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.
MeSH terms
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Acetylation
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Animals
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Binding Sites
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Crystallography
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Evolution, Molecular
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Histone Acetyltransferases / chemistry*
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Histone Acetyltransferases / genetics
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Histone Acetyltransferases / metabolism*
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Humans
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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p300-CBP Transcription Factors / chemistry*
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p300-CBP Transcription Factors / genetics
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p300-CBP Transcription Factors / metabolism*
Substances
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Saccharomyces cerevisiae Proteins
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Histone Acetyltransferases
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Rtt109 protein, S cerevisiae
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p300-CBP Transcription Factors