The Swi2/Snf2 bromodomain is important for the full binding and remodeling activity of the SWI/SNF complex on H3- and H4-acetylated nucleosomes

Ann N Y Acad Sci. 2008 Sep:1138:366-75. doi: 10.1196/annals.1414.038.

Abstract

The SWI/SNF chromatin-remodeling complex contains a bromodomain in its Swi2/Snf2 subunit that helps tether it to acetylated promoter nucleosomes. To study the importance of this bromodomain in the SWI/SNF complex, we have compared the nucleosome-binding and the chromatin-remodeling activities of the SWI/SNF to a mutant complex that lacks the Swi2/Snf2 bromodomain. Here we show that the SWI/SNF complex deleted of the Swi2/Snf2 bromodomain cannot bind to SAGA- or NuA4-acetylated nucleosomes as well as the wild-type complex. Moreover, we show that this reduced binding leads to partial remodeling of these acetylated nucleosome templates by the Deltabromodomain SWI/SNF complex. These results demonstrate that the Swi2/Snf2 bromodomain is required for the full binding and functional activity of the SWI/SNF complex on H3- and H4-acetylated nucleosomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Adenosine Triphosphatases
  • DNA-Binding Proteins / metabolism*
  • Histones / metabolism*
  • Nucleosomes / metabolism*
  • Protein Binding
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • Histones
  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Adenosine Triphosphatases
  • SNF2 protein, S cerevisiae