Histone H2A Ubiquitination Reinforces Mechanical Stability and Asymmetry at the Single-Nucleosome Level

文献类型： 外文期刊

第一作者： Chen, Ping

作者： Chen, Ping;Liu, Cuifang;Pei, Yingxin;Li, Guohong;Chen, Ping;Xiao, Xue;Kong, Jingwei;Lu, Ke;Ma, Lu;Dou, Shuo-Xing;Wang, Peng-Ye;Li, Wei;Xiao, Xue;Kong, Jingwei;Lu, Ke;Ma, Lu;Dou, Shuo-Xing;Wang, Peng-Ye;Li, Wei;Wang, Peng-Ye;Li, Wei;Xiao, Xue;Pei, Yingxin;Kong, Jingwei;Lu, Ke;Dou, Shuo-Xing;Wang, Peng-Ye;Li, Guohong;Wang, Yi-Zhou;Wang, Peng-Ye

作者机构：

期刊名称：JOURNAL OF THE AMERICAN CHEMICAL SOCIETY （ 影响因子：15.419； 五年影响因子：15.801 ）

ISSN： 0002-7863

年卷期： 2020 年 142 卷 7 期

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收录情况： SCI

摘要： Monoubiquitination at lysine 119 of histone H2A (ubH2A) is a prevalent post-translational modification that is associated with gene repression in the context of chromatin. However, the direct function of ubH2A on nucleosome is poorly understood. Here we identified the effect of ubH2A on nucleosome using single-molecule magnetic tweezers. We revealed that ubH2A stabilizes the nucleosome by blocking the peeling of DNA from the histone octamer. Each ubH2A reinforces one-half of the outer wrap and introduces a robust asymmetry for nucleosome unfolding. Furthermore, a real-time deubiquitination process confirmed that ubH2A-nucleosome is sequentially deubiquitinated and restored to the unmodified nucleosome state. These results provide a novel mechanism to understand the repression of the passage of RNA or DNA polymerases through the ubH2A-nucleosome barrier during gene transcription or replication.

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