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
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
收藏
页码:741 / 747
页数:7
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