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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 publication




Journal article


The Journal of biological chemistry

Publication Date





4386 - 4393


Department of Biological Sciences, Columbia University, New York, New York 10027, USA.


Chromatin, Schizosaccharomyces, DNA Damage, Acetyltransferases, Schizosaccharomyces pombe Proteins, Histones, DNA, Fungal, Acetylation, Mutation