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.author | Huh, Jae-Wan | - |
dc.contributor.author | Wu, Jun | - |
dc.contributor.author | Lee, Chul-Hwan | - |
dc.contributor.author | Yun, Miyong | - |
dc.contributor.author | Gilada, Daniel | - |
dc.contributor.author | Brautigam, Chad A. | - |
dc.contributor.author | Li, Bing | - |
dc.date.accessioned | 2024-05-14T06:37:31Z | - |
dc.date.available | 2024-05-14T06:37:31Z | - |
dc.date.created | 2023-05-09 | - |
dc.date.created | 2023-05-09 | - |
dc.date.issued | 2012-08 | - |
dc.identifier.citation | The EMBO Journal, Vol.31 No.17, pp.3564-3574 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.uri | https://hdl.handle.net/10371/201854 | - |
dc.description.abstract | The 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.language | 영어 | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Multivalent di-nucleosome recognition enables the Rpd3S histone deacetylase complex to tolerate decreased H3K36 methylation levels | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/emboj.2012.221 | - |
dc.citation.journaltitle | The EMBO Journal | - |
dc.identifier.wosid | 000308390700007 | - |
dc.identifier.scopusid | 2-s2.0-84866067719 | - |
dc.citation.endpage | 3574 | - |
dc.citation.number | 17 | - |
dc.citation.startpage | 3564 | - |
dc.citation.volume | 31 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Lee, Chul-Hwan | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | CHROMATIN-STRUCTURE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | TRANSCRIPTION | - |
dc.subject.keywordPlus | ACETYLATION | - |
dc.subject.keywordPlus | INHERITANCE | - |
dc.subject.keywordPlus | STATES | - |
dc.subject.keywordPlus | LYSINE-36 | - |
dc.subject.keywordPlus | RECRUITS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | DIRECTS | - |
dc.subject.keywordAuthor | chromatin recognition | - |
dc.subject.keywordAuthor | di-nucleosome | - |
dc.subject.keywordAuthor | epigenetics | - |
dc.subject.keywordAuthor | HDAC | - |
- Appears in Collections:
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.