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

http://www.ncbi.nlm.nih.gov/pubmed/21454705

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 RIS Download

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

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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

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