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PMID: 16627621 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 103 ·No. 18 ·2006-05-02 ·Pages 6988-93

Recht J, Tsubota T, Tanny JC, Diaz RL, Berger JM, Zhang X, Garcia BA, Shabanowitz J, Burlingame AL, Hunt DF, Kaufman PD, Allis CD

Abstract

Histone acetylation affects many nuclear processes including transcription, chromatin assembly, and DNA damage repair. Acetylation of histone H3 lysine 56 (H3 K56ac) in budding yeast occurs during mitotic S phase and persists during DNA damage repair. Here, we show that H3 K56ac is also present during premeiotic S phase and is conserved in fission yeast. Furthermore, the H3 K56ac modification is not observed in the absence of the histone chaperone Asf1. asf1delta and H3 K56R mutants exhibit similar sensitivity to DNA damaging agents. Mutational analysis of Asf1 demonstrates that DNA damage sensitivity correlates with (i) decreased levels of H3 K56ac and (ii) a region implicated in histone binding. In contrast, multiple asf1 mutants that are resistant to DNA damage display WT levels of K56ac. These data suggest that maintenance of H3 K56 acetylation is a primary contribution of Asf1 to genome stability in yeast.

MeSH Terms
Acetylation Cell Cycle Proteins/chemistry,genetics,metabolism DNA Damage Histones/metabolism Lysine/metabolism Meiosis/physiology Models, Molecular Molecular Chaperones/genetics,metabolism Phenotype Protein Conformation S Phase/physiology Saccharomyces cerevisiae/cytology,genetics,metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism Spores, Fungal/metabolism
Chemicals
ASF1 protein, S cerevisiae Cell Cycle Proteins Histones Molecular Chaperones Saccharomyces cerevisiae Proteins Lysine
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Recht J
Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10021, USA.
Tsubota T
Tanny J C
Diaz R L
Berger J M
Zhang X
Garcia B A
Shabanowitz J
Burlingame A L
Hunt D F
Kaufman P D
Allis C D
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0601676103
Published
2006-05-02
Epub
2006-00-20
Pages
6988-93
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1459006
Subset
IM
Grants
NCI NIH HHS · R01 CA077373 · United States
NCRR NIH HHS · RR01614 · United States
NIGMS NIH HHS · R01 GM037537 · United States
NIGMS NIH HHS · R37 GM053512 · United States
NIGMS NIH HHS · GM53512 · United States
NCRR NIH HHS · P41 RR001614 · United States
External Links
PubMed source DOI: 10.1073/pnas.0601676103 PMC Full Text View journal details
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