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Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast.

ABSTRACT: Histone lysine acetylation has emerged as a key regulator of genome organization. However, with a few exceptions, the contribution of each acetylated lysine to cellular functions is not well understood because of the limited specificity of most histone acetyltransferases and histone deacetylases. Here we show that the Mst2 complex in Schizosaccharomyces pombe is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with Gcn5 to regulate global levels of H3K14 acetylation (H3K14ac). By analyzing the effect of H3K14ac loss through both enzymatic inactivation and histone mutations, we found that H3K14ac is critical for DNA damage checkpoint activation by directly regulating the compaction of chromatin and by recruiting chromatin remodeling protein complex RSC.

SUBMITTER: Wang Y

PROVIDER: S-EPMC3281674 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast.

Wang Yu Y Kallgren Scott P SP Reddy Bharat D BD Kuntz Karen K López-Maury Luis L Thompson James J Watt Stephen S Ma Chun C Hou Haitong H Shi Yang Y Yates John R JR Bähler Jürg J O'Connell Matthew J MJ Jia Songtao S

The Journal of biological chemistry 20111219 6

Histone lysine acetylation has emerged as a key regulator of genome organization. However, with a few exceptions, the contribution of each acetylated lysine to cellular functions is not well understood because of the limited specificity of most histone acetyltransferases and histone deacetylases. Here we show that the Mst2 complex in Schizosaccharomyces pombe is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with Gcn5 to regulate global levels of H3K14 acetylati ...[more]

PMID: 22184112

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Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3.

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Histone H3 lysine 36 methyltransferase mobilizes NER factors to regulate tolerance against alkylation damage in fission yeast.

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CBP/p300-mediated acetylation of histone H3 on lysine 56.

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Fission yeast Jmj2 reverses histone H3 lysine 4 tri-methylation

Project description:We compared the genomic localization of H3K4me3 in wild type and jmj2- S. pombe. Keywords: mutant vs wild-type

2007-08-14 | GSE8175 | GEO

Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.

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| S-EPMC2597342 | biostudies-literature

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

Project description: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.

| S-EPMC1459006 | biostudies-literature

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