Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex

Angew Chem Int Ed Engl. 2016 Jul 25;55(31):8918-22. doi: 10.1002/anie.201603106. Epub 2016 Jun 8.

Abstract

Transcriptional regulation can be established by various post-translational modifications (PTMs) on histone proteins in the nucleosome and by nucleobase modifications on chromosomal DNA. Functional consequences of histone O-GlcNAcylation (O-GlcNAc=O-linked β-N-acetylglucosamine) are largely unexplored. Herein, we generate homogeneously GlcNAcylated histones and nucleosomes by chemical post-translational modification. Mass-spectrometry-based quantitative interaction proteomics reveals a direct interaction between GlcNAcylated nucleosomes and the "facilitates chromatin transcription" (FACT) complex. Preferential binding of FACT to GlcNAcylated nucleosomes may point towards O-GlcNAcylation as one of the triggers for FACT-driven transcriptional control.

Keywords: GlcNAcylation; epigenetics; nucleosomes; protein modifications; synthetic biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / chemistry
  • Acetylglucosamine / metabolism*
  • Chromatin / chemistry
  • Chromatin / metabolism*
  • Glycosylation
  • Models, Molecular
  • Nucleosomes / chemistry
  • Nucleosomes / metabolism*
  • Protein Processing, Post-Translational

Substances

  • Chromatin
  • Nucleosomes
  • Acetylglucosamine