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http://purl.uniprot.org/citations/16815704http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16815704http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16815704http://www.w3.org/2000/01/rdf-schema#comment"

Background

Acetylation of histone H3 lysine 56 (K56Ac) occurs transiently in newly synthesized H3 during passage through S phase and is removed in G2. However, the physiologic roles and effectors of K56Ac turnover are unknown.

Results

The sirtuins Hst3p and, to a lesser extent, Hst4p maintain low levels of K56Ac outside of S phase. In hst3 hst4 mutants, K56 hyperacetylation nears 100%. Residues corresponding to the nicotinamide binding pocket of Sir2p are essential for Hst3p function, and H3 K56 deacetylation is inhibited by nicotinamide in vivo. Rapid inactivation of Hst3/Hst4p prior to S phase elevates K56Ac to 50% in G2, suggesting that K56-acetylated nucleosomes are assembled genome-wide during replication. Inducible expression of Hst3p in G1 or G2 triggers deacetylation of mature chromatin. Cells lacking Hst3/Hst4p exhibit many phenotypes: spontaneous DNA damage, chromosome loss, thermosensitivity, and acute sensitivity to genotoxic agents. These phenotypes are suppressed by mutation of histone H3 K56 into a nonacetylatable residue or by loss of K56Ac in cells lacking the histone chaperone Asf1.

Conclusions

Our results underscore the critical importance of Hst3/Hst4p in controlling histone H3 K56Ac and thereby maintaining chromosome integrity."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.org/dc/terms/identifier"doi:10.1016/j.cub.2006.06.023"xsd:string
http://purl.uniprot.org/citations/16815704http://purl.org/dc/terms/identifier"doi:10.1016/j.cub.2006.06.023"xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Cotter R.J."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Cotter R.J."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Boeke J.D."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Boeke J.D."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Celic I."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Celic I."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Griffith W.P."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Griffith W.P."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Masumoto H."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Masumoto H."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Meluh P."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Meluh P."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Verreault A."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/author"Verreault A."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/pages"1280-1289"xsd:string
http://purl.uniprot.org/citations/16815704http://purl.uniprot.org/core/pages"1280-1289"xsd:string
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