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Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
Author(s): Brownell JE, Zhou JX, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD
Source: CELL    Volume: 84    Issue: 6    Pages: 843-851    Published: MAR 22 1996  
Times Cited: 791     References: 59     
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.
Document Type: Article
Language: English
Addresses:
1. UNIV ROCHESTER, DEPT BIOL, ROCHESTER, NY 14627 USA
2. COLD SPRING HARBOR LAB, COLD SPRING HARBOR, NY 11724 USA
3. UNIV TEXAS, MD ANDERSON CANC CTR, DEPT BIOCHEM & MOLEC BIOL, HOUSTON, TX 77030 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: UC381
ISSN: 0092-8674
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