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

Yu Wang, Scott P. Kallgren, Bharat D. Reddy, Karen Kuntz, Luis López-Maury, James Thompson, Stephen Watt, Ma Chun, Haitong Hou, Yang Shi, John R. Yates, Jürg Bähler, Matthew J. O'Connell, Songtao Jia

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

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.

Original languageEnglish
Pages (from-to)4386-4393
Number of pages8
JournalJournal of Biological Chemistry
Volume287
Issue number6
DOIs
StatePublished - 3 Feb 2012

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