Histone H2A Ubiquitination Reinforces Mechanical Stability and Asymmetry at the Single-Nucleosome Level
- Xue XiaoXue XiaoNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Xue Xiao
- Cuifang LiuCuifang LiuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, ChinaMore by Cuifang Liu
- Yingxin PeiYingxin PeiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Yingxin Pei
- Yi-Zhou WangYi-Zhou WangGenome Analysis Laboratory of the Ministry of Agriculture, Agricultural Synthetic Biology Center, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen, Guangdong 518124, ChinaMore by Yi-Zhou Wang
- Jingwei KongJingwei KongNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Jingwei Kong
- Ke LuKe LuNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Ke Lu
- Lu MaLu MaNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaMore by Lu Ma
- Shuo-Xing DouShuo-Xing DouNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Shuo-Xing Dou
- Peng-Ye WangPeng-Ye WangNational Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaSongshan Lake Materials Laboratory, Dongguan, Guangdong 523808, ChinaMore by Peng-Ye Wang
- Guohong LiGuohong LiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, ChinaUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaMore by Guohong Li
- Ping Chen*Ping Chen*[email protected]School of Basic Medical Sciences, Advanced Innovation Center for Human Brain Protection, Capital Medical University, Beijing 100054, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, ChinaMore by Ping Chen
- Wei Li*Wei Li*[email protected]National Laboratory for Condensed Matter Physics and Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaSongshan Lake Materials Laboratory, Dongguan, Guangdong 523808, ChinaMore by Wei Li
Abstract
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.