The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle

Nat Struct Mol Biol. 2013 Sep;20(9):1119-21. doi: 10.1038/nsmb.2641. Epub 2013 Aug 11.

Abstract

The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Crystallography, X-Ray
  • Macromolecular Substances / chemistry
  • Macromolecular Substances / isolation & purification
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Nucleosomes / metabolism*
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Stability
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Silent Information Regulator Proteins, Saccharomyces cerevisiae / chemistry*
  • Silent Information Regulator Proteins, Saccharomyces cerevisiae / genetics
  • Silent Information Regulator Proteins, Saccharomyces cerevisiae / metabolism*
  • Static Electricity

Substances

  • Macromolecular Substances
  • Nucleosomes
  • Recombinant Proteins
  • SIR3 protein, S cerevisiae
  • Silent Information Regulator Proteins, Saccharomyces cerevisiae

Associated data

  • PDB/4LD9