The CW domain, a new histone recognition module in chromatin proteins
The CW domain, a new histone recognition module in chromatin proteins
复制标题
DOI：
10.1038/emboj.2011.108
复制
发表时间：
2011-05-18
期刊：
影响因子：
11.4
通讯作者：
Aasland, Rein
中科院分区：
文献类型：
--
作者：
Hoppmann, Verena;Thorstensen, Tage;Aasland, Rein
组蛋白N端尾的翻译后修饰，包括赖氨酸甲基化，在染色质和基因表达的调控中具有关键作用。已经鉴定了许多蛋白质模块，其识别差异修饰的组蛋白尾部并为其蛋白质提供感测这种修饰的能力。在这里，我们确定了植物和动物染色质相关蛋白的CW域作为一种新的模块，识别组蛋白H3（H3 K4 me）上赖氨酸4的不同甲基化状态。拟南芥ASH 1 HOMOLOG 2（ASHH 2）组蛋白甲基转移酶的CW结构域的溶液结构提供了对不同CW结构域如何区分不同甲基化组蛋白尾部的见解。我们提供的证据表明，ASH 2作用于H3 K4 me标记的基因，允许ASH 2依赖的H3 K36三甲基化，这有助于组织特异性和发育调控基因的持续表达。这表明ASHH 2是组蛋白密码的“阅读者”和“编写者”的结合体。我们建议，不同的CW结构域，依赖于其特异性不同的H3 K4甲基化，是重要的表观遗传记忆或参与之间的切换允许和抑制染色质状态。The EMBO Journal（2011）30，1939-1952. doi：10.1038/daj.2011.108; 2011年4月26日在线发布
Post-translational modifications of the N-terminal histone tails, including lysine methylation, have key roles in regulation of chromatin and gene expression. A number of protein modules have been identified that recognize differentially modified histone tails and provide their proteins with the capacity to sense such modifications. Here, we identify the CW domain of plant and animal chromatin-related proteins as a novel module that recognizes different methylated states of lysine 4 on histone H3 (H3K4me). The solution structure of the CW domain of the Arabidopsis ASH1 HOMOLOG2 (ASHH2) histone methyltransferase provides insight into how different CW domains can distinguish different methylated histone tails. We provide evidence that ASHH2 is acting on H3K4me-marked genes, allowing for ASHH2-dependent H3K36 tri-methylation, which contributes to sustained expression of tissue-specific and developmentally regulated genes. This suggests that ASHH2 is a combined 'reader' and 'writer' of the histone code. We propose that different CW domains, dependent on their specificity for different H3K4 methylations, are important for epigenetic memory or participate in switching between permissive and repressive chromatin states. The EMBO Journal (2011) 30, 1939-1952. doi: 10.1038/emboj.2011.108; Published online 26 April 2011