Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
复制标题
DOI：
10.1038/nsmb1326
复制
发表时间：
2008-01-01
影响因子：
16.8
通讯作者：
Mer, Georges
中科院分区：
文献类型：
--
作者：
Lee, Joseph;Thompson, James R.;Mer, Georges
赖氨酸脱甲基酶JMJD2A具有通过其tudor结构域结合来自两个不同组蛋白序列（H3K4me3和H4K20me3）的三甲基化肽的独特性质。在这里，我们使用X射线晶体学和量热法表明，被JMJD 2A以相似亲和力识别的H3 K4 me3和H4 K20 me3采用了截然不同的结合模式，以至于我们能够设计JMJD 2A中的单点突变，抑制H3 K4 me3的识别，但不抑制H4 K20 me3，反之亦然。
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.