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

被引：129

作者：

Wang, Ling ^{[1
]}

Tang, Yong ^{[2
]}

Cole, Philip A. ^{[1
]}

Marmorstein, Ronen ^{[2
,3
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA

[2] Wistar Inst Anat & Biol, Program Gene Express & Regulat, Philadelphia, PA 19104 USA

[3] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2008年 / 18卷 / 06期

关键词：

D O I：

10.1016/j.sbi.2008.09.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：741 / 747

页数：7

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