Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo

Mol Cell Biol. 1998 Sep;18(9):5121-7. doi: 10.1128/MCB.18.9.5121.

Abstract

Eukaryotic organisms contain a multiprotein complex that includes Rpd3 histone deacetylase and the Sin3 corepressor. The Sin3-Rpd3 complex is recruited to promoters by specific DNA-binding proteins, whereupon it represses transcription. By directly analyzing the chromatin structure of a repressed promoter in yeast cells, we demonstrate that transcriptional repression is associated with localized histone deacetylation. Specifically, we observe decreased acetylation of histones H3 and H4 (preferentially lysines 5 and 12) that depends on the DNA-binding repressor (Ume6), Sin3, and Rpd3. Mapping experiments indicate that the domain of histone deacetylation is highly localized, occurring over a range of one to two nucleosomes. Taken together with previous observations, these results define a novel mechanism of transcriptional repression which involves targeted recruitment of a histone-modifying activity and localized perturbation of chromatin structure.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromatin / genetics*
  • Chromatin / metabolism
  • Chromosome Mapping
  • Enzyme Repression
  • Fungal Proteins / metabolism
  • Histone Deacetylases / biosynthesis*
  • Histone Deacetylases / genetics*
  • Histones / metabolism
  • Lysine
  • Nucleosomes / genetics
  • Nucleosomes / metabolism
  • Promoter Regions, Genetic*
  • Repressor Proteins / metabolism*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / metabolism*
  • Transcription, Genetic

Substances

  • Chromatin
  • Fungal Proteins
  • Histones
  • Nucleosomes
  • Repressor Proteins
  • SIN3 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • RPD3 protein, S cerevisiae
  • Histone Deacetylases
  • Lysine