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p300/CBP和Rtt109组蛋白乙酰转移酶的结构与化学性质:对组蛋白乙酰转移酶进化及功能的启示

Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function.

作者信息

Wang Ling, Tang Yong, Cole Philip A, Marmorstein Ronen

机构信息

Department of Pharmacology and Molecular Sciences, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.

出版信息

Curr Opin Struct Biol. 2008 Dec;18(6):741-7. doi: 10.1016/j.sbi.2008.09.004. Epub 2008 Oct 27.

Abstract

The recent structure and associated biochemical studies of the metazoan-specific p300/CBP and fungal-specific Rtt109 histone acetyltransferases (HATs) have provided new insights into the ancestral relationship between HATs and their functions. These studies point to a common HAT ancester that has evolved around a common structural framework to form HATs with divergent catalytic and substrate-binding properties. These studies also point to the importance of regulatory loops within HATs and autoacetylation in HAT function. Implications for future studies are discussed.

摘要

后生动物特异性的p300/CBP和真菌特异性的Rtt109组蛋白乙酰转移酶(HATs)的近期结构及相关生化研究,为HATs及其功能之间的祖先关系提供了新见解。这些研究表明存在一个共同的HAT祖先,它围绕一个共同的结构框架进化,形成了具有不同催化和底物结合特性的HATs。这些研究还指出了HATs内调控环和自身乙酰化在HAT功能中的重要性。文中讨论了对未来研究的启示。

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本文引用的文献

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Molecular basis for the autoregulation of the protein acetyl transferase Rtt109.蛋白质乙酰转移酶Rtt109自动调节的分子基础
Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12236-41. doi: 10.1073/pnas.0805813105. Epub 2008 Aug 21.
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