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Papers In Press, published online ahead of print May 30, 2002
J. Biol. Chem, 10.1074/jbc.M200651200
Submitted on January 22, 2002
Revised on May 30, 2002
Accepted on May 30, 2002

Site-specific loss of acetylation upon phosphorylation of histone H3

Diane G. Edmondson, Judith K. Davie, Jenny Zhou, Banafsheh Mirnikjoo, Kelly Tatchell, and Sharon Y.R. Dent

Biochemistry and Molecular Biology Box 117, UT M.D. Anderson Cancer Center, Houston, Texas 77030

Corresponding Author: syr{at}mdacc.tmc.edu

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 (S10) facilitates acetylation of lysine 14 (K14) 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 S10 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 S10 to glutamate (S10E) or aspartate (S10D) causes almost complete loss of H3 acetylation at lysine 9 (K9) in vivo. Acetylation of K9 is also significantly reduced in cells bearing mutations in the Glc7 phosphatase that increase H3 phosphorylation levels. Mutation of S10 in H3 and the concomitant loss of K9 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 S10 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, K9 and K14, and they highlight the importance of these histone modifications to normal cell functions.


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