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Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function Wang L; Tang Y; Cole PA; Marmorstein RCurr Opin Struct Biol 2008[Dec]; 18 (6): 741-7The 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.|Acetylation[MESH]|Animals[MESH]|Binding Sites[MESH]|Crystallography[MESH]|Evolution, Molecular[MESH]|Histone Acetyltransferases/*chemistry/genetics/*metabolism[MESH]|Humans[MESH]|Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism[MESH]|p300-CBP Transcription Factors/*chemistry/genetics/*metabolism[MESH] |
