Structural dynamics of protein lysine methylation and demethylation

被引：52

作者：

Cheng, Xiaodong ^{[1
]}

Zhang, Xing ^{[1
]}

机构：

[1] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

来源：

MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS | 2007年 / 618卷 / 1-2期

关键词：

protein lysine methylation and demethylation; SET domain proteins; S-adenosyl-L-methionine (AdoMet);

D O I：

10.1016/j.mrfmmm.2006.05.041

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Lysine methylation plays a central role in the "histone code" that regulates chromatin structure, impacts transcription, and responds to DNA damage. A single lysine can be mono-, di-, tri-methylated, or unmethylated, with different functional consequences for each of the four forms. This review (written in the early 2006) described structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot 1 p), and the protein motifs that recognize (decode) these methyl-lysine signals. We also discuss the recently discovered protein lysine demethylating enzymes (LSD1 and JmjC domains). (C) 2007 Elsevier B.V. All rights reserved.

引用

页码：102 / 115

页数：14

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