Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Nov (2006); 0: Nucleotide-dependent interaction of yeast Hsp90 with the co-chaperone proteins Sti1, Cpr6 and Sba1- Johnson JL, Halas A, Flom G Department of Microbiology, Molecular Biology and Biochemistry and the Center for Reproductive Biology, University of Idaho, Moscow, ID 83844-3052- Abstract: The ATP-dependent molecular chaperone Hsp90 and partner co-chaperone proteins are required for the folding and activity of diverse cellular client proteins, including steroid hormone receptors and multiple oncogenic kinases- Hsp90 undergoes nucleotide-dependent conformational changes but little is known about how these changes are coupled to client protein activation- In order to clarify how nucleotide affects Hsp90 interactions with co-chaperone proteins, we monitored assembly of wild-type and mutant Hsp90 with Sti1, Sba1 and Cpr6 in yeast cell extracts- Wild-type Hsp90 bound Sti1 in a nucleotide-independent manner, while Sba1 and Cpr6 specifically and independently interacted with Hsp90 in the presence of the non-hydrolyzable analog of ATP, AMP-PNP- Alterations in Hsp90 residues that contribute to ATP binding or hydrolysis prevented or altered Sba1 and Cpr6 interaction; additional alterations affected the specificity of Cpr6 interaction- Some mutant forms of Hsp90 also displayed reduced Sti1 interaction in the presence of nucleotide- These studies indicate that cycling of Hsp90 between the nucleotide-free, open conformation and the ATP-bound, closed conformation is influenced by residues both within and outside the N-terminal ATPase domain and that these conformational changes have dramatic effects on interaction with co-chaperone proteins- [PUBMED: 17101799] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.