Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation

Cell. 1996 Mar 22;84(6):843-51. doi: 10.1016/s0092-8674(00)81063-6.


We report the cloning of a transcription-associated histone acetyltransferase type A(HAT A). This Tetrahymena enzyme is strikingly homologous to the yeast protein Gcn5, a putative transcriptional adaptor, and we demonstrate that recombinant Gcn5p possesses HAT activity. Both the ciliate enzyme and Gcn5p contain potential active site residues found in other acetyltransferases and a highly conserved bromodomain. The presence of this domain in nuclear A-type HATs, but not in cytoplasmic B-type HATs, suggests a mechanism whereby HAT A is directed to chromatin to facilitate transcriptional activation. These findings shed light on the biochemical function of the evolutionarily conserved Gcn5p-Ada complex, directly linking histone acetylation to gene activation, and indicate that histone acetylation is a targeted phenomenon.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylation
  • Acetyltransferases / genetics*
  • Acetyltransferases / metabolism
  • Animals
  • Base Sequence
  • Chromatin / genetics
  • Cloning, Molecular
  • Conserved Sequence
  • Gene Expression Regulation, Enzymologic / physiology
  • Genes, Protozoan / physiology
  • Histone Acetyltransferases
  • Histones / metabolism*
  • Molecular Sequence Data
  • Saccharomyces cerevisiae Proteins*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Tetrahymena thermophila / genetics*
  • Transcriptional Activation
  • Yeasts / genetics


  • Chromatin
  • Histones
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • Histone Acetyltransferases

Associated data

  • GENBANK/U47321