histone h4 lysine 12 acetylation regulates telomeric heterochromatin plasticity in saccharomyces cerevisiae12组蛋白h4赖氨酸乙酰化调节端粒的异染色质在酿酒酵母可塑性.pdfVIP

Histone H4 Lysine 12 Acetylation Regulates Telomeric Heterochromatin Plasticity in Saccharomyces cerevisiae 1 1 1 1 1 2 Bo O. Zhou , Shan-Shan Wang , Yang Zhang , Xiao-Hong Fu , Wei Dang , Brian A. Lenzmeier , Jin-Qiu Zhou1* 1 State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China, 2 School of Science, Buena Vista University, Storm Lake, Iowa, United States of America Abstract Recent studies have established that the highly condensed and transcriptionally silent heterochromatic domains in budding yeast are virtually dynamic structures. The underlying mechanisms for heterochromatin dynamics, however, remain obscure. In this study, we show that histones are dynamically acetylated on H4K12 at telomeric heterochromatin, and this acetylation regulates several of the dynamic telomere properties. Using a de novo heterochromatin formation assay, we surprisingly found that acetylated H4K12 survived the formation of telomeric heterochromatin. Consistently, the histone acetyltransferase complex NuA4 bound to silenced telomeric regions and acetylated H4K12. H4K12 acetylation prevented the over-accumulation of Sir proteins at telomeric heterochromatin and elimination of this acetylation caused defects in multiple telomere-related processes, including transcription, telomere replication, and recombination. Together, these data shed light on a potential histone acetylation mark within telomeric heterochromatin that contributes to telomere plasticity. Citation: Zhou BO, Wang S-S, Zhang Y, Fu X-H, Dang W, et al. (2011) Histone H4 Lysine 12 Acetylation Regulates Telomeri