Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase

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dc.contributor.authorJang, Seongminko
dc.contributor.authorKang, Chanshinko
dc.contributor.authorYang, Han-Solko
dc.contributor.authorJung, Taeyangko
dc.contributor.authorHebert, Hansko
dc.contributor.authorChung, Ka Youngko
dc.contributor.authorKim, Seung Joongko
dc.contributor.authorHohng, Sungchulko
dc.contributor.authorSong, Ji-Joonko
dc.date.accessioned2019-06-24T01:50:05Z-
dc.date.available2019-06-24T01:50:05Z-
dc.date.created2019-06-12-
dc.date.created2019-06-12-
dc.date.created2019-06-12-
dc.date.created2019-06-12-
dc.date.created2019-06-12-
dc.date.issued2019-06-
dc.identifier.citationGENES & DEVELOPMENT, v.33, no.11-12, pp.620 - 625-
dc.identifier.issn0890-9369-
dc.identifier.urihttp://hdl.handle.net/10203/262794-
dc.description.abstractDOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome. These results establish the molecular basis of the cross-talk between H2B ubiquitination and H3 Lys79 methylation as well as nucleosome destabilization by DOT1L.-
dc.languageEnglish-
dc.publisherCOLD SPRING HARBOR LAB PRESS-
dc.titleStructural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase-
dc.typeArticle-
dc.identifier.wosid000470071900003-
dc.identifier.scopusid2-s2.0-85065786784-
dc.type.rimsART-
dc.citation.volume33-
dc.citation.issue11-12-
dc.citation.beginningpage620-
dc.citation.endingpage625-
dc.citation.publicationnameGENES & DEVELOPMENT-
dc.identifier.doi10.1101/gad.323790.118-
dc.contributor.localauthorKim, Seung Joong-
dc.contributor.localauthorSong, Ji-Joon-
dc.contributor.nonIdAuthorKang, Chanshin-
dc.contributor.nonIdAuthorYang, Han-Sol-
dc.contributor.nonIdAuthorJung, Taeyang-
dc.contributor.nonIdAuthorHebert, Hans-
dc.contributor.nonIdAuthorChung, Ka Young-
dc.contributor.nonIdAuthorHohng, Sungchul-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorcryo-EM-
dc.subject.keywordAuthorhistone-
dc.subject.keywordAuthornucleosome-
dc.subject.keywordAuthormethylation-
dc.subject.keywordAuthorubiquitin-
dc.subject.keywordPlusCORE PARTICLE-
dc.subject.keywordPlusOCTAMER-
dc.subject.keywordPlusDOMAIN-
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