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

J. E. Brownell, J. Zhou, T. Ranalli, R. Kobayashi, D. G. Edmondson, S. Y. Roth, C. D. Allis

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1320 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)843-851
Number of pages9
JournalCell
Volume84
Issue number6
DOIs
StatePublished - 1996
Externally publishedYes

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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