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

David Kadosh, Kevin Struhl

Producción científica: Articlerevisión exhaustiva

272 Citas (Scopus)

Resumen

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.

Idioma originalEnglish (US)
Páginas (desde-hasta)5121-5127
Número de páginas7
PublicaciónMolecular and cellular biology
Volumen18
N.º9
DOI
EstadoPublished - 1998
Publicado de forma externa

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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