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Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.

The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)(2) tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)(2). Investigation of Vps75-Rtt109-(H3-H4)(2) and Vps75-(H3-H4)(2) complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.

Pubmed ID: 21454705


  • Su D
  • Hu Q
  • Zhou H
  • Thompson JR
  • Xu RM
  • Zhang Z
  • Mer G


The Journal of biological chemistry

Publication Data

May 6, 2011

Associated Grants

  • Agency: NCI NIH HHS, Id: CA132878
  • Agency: NIGMS NIH HHS, Id: GM81838
  • Agency: NCI NIH HHS, Id: R01 CA132878
  • Agency: NCI NIH HHS, Id: R01 CA132878-03
  • Agency: NCI NIH HHS, Id: R01 CA132878-04
  • Agency: NCI NIH HHS, Id: R01 CA132878-05

Mesh Terms

  • Acetylation
  • Crystallography, X-Ray
  • Histone Acetyltransferases
  • Histones
  • Molecular Chaperones
  • Multiprotein Complexes
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Structure-Activity Relationship