Histone H4 Lysine 12 Acetylation Regulates Telomeric Heterochromatin Plasticity in Saccharomyces cerevisiae

• DOI: 10.1371/journal.pgen.1001272
• Publication Date: 2011-01-13T21:25:54Z
• Authors: Bo O. Zhou; Shan-Shan Wang; Yang Zhang; Xiao-Hong Fu; Wei Dang; Brian A. Lenzmeier; Jin-Qiu Zhou
• Keywords: Heterochromatin protein 1; Histone H4; Euchromatin

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 histones dynamically acetylated on H4K12 at telomeric heterochromatin, acetylation regulates several of telomere properties. Using a de novo formation assay, surprisingly found survived heterochromatin. Consistently, histone acetyltransferase complex NuA4 bound to silenced regions H4K12. prevented over-accumulation Sir proteins elimination caused defects multiple telomere-related processes, including transcription, replication, recombination. Together, these data shed light potential mark within contributes plasticity.