Journal
GENES & DEVELOPMENT
Volume 33, Issue 11-12, Pages 620-625Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.323790.118
Keywords
cryo-EM; histone; nucleosome; methylation; ubiquitin
Categories
Funding
- National Research Foundation (NRF) of Korea [NRF-2016R1A2B3006293, NRF-2016K1A1A2912057, NRF-2012R1A5A2A28671 860]
- Swedish Research Council [201603810]
- Global Science Experimental Data Hub Center (GSDC), Korea Institute of Science and Technology Information (KISTI) [NRF-2018R1A6A7052113]
- Korea National Research Foundation [NRF-2016H1A2A1908806]
- National Research Foundation of Korea [2016H1A2A1908806] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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