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

Curr Opin Struct Biol. 2008 Dec;18(6):741-7. doi: 10.1016/ 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.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Animals
  • Binding Sites
  • Crystallography
  • Evolution, Molecular
  • Histone Acetyltransferases / chemistry*
  • Histone Acetyltransferases / genetics
  • Histone Acetyltransferases / metabolism*
  • Humans
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • p300-CBP Transcription Factors / chemistry*
  • p300-CBP Transcription Factors / genetics
  • p300-CBP Transcription Factors / metabolism*


  • Saccharomyces cerevisiae Proteins
  • Histone Acetyltransferases
  • Rtt109 protein, S cerevisiae
  • p300-CBP Transcription Factors