Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s Histone deacetylase complex and to repress spurious transcription

Bing Li, Jessica Jackson, Matthew D. Simon, Brian Fleharty, Madelaine Gogol, Chris Seidel, Jerry L. Workman, Ali Shilatifard

Research output: Contribution to journalArticle

107 Scopus citations

Abstract

Histone methylation is associated with both transcription activation and repression. However, the functions of different states of methylation remain largely elusive. Here, using methyllysine analog technology, we demonstrate that the histone deacetylase complex, Rpd3S, can distinguish the nucleosomes methylated to different extents and that K36me2 is sufficient to target Rpd3S in vitro. Through a genome-wide survey, we identified a few mutants in which the level of K36me3 is significantly reduced, whereas the level of K36me2 is sustained. Transcription analysis and genome-wide histone modification studies on these mutants suggested that K36me2 is sufficient to target Rpd3S in vivo, thereby maintaining a functional Set2-Rpd3S pathway.

Original languageEnglish (US)
Pages (from-to)7970-7976
Number of pages7
JournalJournal of Biological Chemistry
Volume284
Issue number12
DOIs
StatePublished - Mar 20 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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