Connecting the DOTs: covalent histone modifications and the formation of silent chromatin

被引：16

作者：

Khan, AU ^{[1
]}

Hampsey, M ^{[1
]}

机构：

[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem, Div Nucleic Acids Enzymol, Piscataway, NJ 08854 USA

来源：

TRENDS IN GENETICS | 2002年 / 18卷 / 08期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

D O I：

10.1016/S0168-9525(02)02746-4

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Histone methylation has emerged as a significant regulator of chromatin structure and function. Two different classes of histone methyltransferase (HMT) have been described, which target either lysine or arginine residues in the histone N-terminal tails. A flurry of recent papers now describe a third class of HMT that affects chromatin silencing indirectly, not by methylation of histone tails, but instead by targeting a conserved lysine residue in the core domain of the nucleosome.

引用

页码：387 / 389

页数：3

共 27 条

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