Wang Ling, Tang Yong, Cole Philip A, Marmorstein Ronen
Department of Pharmacology and Molecular Sciences, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
Curr Opin Struct Biol. 2008 Dec;18(6):741-7. doi: 10.1016/j.sbi.2008.09.004. Epub 2008 Oct 27.
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.
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。