Tetrahymena Histone Acetyltransferase A: A Homolog to Yeast Gcn5p Linking Histone Acetylation to Gene Activation

1996/03/01 by James E. Brownell, Jianxin Zhou, Tamara A. Ranalli +4 · 5 citations
Biochemistry, Genetics and Molecular Biology · #RNA modifications and cancer #Epigenetics and DNA Methylation #Ubiquitin and proteasome pathways

paper · pdf · doi:10.1016/s0092-8674(00)81063-6

openalex publication_date 1996/03/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

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.

Citations

• ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
• Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast
• Basic local alignment search tool

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• Histone [wikipedia]