Xhemalce B, Miller KM, Driscoll R, Masumoto H, Jackson SP, Kouzarides T, Verreault A, Arcangioli B. (2007) Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe. J Biol Chem. 282: 15040-15047.

In S. cerevisiae, acetylation of lysine 56 (K56) in the globular domain of histone H3 plays an important role in the response to genotoxic agents that interfere with DNA replication. However, the regulation and biological function of this modification are poorly defined in other eukaryotes. Here we show that K56 acetylation in Schizosaccharomyces pombe occurs transiently during passage through S-phase and is normally removed in G2. Genotoxic agents that cause DNA double-strand breaks during replication elicit a delay in deacetylation of histone H3 K56. In addition, mutant cells that cannot acetylate K56 are acutely sensitive to genotoxic agents that block DNA replication. Moreover, we show that Spbc342.06cp, a previously uncharacterized open reading frame (ORF) , encodes the functional homolog of S. cerevisiae Rtt109 and that this protein acetylates H3 K56 both in vitro and in vivo. Altogether, our results indicate that both the regulation of histone H3 K56 acetylation by its HAT and HDAC and its role in the DNA damage response are conserved among two distantly related yeast model organisms.