Modular paths to 'decoding' and 'wiping' histone lysine methylation

被引:12
作者
Kustatscher, Georg [1 ]
Ladurner, Andreas G. [1 ]
机构
[1] European Mol Biol Lab, Gene Express Unit, Struct & Computat Biol Unit, D-69117 Heidelberg, Germany
关键词
D O I
10.1016/j.cbpa.2007.09.011
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
Specific cell activity results from developmental and environmental control over the expression of our genes. A key component in epigenetic forms of biological regulation is the methylation of lysine residues in histone proteins. This post-translational modification of chromatin has been vigorously studied over the past few years. Highly specific enzymes catalyzing the synthesis and targeted removal of methyl marks, as well as protein motifs recognizing distinct methylated lysines, have been identified. Here, we provide a molecular overview of discrete structural mechanisms that allow these modular proteins to effect and recognize particular lysine methylation imprints on the chromatin polymer.
引用
收藏
页码:628 / 635
页数:8
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