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H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity

Nat Chem Biol. 2022-09; 
Huasong Ai , Maoshen Sun , Aijun Liu , Zixian Sun , Tingting Liu , Lin Cao , Lujun Liang , Qian Qu , Zichen Li , Zhiheng Deng , Zebin Tong , Guochao Chu , Xiaolin Tian , Haiteng Deng , Suwen Zhao , Jia-Bin Li , Zhiyong Lou , Lei Liu
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Abstract

Ubiquitination-dependent histone crosstalk plays critical roles in chromatin-associated processes and is highly associated with human diseases. Mechanism studies of the crosstalk have been of the central focus. Here our study on the crosstalk between H2BK34ub and Dot1L-catalyzed H3K79me suggests a novel mechanism of ubiquitination-induced nucleosome distortion to stimulate the activity of an enzyme. We determined the cryo-electron microscopy structures of Dot1L-H2BK34ub nucleosome complex and the H2BK34ub nucleosome alone. The structures reveal that H2BK34ub induces an almost identical orientation and binding pattern of Dot1L on nucleosome as H2BK120ub, which positions Dot1L for the productive conformation thro... More

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