20of%20the%20approach%20by%20demonstrating%20that%20two%20of%20the%20SRM-identified%20factors%2C%20Mot3%20and%20Azf1%2C%20are%20required%20for%20proper%20FLO11%20expression.%20These%20results%20demonstrate%20the%20utility%20of%20SRM-based%20targeted%20proteomics%20to%20guide%20the%20identification%20of%20gene-specific%20transcriptional%20regulators.%22%2C%22date%22%3A%222013%20February%2026%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22WF8GCIXS%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Akiyoshi%20et%20al.%22%2C%22parsedDate%22%3A%222013%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAkiyoshi%2C%20B.%2C%20Nelson%2C%20C.%20R.%2C%20Duggan%2C%20N.%2C%20Ceto%2C%20S.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Biggins%2C%20S.%20%282013%29.%20The%20Mub1%5C%2FUbr2%20ubiquitin%20ligase%20complex%20regulates%20the%20conserved%20Dsn1%20kinetochore%20protein.%20%3Ci%3EPLoS%20Genet%3C%5C%2Fi%3E%2C%20%3Ci%3E9%3C%5C%2Fi%3E%282%29%2C%20e1003216.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DWF8GCIXS%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20Mub1%5C%2FUbr2%20ubiquitin%20ligase%20complex%20regulates%20the%20conserved%20Dsn1%20kinetochore%20protein%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Akiyoshi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20R.%22%2C%22lastName%22%3A%22Nelson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22N.%22%2C%22lastName%22%3A%22Duggan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Ceto%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Biggins%22%7D%5D%2C%22abstractNote%22%3A%22The%20kinetochore%20is%20the%20macromolecular%20complex%20that%20assembles%20onto%20centromeric%20DNA%20and%20orchestrates%20the%20segregation%20of%20duplicated%20chromosomes.%20More%20than%2060%20components%20make%20up%20the%20budding%20yeast%20kinetochore%2C%20including%20inner%20kinetochore%20proteins%20that%20bind%20to%20centromeric%20chromatin%20and%20outer%20proteins%20that%20directly%20interact%20with%20microtubules.%20However%2C%20little%20is%20known%20about%20how%20these%20components%20assemble%20into%20a%20functional%20kinetochore%20and%20whether%20there%20are%20quality%20control%20mechanisms%20that%20monitor%20kinetochore%20integrity.%20We%20previously%20developed%20a%20method%20to%20isolate%20kinetochore%20particles%20via%20purification%20of%20the%20conserved%20Dsn1%20kinetochore%20protein.%20We%20find%20that%20the%20Mub1%5C%2FUbr2%20ubiquitin%20ligase%20complex%20associates%20with%20kinetochore%20particles%20through%20the%20CENP-C%28Mif2%29%20protein.%20Although%20Mub1%5C%2FUbr2%20are%20not%20stable%20kinetochore%20components%20in%20vivo%2C%20they%20regulate%20the%20levels%20of%20the%20conserved%20outer%20kinetochore%20protein%20Dsn1%20via%20ubiquitylation.%20Strikingly%2C%20a%20deletion%20of%20Mub1%5C%2FUbr2%20restores%20the%20levels%20and%20viability%20of%20a%20mutant%20Dsn1%20protein%2C%20reminiscent%20of%20quality%20control%20systems%20that%20target%20aberrant%20proteins%20for%20degradation.%20Consistent%20with%20this%2C%20Mub1%5C%2FUbr2%20help%20to%20maintain%20viability%20when%20kinetochores%20are%20defective.%20Together%2C%20our%20data%20identify%20a%20previously%20unknown%20regulatory%20mechanism%20for%20the%20conserved%20Dsn1%20kinetochore%20protein.%20We%20propose%20that%20Mub1%5C%2FUbr2%20are%20part%20of%20a%20quality%20control%20system%20that%20monitors%20kinetochore%20integrity%2C%20thus%20ensuring%20genomic%20stability.%22%2C%22date%22%3A%222013%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22AMHJAMBH%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Kloet%20et%20al.%22%2C%22parsedDate%22%3A%222012-08%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKloet%2C%20S.%20L.%2C%20Whiting%2C%20J.%20L.%2C%20Gafken%2C%20P.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Wang%2C%20E.%20H.%20%282012%29.%20Phosphorylation-Dependent%20Regulation%20of%20Cyclin%20D1%20and%20Cyclin%20A%20Gene%20Transcription%20by%20TFIID%20Subunits%20TAF1%20and%20TAF7.%20%3Ci%3EMolecular%20and%20Cellular%20Biology%3C%5C%2Fi%3E%2C%20%3Ci%3E32%3C%5C%2Fi%3E%2816%29%2C%203358%26%23x2013%3B3369.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DAMHJAMBH%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Phosphorylation-Dependent%20Regulation%20of%20Cyclin%20D1%20and%20Cyclin%20A%20Gene%20Transcription%20by%20TFIID%20Subunits%20TAF1%20and%20TAF7%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%20L.%22%2C%22lastName%22%3A%22Kloet%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%20L.%22%2C%22lastName%22%3A%22Whiting%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22P.%22%2C%22lastName%22%3A%22Gafken%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22E.%20H.%22%2C%22lastName%22%3A%22Wang%22%7D%5D%2C%22abstractNote%22%3A%22The%20largest%20transcription%20factor%20IID%20%28TFIID%29%20subunit%2C%20TBP-associated%20factor%201%20%28TAF1%29%2C%20possesses%20protein%20kinase%20and%20histone%20acetyltransferase%20%28HAT%29%20activities.%20Both%20enzymatic%20activities%20are%20essential%20for%20transcription%20from%20a%20subset%20of%20genes%20and%20G%281%29%20progression%20in%20mammalian%20cells.%20TAF7%2C%20another%20TFIID%20subunit%2C%20binds%20TAF1%20and%20inhibits%20TAF1%20HAT%20activity.%20Here%20we%20present%20data%20demonstrating%20that%20disruption%20of%20the%20TAF1%5C%2FTAF7%20interaction%20within%20TFIID%20by%20protein%20phosphorylation%20leads%20to%20activation%20of%20TAF1%20HAT%20activity%20and%20stimulation%20of%20cyclin%20D1%20and%20cyclin%20A%20gene%20transcription.%20Overexpression%20and%20small%20interfering%20RNA%20knockdown%20experiments%20confirmed%20that%20TAF7%20functions%20as%20a%20transcriptional%20repressor%20at%20these%20promoters.%20Release%20of%20TAF7%20from%20TFIID%20by%20TAF1%20phosphorylation%20of%20TAF7%20increased%20TAF1%20HAT%20activity%20and%20elevated%20histone%20H3%20acetylation%20levels%20at%20the%20cyclin%20D1%20and%20cyclin%20A%20promoters.%20Serine-264%20of%20TAF7%20was%20identified%20as%20a%20substrate%20for%20TAF1%20kinase%20activity.%20Using%20TAF7%20S264A%20and%20S264D%20phosphomutants%2C%20we%20determined%20that%20the%20phosphorylation%20state%20of%20TAF7%20at%20S264%20influences%20the%20levels%20of%20cyclin%20D1%20and%20cyclin%20A%20gene%20transcription%20and%20promoter%20histone%20H3%20acetylation.%20Our%20studies%20have%20uncovered%20a%20novel%20function%20for%20the%20TFIID%20subunit%20TAF7%20as%20a%20phosphorylation-dependent%20regulator%20of%20TAF1-catalyzed%20histone%20H3%20acetylation%20at%20the%20cyclin%20D1%20and%20cyclin%20A%20promoters.%22%2C%22date%22%3A%222012%20August%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22XTUEDFSA%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22London%20et%20al.%22%2C%22parsedDate%22%3A%222012-05-22%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELondon%2C%20N.%2C%20Ceto%2C%20S.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Biggins%2C%20S.%20%282012%29.%20Phosphoregulation%20of%20Spc105%20by%20Mps1%20and%20PP1%20regulates%20Bub1%20localization%20to%20kinetochores.%20%3Ci%3ECurr%20Biol%3C%5C%2Fi%3E%2C%20%3Ci%3E22%3C%5C%2Fi%3E%2C%20900%26%23x2013%3B906.%20%3Ca%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cub.2012.03.052%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.cub.2012.03.052%3C%5C%2Fa%3E%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DXTUEDFSA%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Phosphoregulation%20of%20Spc105%20by%20Mps1%20and%20PP1%20regulates%20Bub1%20localization%20to%20kinetochores.%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nitobe%22%2C%22lastName%22%3A%22London%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Steven%22%2C%22lastName%22%3A%22Ceto%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sue%22%2C%22lastName%22%3A%22Biggins%22%7D%5D%2C%22abstractNote%22%3A%22Kinetochores%20are%20the%20macromolecular%20complexes%20that%20interact%20with%20microtubules%20to%20mediate%20chromosome%20segregation.%20Accurate%20segregation%20requires%20that%20kinetochores%20make%20bioriented%20attachments%20to%20microtubules%20from%20opposite%20poles.%20Attachments%20between%20kinetochores%20and%20microtubules%20are%20monitored%20by%20the%20spindle%20checkpoint%2C%20a%20surveillance%20system%20that%20prevents%20anaphase%20until%20every%20pair%20of%20chromosomes%20makes%20proper%20bioriented%20attachments.%20Checkpoint%20activity%20is%20correlated%20with%20the%20recruitment%20of%20checkpoint%20proteins%20to%20the%20kinetochore.%20Mps1%20is%20a%20conserved%20protein%20kinase%20that%20regulates%20segregation%20and%20the%20spindle%20checkpoint%2C%20but%20few%20of%20the%20targets%20that%20mediate%20its%20functions%20have%20been%20identified.%20Here%2C%20we%20show%20that%20Mps1%20is%20the%20major%20kinase%20activity%20that%20copurifies%20with%20budding%20yeast%20kinetochore%20particles%20and%20identify%20the%20conserved%20Spc105%5C%2FKNL-1%5C%2Fblinkin%20kinetochore%20protein%20as%20a%20substrate.%20Phosphorylation%20of%20conserved%20MELT%20motifs%20within%20Spc105%20recruits%20the%20Bub1%20protein%20to%20kinetochores%2C%20and%20this%20is%20reversed%20by%20protein%20phosphatase%20I%20%28PP1%29.%20Spc105%20mutants%20lacking%20Mps1%20phosphorylation%20sites%20are%20defective%20in%20the%20spindle%20checkpoint%20and%20exhibit%20growth%20defects.%20Together%2C%20these%20data%20identify%20Spc105%20as%20a%20key%20target%20of%20the%20Mps1%20kinase%20and%20show%20that%20the%20opposing%20activities%20of%20Mps1%20and%20PP1%20regulate%20the%20kinetochore%20localization%20of%20the%20Bub1%20protein.%22%2C%22date%22%3A%222012%20May%2022%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.cub.2012.03.052%22%2C%22ISSN%22%3A%221879-0445%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22SXE9A868%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Luo%20et%20al.%22%2C%22parsedDate%22%3A%222012-02%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELuo%2C%20J.%2C%20Fishburn%2C%20J.%2C%20Hahn%2C%20S.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282012%29.%20An%20Integrated%20Chemical%20Cross-linking%20and%20Mass%20Spectrometry%20Approach%20to%20Study%20Protein%20Complex%20Architecture%20and%20Function.%20%3Ci%3EMolecular%20%26amp%3B%20Cellular%20Proteomics%26%23x202F%3B%3A%20MCP%3C%5C%2Fi%3E%2C%20%3Ci%3E11%3C%5C%2Fi%3E%282%29%2C%20M111%20008318.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DSXE9A868%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22An%20Integrated%20Chemical%20Cross-linking%20and%20Mass%20Spectrometry%20Approach%20to%20Study%20Protein%20Complex%20Architecture%20and%20Function%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Fishburn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Hahn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Knowledge%20of%20protein%20structures%20and%20protein-protein%20interactions%20is%20essential%20for%20understanding%20biological%20processes.%20Chemical%20cross-linking%20combined%20with%20mass%20spectrometry%20is%20an%20attractive%20approach%20for%20studying%20protein-protein%20interactions%20and%20protein%20structure%2C%20but%20to%20date%20its%20use%20has%20been%20limited%20largely%20by%20low%20yields%20of%20informative%20cross-links%20%28because%20of%20inefficient%20cross-linking%20reactions%29%20and%20by%20the%20difficulty%20of%20confidently%20identifying%20the%20sequences%20of%20cross-linked%20peptide%20pairs%20from%20their%20fragmentation%20spectra.%20Here%20we%20present%20an%20approach%20based%20on%20a%20new%20MS%20labile%20cross-linking%20reagent%2C%20BDRG%20%28biotin-aspartate-Rink-glycine%29%2C%20which%20addresses%20these%20issues.%20BDRG%20incorporates%20a%20biotin%20handle%20%28for%20enrichment%20of%20cross-linked%20peptides%20prior%20to%20MS%20analysis%29%2C%20two%20pentafluorophenyl%20ester%20groups%20that%20react%20with%20peptide%20amines%2C%20and%20a%20labile%20Rink-based%20bond%20between%20the%20pentafluorophenyl%20groups%20that%20allows%20cross-linked%20peptides%20to%20be%20separated%20during%20MS%20and%20confidently%20identified%20by%20database%20searching%20of%20their%20fragmentation%20spectra.%20We%20developed%20a%20protocol%20for%20the%20identification%20of%20BDRG%20cross-linked%20peptides%20derived%20from%20purified%20or%20partially%20purified%20protein%20complexes%2C%20including%20software%20to%20aid%20in%20the%20identification%20of%20different%20classes%20of%20cross-linker-modified%20peptides.%20Importantly%2C%20our%20approach%20permits%20the%20use%20of%20high%20accuracy%20precursor%20mass%20measurements%20to%20verify%20the%20database%20search%20results.%20We%20demonstrate%20the%20utility%20of%20the%20approach%20by%20applying%20it%20to%20purified%20yeast%20TFIIE%2C%20a%20heterodimeric%20transcription%20factor%20complex%2C%20and%20to%20a%20single-step%20affinity-purified%20preparation%20of%20the%2012-subunit%20RNA%20polymerase%20II%20complex.%20The%20results%20show%20that%20the%20method%20is%20effective%20at%20identifying%20cross-linked%20peptides%20derived%20from%20purified%20and%20partially%20purified%20protein%20complexes%20and%20provides%20complementary%20information%20to%20that%20from%20other%20structural%20approaches.%20As%20such%2C%20it%20is%20an%20attractive%20approach%20to%20study%20the%20topology%20of%20protein%20complexes.%22%2C%22date%22%3A%222012%20February%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-07-09T02%3A05%3A23Z%22%7D%7D%2C%7B%22key%22%3A%22SUUNCZBB%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Yan%20et%20al.%22%2C%22parsedDate%22%3A%222011-03%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EYan%2C%20W.%2C%20Luo%2C%20J.%2C%20Robinson%2C%20M.%2C%20Eng%2C%20J.%2C%20Aebersold%2C%20R.%2C%20%26amp%3B%20Ranish%2C%20J.%20%282011%29.%20Index-ion%20Triggered%20MS2%20Ion%20Quantification%3A%20A%20Novel%20Proteomics%20Approach%20for%20Reproducible%20Detection%20and%20Quantification%20of%20Targeted%20Proteins%20in%20Complex%20Mixtures.%20%3Ci%3EMol%20Cell%20Proteomics%3C%5C%2Fi%3E%2C%20%3Ci%3E10%3C%5C%2Fi%3E%283%29%2C%20M110%20005611.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DSUUNCZBB%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Index-ion%20Triggered%20MS2%20Ion%20Quantification%3A%20A%20Novel%20Proteomics%20Approach%20for%20Reproducible%20Detection%20and%20Quantification%20of%20Targeted%20Proteins%20in%20Complex%20Mixtures%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22W.%22%2C%22lastName%22%3A%22Yan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Luo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Robinson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Eng%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22R.%22%2C%22lastName%22%3A%22Aebersold%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%5D%2C%22abstractNote%22%3A%22Biomedical%20research%20requires%20protein%20detection%20technology%20that%20is%20not%20only%20sensitive%20and%20quantitative%2C%20but%20that%20can%20reproducibly%20measure%20any%20set%20of%20proteins%20in%20a%20biological%20system%20in%20a%20high%20throughput%20manner.%20Here%20we%20report%20the%20development%20and%20application%20of%20a%20targeted%20proteomics%20platform%20termed%20index-ion%20triggered%20MS2%20ion%20quantification%20%28iMSTIQ%29%20that%20allows%20reproducible%20and%20accurate%20peptide%20quantification%20in%20complex%20mixtures.%20The%20key%20feature%20of%20iMSTIQ%20is%20an%20approach%20called%20index-ion%20triggered%20analysis%20%28ITA%29%20that%20permits%20the%20reproducible%20acquisition%20of%20full%20MS2%20spectra%20of%20targeted%20peptides%20independent%20of%20their%20ion%20intensities.%20Accurate%20quantification%20is%20achieved%20by%20comparing%20the%20relative%20intensities%20of%20multiple%20pairs%20of%20fragment%20ions%20derived%20from%20isobaric%20targeted%20peptides%20during%20MS2%20analysis.%20Importantly%2C%20the%20method%20takes%20advantage%20of%20the%20favorable%20performance%20characteristics%20of%20the%20LTQ-Orbitrap%2C%20which%20include%20high%20mass%20accuracy%2C%20resolution%2C%20and%20throughput.%20As%20such%20it%20provides%20an%20attractive%20targeted%20proteomics%20tool%20to%20meet%20the%20demands%20of%20systems%20biology%20research%20and%20biomarker%20studies.%22%2C%22date%22%3A%222011%20March%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22DCF9F4WV%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Heldring%20et%20al.%22%2C%22parsedDate%22%3A%222011-02-17%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EHeldring%2C%20N.%2C%20Isaacs%2C%20G.%20D.%2C%20Diehl%2C%20A.%20G.%2C%20Sun%2C%20M.%2C%20Cheung%2C%20E.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Kraus%2C%20W.%20L.%20%282011%29.%20Multiple%20Sequence-Specific%20DNA-Binding%20Proteins%20Mediate%20Estrogen%20Receptor%20Signaling%20through%20a%20Tethering%20Pathway.%20%3Ci%3EMol%20Endocrinol%3C%5C%2Fi%3E.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DDCF9F4WV%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Multiple%20Sequence-Specific%20DNA-Binding%20Proteins%20Mediate%20Estrogen%20Receptor%20Signaling%20through%20a%20Tethering%20Pathway%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22N.%22%2C%22lastName%22%3A%22Heldring%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22G.%20D.%22%2C%22lastName%22%3A%22Isaacs%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%20G.%22%2C%22lastName%22%3A%22Diehl%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Sun%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22E.%22%2C%22lastName%22%3A%22Cheung%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22W.%20L.%22%2C%22lastName%22%3A%22Kraus%22%7D%5D%2C%22abstractNote%22%3A%22The%20indirect%20recruitment%20%28tethering%29%20of%20estrogen%20receptors%20%28ERs%29%20to%20DNA%20through%20other%20DNA-bound%20transcription%20factors%20%28e.g.%20activator%20protein%201%29%20is%20an%20important%20component%20of%20estrogen-signaling%20pathways%2C%20but%20our%20understanding%20of%20the%20mechanisms%20of%20ligand-dependent%20activation%20in%20this%20pathway%20is%20limited.%20Using%20proteomic%2C%20genomic%2C%20and%20gene-specific%20analyses%2C%20we%20demonstrate%20that%20a%20large%20repertoire%20of%20DNA-binding%20transcription%20factors%20contribute%20to%20estrogen%20signaling%20through%20the%20tethering%20pathway.%20In%20addition%2C%20we%20define%20a%20set%20of%20endogenous%20genes%20for%20which%20ERalpha%20tethering%20through%20activator%20protein%201%20%28e.g.%20c-Fos%29%20and%20cAMP%20response%20element-binding%20protein%20family%20members%20mediates%20estrogen%20responsiveness.%20Finally%2C%20we%20show%20that%20functional%20interplay%20between%20c-Fos%20and%20cAMP%20response%20element-binding%20protein%201%20contributes%20to%20estrogen-dependent%20regulation%20through%20the%20tethering%20pathway.%20Based%20on%20our%20results%2C%20we%20conclude%20that%20ERalpha%20recruitment%20in%20the%20tethering%20pathway%20is%20dependent%20on%20the%20ligand-induced%20formation%20of%20transcription%20factor%20complexes%20that%20involves%20interplay%20between%20the%20transcription%20factors%20from%20different%20protein%20families.%22%2C%22date%22%3A%222011%20February%2017%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22PBW8V24R%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Himeda%20et%20al.%22%2C%22parsedDate%22%3A%222010-07%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EHimeda%2C%20C.%20L.%2C%20Ranish%2C%20J.%2C%20Pearson%2C%20R.%20C.%2C%20Crossley%2C%20M.%2C%20%26amp%3B%20Hauschka%2C%20S.%20D.%20%282010%29.%20KLF3%20regulates%20muscle-specific%20gene%20expression%20and%20synergizes%20with%20serum%20response%20factor%20on%20KLF%20binding%20sites.%20%3Ci%3EMol%20Cell%20Biol%3C%5C%2Fi%3E%2C%20%3Ci%3E30%3C%5C%2Fi%3E%2814%29%2C%203430%26%23x2013%3B3443.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DPBW8V24R%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22KLF3%20regulates%20muscle-specific%20gene%20expression%20and%20synergizes%20with%20serum%20response%20factor%20on%20KLF%20binding%20sites%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20L.%22%2C%22lastName%22%3A%22Himeda%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22R.%20C.%22%2C%22lastName%22%3A%22Pearson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Crossley%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%20D.%22%2C%22lastName%22%3A%22Hauschka%22%7D%5D%2C%22abstractNote%22%3A%22This%20study%20identifies%20KLF3%20as%20a%20transcriptional%20regulator%20of%20muscle%20genes%20and%20reveals%20a%20novel%20synergistic%20interaction%20between%20KLF3%20and%20serum%20response%20factor%20%28SRF%29.%20Using%20quantitative%20proteomics%2C%20KLF3%20was%20identified%20as%20one%20of%20several%20candidate%20factors%20that%20recognize%20the%20MPEX%20control%20element%20in%20the%20Muscle%20creatine%20kinase%20%28MCK%29%20promoter.%20Chromatin%20immunoprecipitation%20analysis%20indicated%20that%20KLF3%20is%20enriched%20at%20many%20muscle%20gene%20promoters%20%28MCK%2C%20Myosin%20heavy%20chain%20IIa%2C%20Six4%2C%20Calcium%20channel%20receptor%20alpha-1%2C%20and%20Skeletal%20alpha-actin%29%2C%20and%20two%20KLF3%20isoforms%20are%20upregulated%20during%20muscle%20differentiation.%20KLF3%20and%20SRF%20physically%20associate%20and%20synergize%20in%20transactivating%20the%20MCK%20promoter%20independently%20of%20SRF%20binding%20to%20CArG%20motifs.%20The%20zinc%20finger%20and%20repression%20domains%20of%20KLF3%20plus%20the%20MADS%20box%20and%20transcription%20activation%20domain%20of%20SRF%20are%20implicated%20in%20this%20synergy.%20Our%20results%20provide%20the%20first%20evidence%20of%20a%20role%20for%20KLF3%20in%20muscle%20gene%20regulation%20and%20reveal%20an%20alternate%20mechanism%20for%20transcriptional%20regulation%20by%20SRF%20via%20its%20recruitment%20to%20KLF%20binding%20sites.%20Since%20both%20factors%20are%20expressed%20in%20all%20muscle%20lineages%2C%20SRF%20may%20regulate%20many%20striated-%20and%20smooth-muscle%20genes%20that%20lack%20known%20SRF%20control%20elements%2C%20thus%20further%20expanding%20the%20breadth%20of%20the%20emerging%20CArGome.%22%2C%22date%22%3A%222010%20July%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22ESU89MVS%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Gillespie%20et%20al.%22%2C%22parsedDate%22%3A%222009-12-28%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EGillespie%2C%20M.%20A.%2C%20Le%20Grand%2C%20F.%2C%20Scime%2C%20A.%2C%20Kuang%2C%20S.%2C%20von%20Maltzahn%2C%20J.%2C%20Seale%2C%20V.%2C%20Cuenda%2C%20A.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Rudnicki%2C%20M.%20A.%20%282009%29.%20p38-gamma-dependent%20gene%20silencing%20restricts%20entry%20into%20the%20myogenic%20differentiation%20program.%20%3Ci%3EJ%20Cell%20Biol%3C%5C%2Fi%3E%2C%20%3Ci%3E187%3C%5C%2Fi%3E%287%29%2C%20991%26%23x2013%3B1005.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DESU89MVS%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22p38-gamma-dependent%20gene%20silencing%20restricts%20entry%20into%20the%20myogenic%20differentiation%20program%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%20A.%22%2C%22lastName%22%3A%22Gillespie%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22F.%22%2C%22lastName%22%3A%22Le%20Grand%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%22%2C%22lastName%22%3A%22Scime%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Kuang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22von%20Maltzahn%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22V.%22%2C%22lastName%22%3A%22Seale%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%22%2C%22lastName%22%3A%22Cuenda%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%20A.%22%2C%22lastName%22%3A%22Rudnicki%22%7D%5D%2C%22abstractNote%22%3A%22The%20mitogen-activated%20protein%20kinase%20p38-gamma%20is%20highly%20expressed%20in%20skeletal%20muscle%20and%20is%20associated%20with%20the%20dystrophin%20glycoprotein%20complex%3B%20however%2C%20its%20function%20remains%20unclear.%20After%20induced%20damage%2C%20muscle%20in%20mice%20lacking%20p38-gamma%20generated%20significantly%20fewer%20myofibers%20than%20wild-type%20muscle.%20Notably%2C%20p38-gamma-deficient%20muscle%20contained%2050%25%20fewer%20satellite%20cells%20that%20exhibited%20premature%20Myogenin%20expression%20and%20markedly%20reduced%20proliferation.%20We%20determined%20that%20p38-gamma%20directly%20phosphorylated%20MyoD%20on%20Ser199%20and%20Ser200%2C%20which%20results%20in%20enhanced%20occupancy%20of%20MyoD%20on%20the%20promoter%20of%20myogenin%20together%20with%20markedly%20decreased%20transcriptional%20activity.%20This%20repression%20is%20associated%20with%20extensive%20methylation%20of%20histone%20H3K9%20together%20with%20recruitment%20of%20the%20KMT1A%20methyltransferase%20to%20the%20myogenin%20promoter.%20Notably%2C%20a%20MyoD%20S199A%5C%2FS200A%20mutant%20exhibits%20markedly%20reduced%20binding%20to%20KMT1A.%20Therefore%2C%20p38-gamma%20signaling%20directly%20induces%20the%20assembly%20of%20a%20repressive%20MyoD%20transcriptional%20complex.%20Together%2C%20these%20results%20establish%20a%20hitherto%20unappreciated%20and%20essential%20role%20for%20p38-gamma%20signaling%20in%20positively%20regulating%20the%20expansion%20of%20transient%20amplifying%20myogenic%20precursor%20cells%20during%20muscle%20growth%20and%20regeneration.%22%2C%22date%22%3A%222009%20December%2028%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%22VUAV9HKB%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Akiyoshi%20et%20al.%22%2C%22parsedDate%22%3A%222009-12-15%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAkiyoshi%2C%20B.%2C%20Nelson%2C%20C.%20R.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Biggins%2C%20S.%20%282009%29.%20Quantitative%20proteomic%20analysis%20of%20purified%20yeast%20kinetochores%20identifies%20a%20PP1%20regulatory%20subunit.%20%3Ci%3EGenes%20Dev%3C%5C%2Fi%3E%2C%20%3Ci%3E23%3C%5C%2Fi%3E%2824%29%2C%202887%26%23x2013%3B2899.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3DVUAV9HKB%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Quantitative%20proteomic%20analysis%20of%20purified%20yeast%20kinetochores%20identifies%20a%20PP1%20regulatory%20subunit%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Akiyoshi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20R.%22%2C%22lastName%22%3A%22Nelson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Biggins%22%7D%5D%2C%22abstractNote%22%3A%22The%20kinetochore%20is%20a%20macromolecular%20complex%20that%20controls%20chromosome%20segregation%20and%20cell%20cycle%20progression.%20When%20sister%20kinetochores%20make%20bioriented%20attachments%20to%20microtubules%20from%20opposite%20poles%2C%20the%20spindle%20checkpoint%20is%20silenced.%20Biorientation%20and%20the%20spindle%20checkpoint%20are%20regulated%20by%20a%20balance%20between%20the%20Ipl1%5C%2FAurora%20B%20protein%20kinase%20and%20the%20opposing%20activity%20of%20protein%20phosphatase%20I%20%28PP1%29.%20However%2C%20little%20is%20known%20about%20the%20regulation%20of%20PP1%20localization%20and%20activity%20at%20the%20kinetochore.%20Here%2C%20we%20developed%20a%20method%20to%20purify%20centromere-bound%20kinetochores%20and%20used%20quantitative%20proteomics%20to%20identify%20the%20Fin1%20protein%20as%20a%20PP1%20regulatory%20subunit.%20The%20Fin1%5C%2FPP1%20complex%20is%20regulated%20by%20phosphorylation%20and%2014-3-3%20protein%20binding.%20When%20Fin1%20is%20mislocalized%2C%20bipolar%20spindles%20fail%20to%20assemble%20but%20the%20spindle%20checkpoint%20is%20inappropriately%20silenced%20due%20to%20PP1%20activity.%20These%20data%20suggest%20that%20Fin1%20is%20a%20PP1%20regulatory%20subunit%20whose%20spatial%20and%20temporal%20activity%20must%20be%20precisely%20controlled%20to%20ensure%20genomic%20stability.%22%2C%22date%22%3A%222009%20December%2015%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%2C%7B%22key%22%3A%224S4G862N%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Akiyoshi%20et%20al.%22%2C%22parsedDate%22%3A%222009-12%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAkiyoshi%2C%20B.%2C%20Nelson%2C%20C.%20R.%2C%20Ranish%2C%20J.%2C%20%26amp%3B%20Biggins%2C%20S.%20%282009%29.%20Analysis%20of%20Ipl1-mediated%20phosphorylation%20of%20the%20Ndc80%20kinetochore%20protein%20in%20Saccharomyces%20cerevisiae.%20%3Ci%3EGenetics%3C%5C%2Fi%3E%2C%20%3Ci%3E183%3C%5C%2Fi%3E%284%29%2C%201591%26%23x2013%3B1595.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D4S4G862N%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Analysis%20of%20Ipl1-mediated%20phosphorylation%20of%20the%20Ndc80%20kinetochore%20protein%20in%20Saccharomyces%20cerevisiae%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22B.%22%2C%22lastName%22%3A%22Akiyoshi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20R.%22%2C%22lastName%22%3A%22Nelson%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22S.%22%2C%22lastName%22%3A%22Biggins%22%7D%5D%2C%22abstractNote%22%3A%22Phosphorylation%20of%20the%20Ndc80%20kinetochore%20protein%20by%20the%20Ipl1%5C%2FAurora%20B%20kinase%20reduces%20its%20microtubule%20binding%20activity%20in%20vitro.%20We%20found%20that%20kinetochore-bound%20Ndc80%20is%20phosphorylated%20on%20Ipl1%20sites%20in%20vivo%2C%20but%20this%20phosphorylation%20is%20not%20essential.%20Instead%2C%20we%20show%20that%20additional%20Ipl1%20targets%20contribute%20to%20segregation%20and%20the%20spindle%20checkpoint.%22%2C%22date%22%3A%222009%20December%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222024-07-09T02%3A08%3A42Z%22%7D%7D%2C%7B%22key%22%3A%2233JWG4GU%22%2C%22library%22%3A%7B%22id%22%3A2323737%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Chaturvedi%20et%20al.%22%2C%22parsedDate%22%3A%222009-10-27%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%202%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EChaturvedi%2C%20C.%20P.%2C%20Hosey%2C%20A.%20M.%2C%20Palii%2C%20C.%2C%20Perez-Iratxeta%2C%20C.%2C%20Nakatani%2C%20Y.%2C%20Ranish%2C%20J.%2C%20Dilworth%2C%20F.%20J.%2C%20%26amp%3B%20Brand%2C%20M.%20%282009%29.%20Dual%20role%20for%20the%20methyltransferase%20G9a%20in%20the%20maintenance%20of%20beta-globin%20gene%20transcription%20in%20adult%20erythroid%20cells.%20%3Ci%3EProc%20Natl%20Acad%20Sci%20U%20S%20A%3C%5C%2Fi%3E%2C%20%3Ci%3E106%3C%5C%2Fi%3E%2843%29%2C%2018303%26%23x2013%3B18308.%20%3Ca%20title%3D%27Cite%20in%20RIS%20Format%27%20class%3D%27zp-CiteRIS%27%20href%3D%27https%3A%5C%2F%5C%2Franish.isbscience.org%5C%2Fwp-content%5C%2Fplugins%5C%2Fzotpress%5C%2Flib%5C%2Frequest%5C%2Frequest.cite.php%3Fapi_user_id%3D2323737%26amp%3Bitem_key%3D33JWG4GU%27%3ECite%3C%5C%2Fa%3E%20%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Dual%20role%20for%20the%20methyltransferase%20G9a%20in%20the%20maintenance%20of%20beta-globin%20gene%20transcription%20in%20adult%20erythroid%20cells%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%20P.%22%2C%22lastName%22%3A%22Chaturvedi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22A.%20M.%22%2C%22lastName%22%3A%22Hosey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%22%2C%22lastName%22%3A%22Palii%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C.%22%2C%22lastName%22%3A%22Perez-Iratxeta%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Y.%22%2C%22lastName%22%3A%22Nakatani%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J.%22%2C%22lastName%22%3A%22Ranish%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22F.%20J.%22%2C%22lastName%22%3A%22Dilworth%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M.%22%2C%22lastName%22%3A%22Brand%22%7D%5D%2C%22abstractNote%22%3A%22Using%20a%20proteomics%20screen%2C%20we%20have%20identified%20the%20methyltransferase%20G9a%20as%20an%20interacting%20partner%20of%20the%20hematopoietic%20activator%20NF-E2.%20We%20show%20that%20G9a%20is%20recruited%20to%20the%20beta-globin%20locus%20in%20a%20NF-E2-dependent%20manner%20and%20spreads%20over%20the%20entire%20locus.%20While%20G9a%20is%20often%20regarded%20as%20a%20corepressor%2C%20knocking%20down%20this%20protein%20in%20differentiating%20adult%20erythroid%20cells%20leads%20to%20repression%20of%20the%20adult%20beta%28maj%29%20globin%20gene%20and%20aberrant%20reactivation%20of%20the%20embryonic%20beta-like%20globin%20gene%20E%28y%29.%20While%20in%20adult%20cells%20G9a%20maintains%20E%28y%29%20in%20a%20repressed%20state%20via%20dimethylation%20of%20histone%20H3%20at%20lysines%209%20and%2027%2C%20it%20activates%20beta%28maj%29%20transcription%20in%20a%20methyltransferase-independent%20manner.%20Interestingly%2C%20the%20demethylase%20UTX%20is%20recruited%20to%20the%20beta%28maj%29%20%28but%20not%20the%20E%28y%29%29%20promoter%20where%20it%20antagonizes%20G9a-dependent%20H3K27%20dimethylation.%20Collectively%2C%20these%20results%20reveal%20a%20dual%20role%20for%20G9a%20in%20maintaining%20proper%20expression%20%28both%20repression%20and%20activation%29%20of%20the%20beta-globin%20genes%20in%20differentiating%20adult%20erythroid%20cells.%22%2C%22date%22%3A%222009%20October%2027%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%22%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%222RQKSFR5%22%5D%2C%22dateModified%22%3A%222016-02-09T00%3A19%3A05Z%22%7D%7D%5D%7D
Luo, J., & Ranish, J. (2024). Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. ELife, 13. https://doi.org/10.7554/eLife.99809.2 Cite Download
Kopp, A., Nissa, M. U., Dollinger, R., Ranish, J., & Brand, M. (2024). 3106 – PROTEOMICS AND GENOMICS STUDIES REVEALED A NEW ROLE FOR MLL PARTIAL TANDEM DUPLICATION (PTD) IN MYELODYSPLASTIC SYNDROME (MDS) AND ACUTE MYELOID LEUKEMIA (AML). Experimental Hematology, 137, 104428. https://doi.org/10.1016/j.exphem.2024.104428 Cite
Yang, Z., Mameri, A., Cattoglio, C., Lachance, C., Florez Ariza, A. J., Luo, J., Humbert, J., Sudarshan, D., Banerjea, A., Galloy, M., Fradet-Turcotte, A., Lambert, J.-P., Ranish, J. A., Côté, J., & Nogales, E. (2024). Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. Science (New York, N.Y.), eadl5816. https://doi.org/10.1126/science.adl5816 Cite
Saha, D., Hailu, S., Hada, A., Lee, J., Luo, J., Ranish, J. A., Lin, Y.-C., Feola, K., Persinger, J., Jain, A., Liu, B., Lu, Y., Sen, P., & Bartholomew, B. (2023). The AT-hook is an evolutionarily conserved auto-regulatory domain of SWI/SNF required for cell lineage priming. Nature Communications, 14(1), 4682. https://doi.org/10.1038/s41467-023-40386-8 Cite Download
Luo, J., & Ranish, J. (2022). Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes. bioRxiv. https://doi.org/10.1101/2022.12.02.518925 Cite Download
Bassett, J., Rimel, J. K., Basu, S., Basnet, P., Luo, J., Engel, K. L., Nagel, M., Woyciehowsky, A., Ebmeier, C. C., Kaplan, C. D., Taatjes, D. J., & Ranish, J. A. (2022). Systematic mutagenesis of TFIIH subunit p52/Tfb2 identifies residues required for XPB/Ssl2 subunit function and genetic interactions with TFB6. The Journal of Biological Chemistry, 298(10), 102433. https://doi.org/10.1016/j.jbc.2022.102433 Cite Download
Danileviciute, E., Zeng, N., Capelle, C. M., Paczia, N., Gillespie, M. A., Kurniawan, H., Benzarti, M., Merz, M. P., Coowar, D., Fritah, S., Vogt Weisenhorn, D. M., Gomez Giro, G., Grusdat, M., Baron, A., Guerin, C., Franchina, D. G., Léonard, C., Domingues, O., Delhalle, S., … Hefeng, F. Q. (2022). PARK7/DJ-1 promotes pyruvate dehydrogenase activity and maintains Treg homeostasis during ageing. Nature Metabolism, 4(5), 589–607. https://doi.org/10.1038/s42255-022-00576-y Cite
Scheer, E., Luo, J., Bernardini, A., Ruffenach, F., Garnier, J.-M., Kolb-Cheynel, I., Gupta, K., Berger, I., Ranish, J., & Tora, L. (2021). TAF8 regions important for TFIID lobe B assembly or for TAF2 interactions are required for embryonic stem cell survival. The Journal of Biological Chemistry, 101288. https://doi.org/10.1016/j.jbc.2021.101288 Cite
Brand, M., & Ranish, J. A. (2021). Proteomic/transcriptomic analysis of erythropoiesis. Current Opinion in Hematology, 28(3), 150–157. https://doi.org/10.1097/MOH.0000000000000647 Cite
Jensen, B. C., Phan, I. Q., McDonald, J. R., Sur, A., Gillespie, M. A., Ranish, J. A., Parsons, M., & Myler, P. J. (2021). Chromatin-Associated Protein Complexes Link DNA Base J and Transcription Termination in Leishmania. MSphere, 6(1). https://doi.org/10.1128/mSphere.01204-20 Cite
Kim, M. K., Tranvo, A., Hurlburt, A. M., Verma, N., Phan, P., Luo, J., Ranish, J., & Stumph, W. E. (2020). Assembly of SNAPc, Bdp1, and TBP on the U6 snRNA Gene Promoter in Drosophila melanogaster. Molecular and Cellular Biology, 40(12). https://doi.org/10.1128/MCB.00641-19 Cite
Gillespie, M. A., Palii, C. G., Sanchez-Taltavull, D., Perkins, T. J., Brand, M., & Ranish, J. A. (2020). Absolute quantification of transcription factors in human erythropoiesis using selected reaction monitoring mass spectrometry. STAR Protocols, 1(3), 100216. https://doi.org/10.1016/j.xpro.2020.100216 Cite
Wenderski, W., Wang, L., Krokhotin, A., Walsh, J. J., Li, H., Shoji, H., Ghosh, S., George, R. D., Miller, E. L., Elias, L., Gillespie, M. A., Son, E. Y., Staahl, B. T., Baek, S. T., Stanley, V., Moncada, C., Shipony, Z., Linker, S. B., Marchetto, M. C. N., … Gleeson, J. G. (2020). Loss of the neural-specific BAF subunit ACTL6B relieves repression of early response genes and causes recessive autism. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.1908238117 Cite Download
Gillespie, M. A., Palii, C. G., Sanchez-Taltavull, D., Shannon, P., Longabaugh, W. J. R., Downes, D. J., Sivaraman, K., Espinoza, H. M., Hughes, J. R., Price, N. D., Perkins, T. J., Ranish, J. A., & Brand, M. (2020). Absolute Quantification of Transcription Factors Reveals Principles of Gene Regulation in Erythropoiesis. Molecular Cell, 78(5), 960-974.e11. https://doi.org/10.1016/j.molcel.2020.03.031 Cite Download
Mashtalir, N., Suzuki, H., Farrell, D. P., Sankar, A., Luo, J., Filipovski, M., D’Avino, A. R., St Pierre, R., Valencia, A. M., Onikubo, T., Roeder, R. G., Han, Y., He, Y., Ranish, J. A., DiMaio, F., Walz, T., & Kadoch, C. (2020). A Structural Model of the Endogenous Human BAF Complex Informs Disease Mechanisms. Cell, 183(3), 802-817.e24. https://doi.org/10.1016/j.cell.2020.09.051 Cite
Patel, A. B., Moore, C. M., Greber, B. J., Luo, J., Zukin, S. A., Ranish, J., & Nogales, E. (2019). Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement. ELife, 8. https://doi.org/10.7554/eLife.54449 Cite Download
Hada, A., Hota, S. K., Luo, J., Lin, Y.-C., Kale, S., Shaytan, A. K., Bhardwaj, S. K., Persinger, J., Ranish, J., Panchenko, A. R., & Bartholomew, B. (2019). Histone Octamer Structure Is Altered Early in ISW2 ATP-Dependent Nucleosome Remodeling. Cell Reports, 28(1), 282-294.e6. https://doi.org/10.1016/j.celrep.2019.05.106 Cite Download
Luo, J., Bassett, J., & Ranish, J. (2019). Identification of Cross-linked Peptides Using Isotopomeric Cross-linkers. Journal of the American Society for Mass Spectrometry. https://doi.org/10.1007/s13361-019-02253-z Cite
Palii, C. G., Cheng, Q., Gillespie, M. A., Shannon, P., Mazurczyk, M., Napolitani, G., Price, N. D., Ranish, J. A., Morrissey, E., Higgs, D. R., & Brand, M. (2019). Single-Cell Proteomics Reveal that Quantitative Changes in Co-expressed Lineage-Specific Transcription Factors Determine Cell Fate. Cell Stem Cell, 24(5), 812-820.e5. https://doi.org/10.1016/j.stem.2019.02.006 Cite
Patel, A. B., Louder, R. K., Greber, B. J., Grünberg, S., Luo, J., Fang, J., Liu, Y., Ranish, J., Hahn, S., & Nogales, E. (2018). Structure of human TFIID and mechanism of TBP loading onto promoter DNA. Science (New York, N.Y.), 362(6421). https://doi.org/10.1126/science.aau8872 Cite
Kolesnikova, O., Ben-Shem, A., Luo, J., Ranish, J., Schultz, P., & Papai, G. (2018). Molecular structure of promoter-bound yeast TFIID. Nature Communications, 9(1), 4666. https://doi.org/10.1038/s41467-018-07096-y Cite Download
Mashtalir, N., D’Avino, A. R., Michel, B. C., Luo, J., Pan, J., Otto, J. E., Zullow, H. J., McKenzie, Z. M., Kubiak, R. L., Pierre, R. S., Valencia, A. M., Poynter, S. J., Cassel, S. H., Ranish, J. A., & Kadoch, C. (2018). Modular Organization and Assembly of SWI/SNF Family Chromatin Remodeling Complexes. Cell, 175(5), 1272-1288.e20. https://doi.org/10.1016/j.cell.2018.09.032 Cite
Tuttle, L. M., Pacheco, D., Warfield, L., Luo, J., Ranish, J., Hahn, S., & Klevit, R. E. (2018). Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex. Cell Reports, 22(12), 3251–3264. https://doi.org/10.1016/j.celrep.2018.02.097 Cite
Pacheco, D., Warfield, L., Brajcich, M., Robbins, H., Luo, J., Ranish, J., & Hahn, S. (2018). Transcription activation domains of the yeast factors Met4 and Ino2: tandem activation domains with properties similar to the yeast Gcn4 activator. Molecular and Cellular Biology. https://doi.org/10.1128/MCB.00038-18 Cite
Turkarslan, S., Raman, A. V., Thompson, A. W., Arens, C. E., Gillespie, M. A., von Netzer, F., Hillesland, K. L., Stolyar, S., López García de Lomana, A., Reiss, D. J., Gorman-Lewis, D., Zane, G. M., Ranish, J. A., Wall, J. D., Stahl, D. A., & Baliga, N. S. (2017). Mechanism for microbial population collapse in a fluctuating resource environment. Molecular Systems Biology, 13(3), 919. Cite
Sen, P., Luo, J., Hada, A., Hailu, S. G., Dechassa, M. L., Persinger, J., Brahma, S., Paul, S., Ranish, J., & Bartholomew, B. (2017). Loss of Snf5 Induces Formation of an Aberrant SWI/SNF Complex. Cell Reports, 18(9), 2135–2147. https://doi.org/10.1016/j.celrep.2017.02.017 Cite
Nakayama, R. T., Pulice, J. L., Valencia, A. M., McBride, M. J., McKenzie, Z. M., Gillespie, M. A., Ku, W. L., Teng, M., Cui, K., Williams, R. T., Cassel, S. H., Qing, H., Widmer, C. J., Demetri, G. D., Irizarry, R. A., Zhao, K., Ranish, J. A., & Kadoch, C. (2017). SMARCB1 is required for widespread BAF complex-mediated activation of enhancers and bivalent promoters. Nature Genetics. https://doi.org/10.1038/ng.3958 Cite
McDermott, S. M., Luo, J., Carnes, J., Ranish, J. A., & Stuart, K. (2016). The Architecture of Trypanosoma brucei editosomes. Proceedings of the National Academy of Sciences of the United States of America, 113(42), E6476–E6485. https://doi.org/10.1073/pnas.1610177113 Cite
Warfield, L., Luo, J., Ranish, J., & Hahn, S. (2016). Function of conserved topological regions within the S. cerevisiae basal transcription factor TFIIH. Molecular and Cellular Biology. https://doi.org/10.1128/MCB.00182-16 Cite
Luo, J., Cimermancic, P., Viswanath, S., Ebmeier, C. C., Kim, B., Dehecq, M., Raman, V., Greenberg, C. H., Pellarin, R., Sali, A., Taatjes, D. J., Hahn, S., & Ranish, J. (2015). Architecture of the Human and Yeast General Transcription and DNA Repair Factor TFIIH. Molecular Cell, 59, 794–806. https://doi.org/10.1016/j.molcel.2015.07.016 Cite
Gillespie, M. A., Gold, E. S., Ramsey, S. A., Podolsky, I., Aderem, A., & Ranish, J. A. (2015). An LXR-NCOA5 gene regulatory complex directs inflammatory crosstalk-dependent repression of macrophage cholesterol efflux. The EMBO Journal, 34(9), 1244–1258. https://doi.org/10.15252/embj.201489819 Cite
Kapoor, P., Bao, Y., Xiao, J., Luo, J., Shen, J., Persinger, J., Peng, G., Ranish, J., Bartholomew, B., & Shen, X. (2015). Regulation of Mec1 kinase activity by the SWI/SNF chromatin remodeling complex. Genes & Development, 29(6), 591–602. https://doi.org/10.1101/gad.257626.114 Cite
Wang, L., Limbo, O., Fei, J., Chen, L., Kim, B., Luo, J., Chong, J., Conaway, R. C., Conaway, J. W., Ranish, J. A., Kadonaga, J. T., Russell, P., & Wang, D. (2014). Regulation of the Rhp26ERCC6/CSB chromatin remodeler by a novel conserved leucine latch motif. Proceedings of the National Academy of Sciences of the United States of America, 111(52), 18566–18571. https://doi.org/10.1073/pnas.1420227112 Cite
Han, Y., Luo, J., Ranish, J., & Hahn, S. (2014). Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex. The EMBO Journal, 33(21), 2534–2546. https://doi.org/10.15252/embj.201488638 Cite
Taylor, A. F., Amundsen, S. K., Guttman, M., Lee, K. K., Luo, J., Ranish, J., & Smith, G. R. (2014). Control of RecBCD enzyme activity by DNA binding- and Chi hotspot-dependent conformational changes. Journal of Molecular Biology, 426(21), 3479–3499. https://doi.org/10.1016/j.jmb.2014.07.017 Cite
Knutson, B. A., Luo, J., Ranish, J., & Hahn, S. (2014). Architecture of the Saccharomyces cerevisiae RNA polymerase I Core Factor complex. Nature Structural & Molecular Biology, 21(9), 810–816. https://doi.org/10.1038/nsmb.2873 Cite
Kadoch, C., Hargreaves, D. C., Hodges, C., Elias, L., Ho, L., Ranish, J., & Crabtree, G. R. (2013). Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes identifies extensive roles in human malignancy. Nat Genet. Cite
Sun, B., Utleg, A. G., Hu, Z., Qin, S., Keller, A., Lorang, C., Gray, L., Brightman, A., Lee, D., Alexander, V., Ranish, J., Moritz, R. L., & Hood, L. (2013). Glycocapture-Assisted Global Quantitative Proteomics (gagQP) Reveals Multiorgan Responses in Serum Toxicoproteome. Journal of Proteome Research. Cite
Mirzaei, H., Knijnenburg, T. A., Kim, B., Robinson, M., Picotti, P., Carter, G. W., Li, S., Dilworth, D. J., Eng, J. K., Aitchison, J. D., Shmulevich, I., Galitski, T., Aebersold, R., & Ranish, J. (2013). Systematic measurement of transcription factor-DNA interactions by targeted mass spectrometry identifies candidate gene regulatory proteins. Proceedings of the National Academy of Sciences of the United States of America, 110(9), 3645–3650. Cite
Akiyoshi, B., Nelson, C. R., Duggan, N., Ceto, S., Ranish, J., & Biggins, S. (2013). The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein. PLoS Genet, 9(2), e1003216. Cite
Kloet, S. L., Whiting, J. L., Gafken, P., Ranish, J., & Wang, E. H. (2012). Phosphorylation-Dependent Regulation of Cyclin D1 and Cyclin A Gene Transcription by TFIID Subunits TAF1 and TAF7. Molecular and Cellular Biology, 32(16), 3358–3369. Cite
London, N., Ceto, S., Ranish, J., & Biggins, S. (2012). Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores. Curr Biol, 22, 900–906. https://doi.org/10.1016/j.cub.2012.03.052 Cite
Luo, J., Fishburn, J., Hahn, S., & Ranish, J. (2012). An Integrated Chemical Cross-linking and Mass Spectrometry Approach to Study Protein Complex Architecture and Function. Molecular & Cellular Proteomics : MCP, 11(2), M111 008318. Cite
Yan, W., Luo, J., Robinson, M., Eng, J., Aebersold, R., & Ranish, J. (2011). Index-ion Triggered MS2 Ion Quantification: A Novel Proteomics Approach for Reproducible Detection and Quantification of Targeted Proteins in Complex Mixtures. Mol Cell Proteomics, 10(3), M110 005611. Cite
Heldring, N., Isaacs, G. D., Diehl, A. G., Sun, M., Cheung, E., Ranish, J., & Kraus, W. L. (2011). Multiple Sequence-Specific DNA-Binding Proteins Mediate Estrogen Receptor Signaling through a Tethering Pathway. Mol Endocrinol. Cite
Himeda, C. L., Ranish, J., Pearson, R. C., Crossley, M., & Hauschka, S. D. (2010). KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sites. Mol Cell Biol, 30(14), 3430–3443. Cite
Gillespie, M. A., Le Grand, F., Scime, A., Kuang, S., von Maltzahn, J., Seale, V., Cuenda, A., Ranish, J., & Rudnicki, M. A. (2009). p38-gamma-dependent gene silencing restricts entry into the myogenic differentiation program. J Cell Biol, 187(7), 991–1005. Cite
Akiyoshi, B., Nelson, C. R., Ranish, J., & Biggins, S. (2009). Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit. Genes Dev, 23(24), 2887–2899. Cite
Akiyoshi, B., Nelson, C. R., Ranish, J., & Biggins, S. (2009). Analysis of Ipl1-mediated phosphorylation of the Ndc80 kinetochore protein in Saccharomyces cerevisiae. Genetics, 183(4), 1591–1595. Cite
Chaturvedi, C. P., Hosey, A. M., Palii, C., Perez-Iratxeta, C., Nakatani, Y., Ranish, J., Dilworth, F. J., & Brand, M. (2009). Dual role for the methyltransferase G9a in the maintenance of beta-globin gene transcription in adult erythroid cells. Proc Natl Acad Sci U S A, 106(43), 18303–18308. Cite