Structural basis of the crosstalk between histone H2B monoubiquitination and H3 lysine 79 methylation on nucleosome

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2019,（4）
• 页码范围: 330-333
• 页数: 4页
• 语种: 英文

摘要

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).2Mono-,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 domaincontaining histone methyltransferase DOT1L (Disrupter of telomere silencing protein 1-1ike) in vivo.2 Incorporation of chemically monoubiquitinated H2B into in vitro reconstituted nucleosome directly stimulates the catalytic activity of DOT1 L4 (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.