Publications

Detailed Information

Multivalent di-nucleosome recognition enables the Rpd3S histone deacetylase complex to tolerate decreased H3K36 methylation levels

DC Field Value Language
dc.contributor.authorHuh, Jae-Wan-
dc.contributor.authorWu, Jun-
dc.contributor.authorLee, Chul-Hwan-
dc.contributor.authorYun, Miyong-
dc.contributor.authorGilada, Daniel-
dc.contributor.authorBrautigam, Chad A.-
dc.contributor.authorLi, Bing-
dc.date.accessioned2024-05-14T06:37:31Z-
dc.date.available2024-05-14T06:37:31Z-
dc.date.created2023-05-09-
dc.date.created2023-05-09-
dc.date.issued2012-08-
dc.identifier.citationThe EMBO Journal, Vol.31 No.17, pp.3564-3574-
dc.identifier.issn0261-4189-
dc.identifier.urihttps://hdl.handle.net/10371/201854-
dc.description.abstractThe Rpd3S histone deacetylase complex represses cryptic transcription initiation within coding regions by maintaining the hypo-acetylated state of transcribed chromatin. Rpd3S recognizes methylation of histone H3 at lysine 36 (H3K36me), which is required for its deacetylation activity. Rpd3S is able to function over a wide range of H3K36me levels, making this a unique system to examine how chromatin regulators tolerate the reduction of their recognition signal. Here, we demonstrated that Rpd3S makes histone modification-independent contacts with nucleosomes, and that Rpd3S prefers di-nucleosome templates since two binding surfaces can be readily accessed simultaneously. Importantly, this multivalent mode of interaction across two linked nucleosomes allows Rpd3S to tolerate a two-fold intramolecular reduction of H3K36me. Our data suggest that chromatin regulators utilize an intrinsic di-nucleosome-recognition mechanism to prevent compromised function when their primary recognition modifications are diluted. © 2012 European Molecular Biology Organization | All Rights Reserved.-
dc.language영어-
dc.publisherNature Publishing Group-
dc.titleMultivalent di-nucleosome recognition enables the Rpd3S histone deacetylase complex to tolerate decreased H3K36 methylation levels-
dc.typeArticle-
dc.identifier.doi10.1038/emboj.2012.221-
dc.citation.journaltitleThe EMBO Journal-
dc.identifier.wosid000308390700007-
dc.identifier.scopusid2-s2.0-84866067719-
dc.citation.endpage3574-
dc.citation.number17-
dc.citation.startpage3564-
dc.citation.volume31-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorLee, Chul-Hwan-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusCHROMATIN-STRUCTURE-
dc.subject.keywordPlusIN-VITRO-
dc.subject.keywordPlusTRANSCRIPTION-
dc.subject.keywordPlusACETYLATION-
dc.subject.keywordPlusINHERITANCE-
dc.subject.keywordPlusSTATES-
dc.subject.keywordPlusLYSINE-36-
dc.subject.keywordPlusRECRUITS-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusDIRECTS-
dc.subject.keywordAuthorchromatin recognition-
dc.subject.keywordAuthordi-nucleosome-
dc.subject.keywordAuthorepigenetics-
dc.subject.keywordAuthorHDAC-
Appears in Collections:
Files in This Item:
There are no files associated with this item.

Related Researcher

  • College of Medicine
Research Area Epigenetics, Heterochromatin, Histone Modifications

Altmetrics

Item View & Download Count

  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.

Share