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首页> 外文期刊>Nature >Structure and catalytic mechanism of the human histone methyltransferase SET7/9
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Structure and catalytic mechanism of the human histone methyltransferase SET7/9

机译：人组蛋白甲基转移酶SET7 / 9的结构和催化机理

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Acetylation, phosphorylation and methylation of the amino-terminal tails of histones are thought to be involved in the regulation of chromatin structure and function. With just one exception, the enzymes identified in the methylation of specific lysine residues on histones (histone methyltransferases) belong to the SET family. The high-resolution crystal structure of a ternary complex of human SET7/9 with a histone peptide and cofactor reveals that the peptide substrate and cofactor bind on opposite surfaces of the enzyme. The target lysine accesses the active site of the enzyme and the S-adenosyl-L-methionine (AdoMet) cofactor by inserting its side chain into a narrow channel that runs through the enzyme, connecting the two surfaces. Here we show from the structure and from solution studies that SET7/9, unlike most other SET proteins, is exclusively a mono-methylase. The structure indicates the molecular basis of the specificity of the enzyme for the histone target, and allows us to propose a model for the methylation reaction that accounts for the role of many of the residues that are invariant across the SET family.
机译：组蛋白氨基末端尾巴的乙酰化，磷酸化和甲基化被认为与染色质结构和功能的调节有关。除了一个例外，在组蛋白上特定赖氨酸残基的甲基化中鉴定出的酶（组蛋白甲基转移酶）属于SET家族。人SET7 / 9与组蛋白肽和辅因子的三元复合物的高分辨率晶体结构表明，肽底物和辅因子结合在酶的相对表面上。靶赖氨酸通过将其侧链插入贯穿酶的狭窄通道并连接两个表面来访问酶和S-腺苷-L-蛋氨酸（AdoMet）辅因子的活性位点。在这里，我们从结构和溶液研究中显示出，与大多数其他SET蛋白不同，SET7 / 9仅是一种单甲基酶。该结构表明了该酶对组蛋白靶标的特异性的分子基础，并允许我们提出一个甲基化反应模型，该模型说明了SET家族中许多不变的残基的作用。

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