Chemical Approaches for Studying Histone Modifications

被引：73
作者：
Chatterjee, Champak [1 ]
Muir, Tom W. [1 ]
机构：
[1] Rockefeller Univ, Lab Synthet Prot Chem, New York, NY 10065 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2010年 / 285卷 / 15期
关键词：
METHYL-LYSINE; SUBSTRATE-SPECIFICITY; CHROMATIN-STRUCTURE; PROTEIN LIGATION; ACETYLATION; H3; NUCLEOSOME; CYSTEINE; TRIMETHYLATION; DIMETHYLATION;
D O I：
10.1074/jbc.R109.080291
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：
Histones form the protein core around which genomic DNA is wrapped in eukaryotic chromatin. Numerous genetic studies have established that the structure and transcriptional state of chromatin are closely related to histone post-translational modifications. Further elucidation of the precise mechanistic roles for individual histone modifications requires the ability to isolate and study homogeneously modified histones. However, the highly heterogeneous nature of histone modifications in vivo poses a significant challenge for such studies. Chemical tools that have enabled biochemical and biophysical studies of site-specifically modified histones are the focus of this minireview.
引用
收藏
页码：11045 / 11050
页数：6
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