Dynamic protein methylation in chromatin biology

被引:141
作者
Ng, S. S. [1 ]
Yue, W. W. [1 ]
Oppermann, U. [1 ,2 ]
Klose, R. J. [1 ,3 ]
机构
[1] Struct Genom Consortium, Oxford OX3 7DQ, England
[2] Botnar Res Ctr, Oxford Biomed Res Unit, Oxford OX3 7LD, England
[3] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England
基金
英国惠康基金;
关键词
Chromatin; methylation; demethylation; histone; epigenetics; CLASS-III ALCOHOL; DEPENDENT FORMALDEHYDE DEHYDROGENASE; HISTONE METHYLTRANSFERASE ACTIVITY; POSTTRANSLATIONAL MODIFICATIONS; STRUCTURAL BASIS; ARGININE METHYLATION; H3; METHYLATION; PHD FINGER; LYSINE-4; TRIMETHYLATION; MOLECULAR RECOGNITION;
D O I
10.1007/s00018-008-8303-z
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
Post-translational modification of chromatin is emerging as an increasingly important regulator of chromosomal processes. In particular, histone lysine and arginine methylation play important roles in regulating transcription, maintaining genomic integrity, and contributing to epigenetic memory. Recently, the use of new approaches to analyse histone methylation, the generation of genetic model systems, and the ability to interrogate genome wide histone modification profiles has aided in defining how histone methylation contributes to these processes. Here we focus on the recent advances in our understanding of the histone methylation system and examine how dynamic histone methylation contributes to normal cellular function in mammals.
引用
收藏
页码:407 / 422
页数:16
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