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J. Biol. Chem., Vol. 282, Issue 20, 15040-15047, May 18, 2007

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Regulation of Histone H3 Lysine 56 Acetylation in Schizosaccharomyces pombe^*

Blerta Xhemalce¹, Kyle M. Miller^¶, Robert Driscoll^¶2, Hiroshi Masumoto^||3, Stephen P. Jackson^¶4, Tony Kouzarides⁴, Alain Verreault^**5, and Benoît Arcangioli⁶

From the Unité de la Dynamique du Génome, Institut Pasteur, 25 rue du Dr. Roux, 75724, Paris Cedex 15, France, ^**Institut de Recherche en Immunologie et Cancérologie, Université de Montréal, CP 6128, Succursale Centre-Ville, Montréal, Québec H3C 3J7, Canada, The Wellcome Trust and Cancer Research and Department of Pathology, Tennis Court Road, Cambridge CB2 1QN, United Kingdom, ^¶The Wellcome Trust and Cancer Research Gurdon Institute and the Department of Zoology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, United Kingdom, and ^||Laboratories for Biomolecular Networks, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan

In Saccharomyces cerevisiae, acetylation of lysine 56 (Lys-56) in the globular domain of histone H3 plays an important role in 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 Lys-56 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 Lys-56. In addition, mutant cells that cannot acetylate Lys-56 are acutely sensitive to genotoxic agents that block DNA replication. Moreover, we show that Spbc342.06cp, a previously uncharacterized open reading frame, encodes the functional homolog of S. cerevisiae Rtt109, and that this protein acetylates H3 Lys-56 both in vitro and in vivo. Altogether, our results indicate that both the regulation of histone H3 Lys-56 acetylation by its histone acetyltransferase and histone deacetylase and its role in the DNA damage response are conserved among two distantly related yeast model organisms.

Received for publication, February 8, 2007 , and in revised form, March 15, 2007.

^* This work was supported by a fellowship from the Ministère de l'Education Nationale, de la Recherche et de la Technologie, and the Association pour la Recherche sur le Cancer (to B. X.) and a grant from the Human Frontiers Science Program (to B. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

² Supported by United Kingdom Biotechnology and Biological Sciences Research Council Cooperative Awards in Science and Engineering studentship with KuDOS Pharmaceuticals and by a Cancer Research United Kingdom programme grant (to S. P. J.).

³ Supported by the Ministry of Education, Culture, Sports, Science, and Technology of Japan.

⁴ Supported by core infrastructure funding from Cancer Research United Kingdom and the Wellcome Trust.

⁵ Supported by the Association for International Cancer Research and the Canadian Institutes for Health Research.

¹ To whom correspondence may be addressed. b.xhemalce{at}gurdon.cam.ac.uk. Tel.: 44-1223-334-111; Fax: 44-1223-334-089. ⁶ To whom correspondence may be addressed. barcan{at}pasteur.fr. Tel.: 33-1-4568-8454; Fax: 33-1-4568-8960.

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