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PMID: 12917332 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast.

Molecular and cellular biology ·Vol. 23 ·No. 17 ·2003-09-00 ·Pages 6086-102

Le Masson I, Yu DY, Jensen K, Chevalier A, Courbeyrette R, Boulard Y, Smith MM, Mann C

Abstract

Yaf9 is one of three proteins in budding yeast containing a YEATS domain. We show that Yaf9 is part of a large complex and that it coprecipitates with three known subunits of the NuA4 histone acetyltransferase. Although Esa1, the catalytic subunit of NuA4, is essential for viability, we found that yaf9 Delta mutants are viable but hypersensitive to microtubule depolymerizing agents and synthetically lethal with two different mutants of the mitotic apparatus. Microtubules depolymerized more readily in the yaf9Delta mutant compared to the wild type in the presence of nocodazole, and recovery of microtubule polymerization and cell division from limiting concentrations of nocodazole was inhibited. Two other NuA4 mutants (esa1-1851 and yng2 Delta) and nonacetylatable histone H4 mutants were also sensitive to benomyl. Furthermore, wild-type budding yeast were more resistant to benomyl when grown in the presence of trichostatin A, a histone deacetylase inhibitor. These results strongly suggest that acetylation of histone H4 by NuA4 is required for the cellular resistance to spindle stress.

MeSH Terms
Acetylation Acetyltransferases/antagonists & inhibitors,genetics,metabolism Actins/genetics Amino Acid Sequence Benomyl/pharmacology Chromatin/metabolism Enzyme Inhibitors/pharmacology Fungal Proteins/drug effects,genetics,metabolism Gene Expression Regulation, Fungal Histone Acetyltransferases Hydroxamic Acids/pharmacology Membrane Proteins/genetics,metabolism Molecular Sequence Data Mutation Nocodazole/pharmacology Nuclear Proteins/genetics,metabolism Protein Structure, Tertiary Protein Subunits Saccharomyces cerevisiae/drug effects,physiology Saccharomyces cerevisiae Proteins/antagonists & inhibitors,drug effects,genetics,metabolism Sequence Homology, Amino Acid Spindle Apparatus/drug effects,genetics Transcription, Genetic
Chemicals
Act1 protein, S cerevisiae Actins Arp4 protein, S cerevisiae Chromatin Enzyme Inhibitors Fungal Proteins Hydroxamic Acids MPS2 protein, S cerevisiae Membrane Proteins Nuclear Proteins Protein Subunits Saccharomyces cerevisiae Proteins YAF9 protein, S cerevisiae trichostatin A Acetyltransferases Eaf3 protein, S cerevisiae Yng2 protein, S cerevisiae Esa1 protein, S cerevisiae Histone Acetyltransferases Nocodazole Benomyl
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Le Masson Ivan
Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, 91191 Gif-sur-Yvette, France.
Yu David Y
Jensen Kurt
Chevalier Anne
Courbeyrette Régis
Boulard Yves
Smith M Mitchell
Mann Carl
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
2003-09-00
Pages
6086-102
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC180919
Subset
IM
Grants
NIGMS NIH HHS · R01 GM028920 · United States
NIGMS NIH HHS · GM28920 · United States
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