Histone Acetylation Inhibits RSC and Stabilizes the +1 Nucleosome

Mol Cell. 2018 Nov 1;72(3):594-600.e2. doi: 10.1016/j.molcel.2018.09.030. Epub 2018 Oct 25.

Abstract

The +1 nucleosome of yeast genes, within which reside transcription start sites, is characterized by histone acetylation, by the displacement of an H2A-H2B dimer, and by a persistent association with the RSC chromatin-remodeling complex. Here we demonstrate the interrelationship of these characteristics and the conversion of a nucleosome to the +1 state in vitro. Contrary to expectation, acetylation performs an inhibitory role, preventing the removal of a nucleosome by RSC. Inhibition is due to both enhanced RSC-histone interaction and diminished histone-chaperone interaction. Acetylation does not prevent all RSC activity, because stably bound RSC removes an H2A-H2B dimer on a timescale of seconds in an irreversible manner.

Keywords: NAP1; NuA4; SAGA; chromatin; chromatin-remodeling; transcription.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Acetylation
  • Animals
  • Chromatin Assembly and Disassembly / physiology*
  • DNA-Binding Proteins / metabolism
  • DNA-Binding Proteins / physiology*
  • Histones / metabolism
  • Histones / physiology*
  • Nucleosome Assembly Protein 1
  • Nucleosomes / physiology
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Rats
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology*
  • Trans-Activators / metabolism
  • Transcription Factors / metabolism
  • Transcription Factors / physiology*

Substances

  • DNA-Binding Proteins
  • Histones
  • Nucleosome Assembly Protein 1
  • Nucleosomes
  • RSC complex, S cerevisiae
  • SAGA complex, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • Acetyl Coenzyme A