Identification of a Gene Encoding a Yeast Histone H4 Acetyltransferase (*)
- From the Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794 and the
- (1) Department of Biology, Brookhaven National Laboratory, Upton, New York 11973
- § To whom correspondence should be addressed. Tel.: 516-632-8565; Fax: 516-632-8575.
Abstract
A collection of yeast temperature-sensitive mutants was screened by an enzymatic assay to find a mutant defective in the acetylation of histone H4. The assay used a fractionated cell extract and measured acetylation of a peptide corresponding to amino acids 1-28 of H4. There are at least two activities in this fraction that acetylate the peptide. A mutation, hat1-1, that eliminates one of the activities was identified and mapped to a locus near the centromere of chromosome XVI. The HAT1 gene was cloned and found to encode a protein of 374 amino acids. Analysis of the peptide used in the assay demonstrated that the HAT1 enzyme acetylates lysine 12 of histone H4. hat1 mutants have no obvious growth defects or phenotypes other than the enzyme defect itself. The HAT1 protein expressed in Escherichia coli gave histone acetyltransferase activity in vitro, demonstrating that HAT1 is the structural gene for the enzyme.
Footnotes
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↵* This work was supported by Grant GM28220 from the National Institutes of Health (to R. S.). Work at the Center for the Analysis and Synthesis of Macromolecules, SUNY at Stony Brook, was supported by National Institutes of Health Grant RR02-427 and by the Center for Biotechnology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
This paper is dedicated to the memory of Hal Weintraub.
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↵1 The abbreviations used are:
- HAT
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histone acetyltransferase
- kb
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kilobase(s)
- bp
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base pair(s).
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↵2S. Tafrov and R. Sternglanz, unpublished data.
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- Received August 14, 1995.
- © 1995 by The American Society for Biochemistry and Molecular Biology, Inc.
