Reversal of Histone Methylation: Biochemical and Molecular Mechanisms of Histone Demethylases

被引：436

作者：

Mosammaparast, Nima ^{[1
,2
]}

Shi, Yang ^{[1
,3
]}

机构：

[1] Harvard Univ, Sch Med, Dept Pathol, Childrens Hosp, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dept Lab Med, Childrens Hosp, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Med, Childrens Hosp,Div Newborn Med, Boston, MA 02115 USA

来源：

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79 | 2010年 / 79卷

关键词：

chromatin; demethylase; epigenetics; transcription; H3; LYSINE-4; METHYLATION; STRUCTURAL BASIS; CHROMATIN-STRUCTURE; METHYLTRANSFERASE ACTIVITY; OXIDATIVE DEMETHYLATION; ARGININE METHYLATION; CRYSTAL-STRUCTURE; GENE ACTIVATION; TARGET GENES; JMJD2; FAMILY;

D O I：

10.1146/annurev.biochem.78.070907.103946

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The importance of histone methylation in gene regulation was suggested over 40 years ago. Yet, the dynamic nature of this histone modification was recognized only recently, with the discovery of the first histone demethylase nearly five years ago. Since then, our insight into the mechanisms, structures, and macromolecular complexes of these enzymes has grown exponentially. Overall, the evidence strongly supports a key role for histone demethylases in eukaryotic transcription and other chromatin-dependent processes. Here, we examine these and related facets of histone demethylases discovered to date, focusing on their biochemistry, structure, and enzymology.

引用

页码：155 / 179

页数：25

共 140 条

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