H2A mono-ubiquitination differentiates FACT's functions in nucleosome assembly and disassembly.
H2A mono-ubiquitination differentiates FACT's functions in nucleosome assembly and disassembly.
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H2A 单泛素化区分了 FACT 在核小体组装和拆卸中的功能。
DOI：
10.1093/nar/gkab1271
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发表时间：
2022-01-25
影响因子：
14.9
通讯作者：
Li W
中科院分区：
文献类型：
--
作者：
Wang YZ;Liu C;Zhao J;Yu J;Luo A;Xiao X;Dou SX;Ma L;Wang PY;Li M;Li G;Yan J;Chen P;Li W
The histone chaperone FACT (FAcilitates Chromatin Transcription) plays an essential role in transcription and DNA replication by its dual functions on nucleosome assembly to maintain chromatin integrity and nucleosome disassembly to destabilize nucleosome and facilitate its accessibility simultaneously. Mono-ubiquitination at Lysine 119 of H2A (ubH2A) has been suggested to repress transcription by preventing the recruitment of FACT at early elongation process. However, up to date, how ubH2A directly affects FACT on nucleosome assembly and disassembly remains elusive. In this study, we demonstrated that the dual functions of FACT are differently regulated by ubH2A. The H2A ubiquitination does not affect FACT’s chaperone function in nucleosome assembly and FACT can deposit ubH2A–H2B dimer on tetrasome to form intact nucleosome. However, ubH2A greatly restricts FACT binding on nucleosome and inhibits its activity of nucleosome disassembly. Interestingly, deubiquitination of ubH2A rescues the nucleosome disassembly function of FACT to activate gene transcription. Our findings provide mechanistic insights of how H2A ubiquitination affects FACT in breaking nucleosome and maintaining its integrity, which sheds light on the biological function of ubH2A and various FACT’s activity under different chromatin states. ubH2A restricts FACT binding on nucleosome, but maintains FACT's chaperone function.
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