4.5 Review

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

期刊

CURRENT OPINION IN CHEMICAL BIOLOGY
卷 11, 期 6, 页码 628-635

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2007.09.011

关键词

-

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据