H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation

Anfeng Luo, Jingwei Kong, Jun Chen, Xue Xiao, Jie Lan, Xiaorong Li, Cuifang Liu, Peng-Ye Wang, Guohong Li, Wei Li () and Ping Chen ()
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Anfeng Luo: Capital Medical University
Jingwei Kong: Chinese Academy of Sciences
Jun Chen: Capital Medical University
Xue Xiao: Chinese Academy of Sciences
Jie Lan: Institute of Biophysics, Chinese Academy of Sciences
Xiaorong Li: Institute of Biophysics, Chinese Academy of Sciences
Cuifang Liu: Institute of Biophysics, Chinese Academy of Sciences
Peng-Ye Wang: Chinese Academy of Sciences
Guohong Li: University of Chinese Academy of Sciences
Wei Li: Chinese Academy of Sciences
Ping Chen: Capital Medical University

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract Histone H2B mono-ubiquitination at lysine 120 (ubH2B) has been found to regulate transcriptional elongation by collaborating with the histone chaperone FACT (Facilitates Chromatin Transcription) and plays essential roles in chromatin-based transcriptional processes. However, the mechanism of how ubH2B directly collaborates with FACT at the nucleosome level still remains elusive. In this study, we demonstrate that ubH2B impairs the mechanical stability of the nucleosome and helps to recruit FACT by enhancing the binding of FACT on the nucleosome. FACT prefers to bind and deposit H2A-ubH2B dimers to form an intact nucleosome. Strikingly, the preferable binding of FACT on ubH2B-nucleosome greatly enhances nucleosome stability and maintains its integrity. The stable altered nucleosome state obtained by ubH2B and FACT provides a key platform for gene transcription, as revealed by genome-wide and time-course ChIP-qPCR analyses. Our findings provide mechanistic insights of how ubH2B directly collaborates with FACT to regulate nucleosome dynamics for gene transcription.

Date: 2023
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DOI: 10.1038/s41467-023-36467-3

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