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Originally published In Press as doi:10.1074/jbc.M200651200 on May 30, 2002

J. Biol. Chem., Vol. 277, Issue 33, 29496-29502, August 16, 2002
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Site-specific Loss of Acetylation upon Phosphorylation of Histone H3*

Diane G. EdmondsonDagger , Judith K. DavieDagger §, Jenny ZhouDagger , Banafsheh MirnikjooDagger , Kelly Tatchell, and Sharon Y. R. DentDagger ||

From the Dagger  Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 and the  Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, Shreveport, Louisiana 71130

Post-translational modification of histones is a central aspect of gene regulation. Emerging data indicate that modification at one site can influence modification of a second site. As one example, histone H3 phosphorylation at serine 10 (Ser10) facilitates acetylation of lysine 14 (Lys14) by Gcn5 in vitro (1, 2). In vivo, phosphorylation of H3 precedes acetylation at certain promoters. Whether H3 phosphorylation globally affects acetylation, or whether it affects all acetylation sites in H3 equally, is not known. We have taken a genetic approach to this question by mutating Ser10 in H3 to fix either a negative or a neutral charge at this position, followed by analysis of the acetylation states of the mutant histones using site-specific antibodies. Surprisingly, we find that conversion of Ser10 to glutamate (S10E) or aspartate (S10D) causes almost complete loss of H3 acetylation at lysine 9 (Lys9) in vivo. Acetylation of Lys9 is also significantly reduced in cells bearing mutations in the Glc7 phosphatase that increase H3 phosphorylation levels. Mutation of Ser10 in H3 and the concomitant loss of Lys9 acetylation has minimal effects on expression of a Gcn5-dependent reporter gene. However, synergistic growth defects are observed upon loss of GCN5 in cells bearing H3 Ser10 mutations that are reminiscent of delays in G2/M progression caused by combined loss of GCN5 and acetylation site mutations. Together these results demonstrate that H3 phosphorylation directly causes site-specific and opposite changes in acetylation levels of two residues within this histone, Lys9 and Lys14, and they highlight the importance of these histone modifications to normal cell functions.

* This work was supported in part by Welch Foundation Grant G1371 and National Institutes of Health Grant GM51189 (to S. Y. R. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by Fellowship PF00131 from the American Cancer Society.

|| To whom correspondence should be addressed (previously Sharon Y. Roth): Dept. of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030. Tel.: 713-794-4908; Fax: 713-790-0329; E-mail: syr@mdacc.tmc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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