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Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms.

There is a close relationship between histone acetylation and ATP-dependent chromatin remodeling that is not fully understood. We show that acetylation of histone H3 tails affects SWI/SNF (mating type switching/ sucrose non fermenting) and RSC (remodels structure of chromatin) remodeling in several distinct ways. Acetylation of the histone H3 N-terminal tail facilitated recruitment and nucleosome mobilization by the ATP-dependent chromatin remodelers SWI/SNF and RSC. Tetra-acetylated H3, but not tetra-acetylated H4 tails, increased the affinity of RSC and SWI/SNF for nucleosomes while also changing the subunits of SWI/SNF that interact with the H3 tail. The enhanced recruitment of SWI/SNF due to H3 acetylation is bromodomain dependent, but is not further enhanced by additional bromodomains found in RSC. The combined effect of H3 acetylation and transcription activators is greater than either separately which suggests they act in parallel to recruit SWI/SNF. Besides enhancing recruitment, H3 acetylation increased nucleosome mobilization and H2A/H2B displacement by RSC and SWI/SNF in a bromodomain dependent manner and to a lesser extent enhanced ATP hydrolysis independent of bromodomains. H3 and H4 acetylation did not stimulate disassembly of adjacent nucleosomes in short arrays by SWI/SNF or RSC. These data illustrate how histone acetylation modulates RSC and SWI/SNF function, and provide a mechanistic insight into their collaborative efforts to remodel chromatin.

Pubmed ID: 21749977

Authors

  • Chatterjee N
  • Sinha D
  • Lemma-Dechassa M
  • Tan S
  • Shogren-Knaak MA
  • Bartholomew B

Journal

Nucleic acids research

Publication Data

October 26, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM 48413
  • Agency: NIGMS NIH HHS, Id: GM 79663
  • Agency: NIGMS NIH HHS, Id: GM060489
  • Agency: NIGMS NIH HHS, Id: R01 GM048413
  • Agency: NIGMS NIH HHS, Id: R01 GM060489

Mesh Terms

  • Acetylation
  • Adenosine Triphosphate
  • Animals
  • Chromatin Assembly and Disassembly
  • DNA-Binding Proteins
  • Histones
  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • Xenopus laevis