组蛋白修饰酶：结构、机制及特异性
Histone modifying enzymes: structures, mechanisms, and specificities.
作者信息
Marmorstein Ronen, Trievel Raymond C
机构信息
Program in Gene Expression and Regulation, The Wistar Institute, Philadelphia, PA 19104, USA.
出版信息
Biochim Biophys Acta. 2009 Jan;1789(1):58-68. doi: 10.1016/j.bbagrm.2008.07.009. Epub 2008 Aug 3.
Histone modifying enzymes catalyze the addition or removal of an array of covalent modifications in histone and non-histone proteins. Within the context of chromatin, these modifications regulate gene expression as well as other genomic functions and have been implicated in establishing and maintaining a heritable epigenetic code that contributes to defining cell identity and fate. Biochemical and structural characterization of histone modifying enzymes has yielded important insights into their respective catalytic mechanisms, substrate specificities, and regulation. In this review, we summarize recent advances in understanding these enzymes, highlighting studies of the histone acetyltransferases (HATs) p300 (also now known as KAT3B) and Rtt109 (KAT11) and the histone lysine demethylases (HDMs) LSD1 (KDM1) and JMJD2A (KDM4A), present overriding themes that derive from these studies, and pose remaining questions concerning their regulatory roles in mediating DNA transactions.
组蛋白修饰酶催化组蛋白和非组蛋白中一系列共价修饰的添加或去除。在染色质环境中，这些修饰调节基因表达以及其他基因组功能，并与建立和维持一种可遗传的表观遗传密码有关，该密码有助于定义细胞身份和命运。组蛋白修饰酶的生化和结构表征已为其各自的催化机制、底物特异性和调节提供了重要见解。在本综述中，我们总结了在理解这些酶方面的最新进展，重点介绍了组蛋白乙酰转移酶（HATs）p300（现也称为KAT3B）和Rtt109（KAT11）以及组蛋白赖氨酸去甲基化酶（HDMs）LSD1（KDM1）和JMJD2A（KDM4A）的研究，呈现这些研究中得出的首要主题，并提出有关它们在介导DNA交易中的调节作用的剩余问题。
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