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PMID: 16543219 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4.

Genes & development ·Vol. 20 ·No. 6 ·2006-03-15 ·Pages 660-5

Keogh MC, Mennella TA, Sawa C, Berthelet S, Krogan NJ, Wolek A, Podolny V, Carpenter LR, Greenblatt JF, Baetz K, Buratowski S

Abstract

The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair. Function-specific modifications may help explain how the same component of chromatin can function in diverse pathways.

MeSH Terms
Acetylation Acetyltransferases/metabolism Amino Acid Sequence Chromosomes, Fungal Histone Acetyltransferases Histones/chemistry,metabolism Molecular Sequence Data Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins/chemistry,metabolism Sequence Homology, Amino Acid
Chemicals
Histones Htz1 protein, S cerevisiae Saccharomyces cerevisiae Proteins Acetyltransferases Histone Acetyltransferases NuA4 protein, S cerevisiae
Authors & Affiliations
11 authors, click to expand affiliations / ORCID
Keogh Michael-Christopher
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Mennella Thomas A
Sawa Chika
Berthelet Sharon
Krogan Nevan J
Wolek Adam
Podolny Vladimir
Carpenter Laura Rocco
Greenblatt Jack F
Baetz Kristin
Buratowski Stephen
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Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
Published
2006-03-15
Pages
660-5
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC1413285
Subset
IM
Grants
NIGMS NIH HHS · R01 GM046498 · United States
NIGMS NIH HHS · GM46498 · United States
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