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J. Biol. Chem., Vol. 280, Issue 28, 25949-25952, July 15, 2005

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Characterization of Lysine 56 of Histone H3 as an Acetylation Site in Saccharomyces cerevisiae^*

Anil Ozdemir, Salvatore Spicuglia, Edwin Lasonder, Michiel Vermeulen, Coen Campsteijn, Hendrik G. Stunnenberg, and Colin Logie

From the Department of Molecular Biology, Nijmegen Center for Molecular Life Sciences, Radboud University, 6500 HB Nijmegen, The Netherlands

Post-translational histone modifications abound and regulate multiple nuclear processes. Most modifications are targeted to the amino-terminal domains of histones. Here we report the identification and characterization of acetylation of lysine 56 within the core domain of histone H3. In the crystal structure of the nucleosome, lysine 56 contacts DNA. Phenotypic analysis suggests that lysine 56 is critical for histone function and that it modulates formamide resistance, ultraviolet radiation sensitivity, and sensitivity to hydroxyurea. We show that the acetylated form of histone H3 lysine 56 (H3-K56) is present during interphase, metaphase, and S phase. Finally, reverse genetic analysis indicates that none of the known histone acetyltransferases is solely responsible for H3-K56 acetylation in Saccharomyces cerevisiae.

Received for publication, April 25, 2005 , and in revised form, May 10, 2005.

^* 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 Tables 1 and 2.

To whom correspondence should be addressed: NCMLS, P. O. Box 9101, 6500 HB Nijmegen, The Netherlands. Tel.: 31-24-3610525; Fax: 31-24-3610520; E-mail: c.logie{at}ncmls.ru.nl.

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