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

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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.
Publisher
COLD SPRING HARBOR LAB PRESS
Issue Date
2019-06
Language
English
Article Type
Article
Citation

GENES & DEVELOPMENT, v.33, no.11-12, pp.620 - 625

ISSN
0890-9369
DOI
10.1101/gad.323790.118
URI
http://hdl.handle.net/10203/262794
Appears in Collection
PH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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