Histone H3 lysine 36 methylation targets the Isw1b remodeling complex to chromatin

Mol Cell Biol. 2012 Sep;32(17):3479-85. doi: 10.1128/MCB.00389-12. Epub 2012 Jul 2.

Abstract

Histone H3 lysine 36 methylation is a ubiquitous hallmark of productive transcription elongation. Despite the prevalence of this histone posttranslational modification, however, the downstream functions triggered by this mark are not well understood. In this study, we showed that H3K36 methylation promoted the chromatin interaction of the Isw1b chromatin-remodeling complex in Saccharomyces cerevisiae. Similar to H3K36 methylation, Isw1b was found at the mid- and 3' regions of transcribed genes genome wide, and its presence at active genes was dependent on H3K36 methylation and the PWWP domain of the Isw1b subunit, Ioc4. Moreover, purified Isw1b preferentially interacted with recombinant nucleosomes that were methylated at lysine 36, and this interaction also required the Ioc4 PWWP domain. While H3K36 methylation has been shown to regulate the binding of numerous factors, this is the first time that it has been shown to facilitate targeting of a chromatin-remodeling complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / analysis
  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Chromatin / chemistry
  • Chromatin / metabolism*
  • DNA-Binding Proteins / analysis
  • DNA-Binding Proteins / metabolism*
  • Genes, Fungal
  • Histones / chemistry
  • Histones / metabolism*
  • Lysine / chemistry
  • Lysine / metabolism*
  • Methylation
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / analysis
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcriptional Activation

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Histones
  • IOC4 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Adenosine Triphosphatases
  • ISW1 protein, S cerevisiae
  • Lysine