Volume 29, No 4, Apr 2019
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 29 Issue 4, April 2019: 330-333
LETTERS TO THE EDITOR
Structural basis of the crosstalk between histone H2B monoubiquitination and H3 lysine 79 methylation on nucleosome
Tonghui Yao 1, Wei Jing 1, Zhiguo Hu 1, Ming Tan 2, Mi Cao 2,Qianmin Wang 2, Yan Li 3, Guiyong Yuan 2, Ming Lei 2 and Jing Huang 2
1 State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai 201210, China; 2Shanghai Institute of Precision Medicine, Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China and 3National Facility for Protein Sciences in Shanghai, Zhangjiang Lab, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China
Correspondence: Jing Huang (huangjing@shsmu.edu.cn)
Dear Editor,
Histone marks deposited by post-translational modifications (PTMs) frequently occur in interrelated combinational patterns to create a complex and precise control on the chromatin structure and function.1 One of the landmark findings of histone PTM crosstalk is the trans-histone regulation of histone H3 lysine 79 (H3K79) methylation by the monoubiquitination of histone H2B on lysine 120 (H2BK120).2 Mono-, di-, and tri-methylation of histone H3K79 serves as a prominent histone mark that participates in transcription regulation and DNA damage response.3 H2BK120 monoubiquitination (H2BK120ub1) is a prerequisite for the efficient methylation of H3K79 by the unique non-SET domain-containing histone methyltransferase DOT1L (Disrupter of telomere silencing protein 1-like) in vivo.2 Incorporation of chemically monoubiquitinated H2B into in vitro reconstituted nucleosome directly stimulates the catalytic activity of DOT1L4 (Supplementary information, Figs. S1 and S2). It still remains poorly understood how the H3K79 methyl marks are deposited and how the associated PTM crosstalk occurs on nucleosome.
https://doi.org/10.1038/s41422-019-0146-7
FULL TEXT | PDF
Browse 1046
