Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10

被引:75
作者
Ahn, Sung-Hee
Diaz, Robert L.
Grunstein, Michael
Allis, C. David
机构
[1] Rockefeller Univ, Lab Chromatin Biol, New York, NY 10021 USA
[2] Univ Calif Los Angeles, Sch Med, Dept Biol Chem, Los Angeles, CA 90095 USA
[3] Univ Calif Los Angeles, Mol Biol Inst, Los Angeles, CA 90095 USA
关键词
D O I
10.1016/j.molcel.2006.09.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chromatin alterations, induced by covalent histone modifications, mediate a wide range of DNA-templated processes, including apoptosis. Apoptotic chromatin condensation has been causally linked to the phosphorylation of histone H2B (serine 14 in human; serine 10 in yeast, H2BS10ph) in human and yeast cells. Here, we extend these studies by demonstrating a unidirectional, crosstalk pathway between H2BS10 phosphorylation and lysine 11 acetylation (H2BK11ac) in yeast. We demonstrate that the H2BK11 acetyl mark, which exists in growing yeast, is removed upon H2O2 treatment but before H2BS10ph occurs, in a unidirectional fashion. H2BK11Q mutants are resistant to cell death elicited by H2O2, while H2BK11R mutants that mimic deacetylation promote cell death. Our results suggest that Hos3 HDAC deacetylates H2BK11ac, which in turn mediates H2BS10ph by Ste20 kinase. Together, these studies underscore a concerted series of enzyme reactions governing histone modifications that promote a switch from cell proliferation to cell death.
引用
收藏
页码:211 / 220
页数:10
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