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Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase
Korea Adv Inst Sci & Technol, Dept Biol Sci, Daejeon 34141, South Korea..
Seoul Natl Univ, Dept Phys & Astron, Seoul 08826, South Korea..
Sungkyunkwan Univ, Sch Pharm, Suwon 16419, South Korea..
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Biomedical Engineering and Health Systems, Structural Biotechnology. Karolinska Inst, Dept Biosci & Nutr, S-14152 Huddinge, Sweden..ORCID iD: 0000-0003-3862-3433
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2019 (English)In: Genes & Development, ISSN 0890-9369, E-ISSN 1549-5477, Vol. 33, no 11-12, p. 620-625Article in journal (Refereed) Published
Abstract [en]

DOT1L 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.

Place, publisher, year, edition, pages
NLM (Medline) , 2019. Vol. 33, no 11-12, p. 620-625
Keywords [en]
cryo-EM, histone, nucleosome, methylation, ubiquitin
National Category
Cell Biology
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URN: urn:nbn:se:kth:diva-254093DOI: 10.1101/gad.323790.118ISI: 000470071900003PubMedID: 30923167Scopus ID: 2-s2.0-85065786784OAI: oai:DiVA.org:kth-254093DiVA, id: diva2:1330065
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QC 20190625

Available from: 2019-06-25 Created: 2019-06-25 Last updated: 2019-06-25Bibliographically approved

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Jung, TaeyangHebert, Hans

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