Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase

Mol Cell. 2000 Dec;6(6):1297-307. doi: 10.1016/s1097-2765(00)00128-3.


The Esa1-containing NuA4 histone acetylase complex can interact with activation domains in vitro and stimulate transcription on reconstituted chromatin templates. In yeast cells, Esa1 is targeted to a small subset of promoters in an activator-specific manner. Esa1 is specifically recruited to ribosomal protein (RP) promoters, and this recruitment appears to require binding by Rap1 or Abf1. Esa1 is important for RP transcription, and Esa1 recruitment to RP promoters correlates with coordinate regulation of RP genes in response to growth stimuli. However, following Esa1 depletion, H4 acetylation decreases dramatically at many loci, but transcription is not generally affected. Therefore, the transcription-associated targeted recruitment of Esa1 to RP promoters occurs in a background of more global nontargeted acetylation that is itself not required for transcription.

Publication types

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

MeSH terms

  • Acetylation
  • Acetyltransferases / genetics
  • Acetyltransferases / immunology
  • Acetyltransferases / metabolism*
  • Binding Sites
  • Chromatin / genetics
  • Chromatin / metabolism
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation, Fungal*
  • Genes, Fungal / genetics
  • Genome, Fungal
  • Heat-Shock Proteins / genetics
  • Histone Acetyltransferases
  • Histones / metabolism
  • Oligonucleotide Array Sequence Analysis
  • Precipitin Tests
  • Promoter Regions, Genetic / genetics
  • Ribosomal Proteins / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / metabolism
  • Yeasts / enzymology*
  • Yeasts / genetics*


  • ABF1 protein, S cerevisiae
  • Chromatin
  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Histones
  • Ribosomal Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Acetyltransferases
  • Histone Acetyltransferases