Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis
Authors
Recht, J.Tsubota, Toshiaki
Tanny, J. C.
Diaz, R. L.
Berger, James M.
Zhang, X.
Garcia, B. A.
Shabanowitz, J.
Burlingame, A. L.
Hunt, D. F.
Kaufman, Paul D.
Allis, C. David
UMass Chan Affiliations
Program in Gene Function and ExpressionDocument Type
Journal ArticlePublication Date
2006-04-22Keywords
AcetylationCell Cycle Proteins
DNA Damage
Histones
Lysine
Meiosis
Models, Molecular
Molecular Chaperones
Phenotype
Protein Conformation
S Phase
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Spores, Fungal
Genetics and Genomics
Metadata
Show full item recordAbstract
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.Source
Proc Natl Acad Sci U S A. 2006 May 2;103(18):6988-93. Epub 2006 Apr 20. Link to article on publisher's siteDOI
10.1073/pnas.0601676103Permanent Link to this Item
http://hdl.handle.net/20.500.14038/43905PubMed ID
16627621Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1073/pnas.0601676103