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Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.

Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules to form a symmetrical holoenzyme with a ∼12 Å diameter central hole. Vps75 and Rtt109 residues that mediate complex formation in the crystals are also important for Rtt109-Vps75 interaction and H3K9/K27 acetylation both in vitro and in yeast cells. The same Rtt109 residues do not participate in Asf1-mediated Rtt109 acetylation in vitro or H3K56 acetylation in yeast cells, demonstrating that Asf1 and Vps75 dictate Rtt109 substrate specificity through distinct mechanisms. These studies also suggest that Vps75 binding stimulates Rtt109 catalytic activity by appropriately presenting the H3-H4 substrate within the central cavity of the holoenzyme to promote H3K9/K27 acetylation of new histones before deposition.

Pubmed ID: 21256037


  • Tang Y
  • Holbert MA
  • Delgoshaie N
  • Wurtele H
  • Guillemette B
  • Meeth K
  • Yuan H
  • Drogaris P
  • Lee EH
  • Durette C
  • Thibault P
  • Verreault A
  • Cole PA
  • Marmorstein R


Structure (London, England : 1993)

Publication Data

February 9, 2011

Associated Grants

  • Agency: NIA NIH HHS, Id: P01 AG031862
  • Agency: NIGMS NIH HHS, Id: R01 GM060293
  • Agency: NIGMS NIH HHS, Id: R01 GM060293
  • Agency: NIGMS NIH HHS, Id: R01 GM060293-11
  • Agency: NIGMS NIH HHS, Id: R01 GM062437

Mesh Terms

  • Acetyl Coenzyme A
  • Acetylation
  • Cell Cycle Proteins
  • Chromatin Assembly and Disassembly
  • Crystallography, X-Ray
  • Gene Expression
  • Genomic Instability
  • Histone Acetyltransferases
  • Histones
  • Humans
  • Lysine
  • Models, Molecular
  • Molecular Chaperones
  • Mutagenesis, Site-Directed
  • Protein Binding
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity