Couture Jean-François, Trievel Raymond C
Department of Biological Chemistry, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0606, USA.
Curr Opin Struct Biol. 2006 Dec;16(6):753-60. doi: 10.1016/j.sbi.2006.10.002. Epub 2006 Oct 27.
Histone-modifying enzymes catalyze a diverse array of post-translational modifications of core and linker histones within chromatin. These modifications govern a multitude of genomic functions, particularly gene expression, and are believed to constitute an epigenetic code. Histone-modifying enzymes inscribe this code by catalyzing site-selective modifications, which are subsequently interpreted by effector proteins that recognize specific covalent marks. The substrate specificity of these enzymes is of fundamental biological importance because it underpins this epigenetic code. Recently, the structural basis of this specificity has been examined with regards to recently determined structures of GCN5 acetyltransferases and SET domain methyltransferases in complex with their cognate histone substrates.
组蛋白修饰酶催化染色质内核组蛋白和连接组蛋白的多种翻译后修饰。这些修饰调控着众多的基因组功能,尤其是基因表达,并且被认为构成了一种表观遗传密码。组蛋白修饰酶通过催化位点选择性修饰来书写这种密码,随后由识别特定共价标记的效应蛋白来解读。这些酶的底物特异性具有根本的生物学重要性,因为它支撑着这种表观遗传密码。最近,已根据GCN5乙酰转移酶和SET结构域甲基转移酶与其同源组蛋白底物形成复合物的最新确定结构,研究了这种特异性的结构基础。