Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor

被引：163

作者：

Lee, Joseph ^{[1
]}

Thompson, James R. ^{[2
]}

Botuyan, Maria Victoria ^{[1
]}

Mer, Georges ^{[1
]}

机构：

[1] Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

[2] Mayo Clin, Coll Med, Dept Phys & Biomed Engn, Rochester, MN 55905 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 01期

关键词：

D O I：

10.1038/nsmb1326

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：

The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences ( H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.

引用

页码：109 / 111

页数：3

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