Recognition of non-methyl histone marks

被引：5
|
作者：
Bycroft, Mark [1 ]
机构：
[1] MRC Lab Mol Biol, Cambridge CB2 0QH, England
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 2011年 / 21卷 / 06期
基金：
英国医学研究理事会;
关键词：
DNA-DAMAGE RESPONSE; MOLECULAR-BASIS; PHD FINGER; CHROMATIN; BINDING; ACETYLATION; PHOSPHORYLATION; ACTIVATION; MECHANISM; DOMAINS;
D O I：
10.1016/j.sbi.2011.09.006
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：
Eukaryotic DNA is packaged into chromatin, a complex assembly of protein and nucleic acid. The histones within chromatin undergo extensive, highly regulated posttranslational modification. One of the main functions of these modifications is to act as markers that ensure that the mutiprotein complexes that regulate the transcription, replication and repair of DNA are directed to the correct region of the genome at the appropriate time. This review focuses on recent biochemical and structural studies on how histones modified by acetylation, ubiquitination, phosphorylation and poly-ADP-ribosylation are recognized.
引用
收藏
页码：761 / 766
页数：6
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