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| J. Biol. Chem. Nov (2006); 281(44):33739-48 | |
| Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p- | |
| Catlett MG, Kaplan KB | |
| Section of Molecular and Cellular Biology, University of California, Davis, California 95616, USA- | |
| Abstract: Sgt1p is a conserved, essential protein required for kinetochore assembly in both yeast and animal cells- Sgt1p has homology to both TPR and p23 domains, sequences often found in proteins that interact with and regulate the molecular chaperone, Hsp90- The presence of these domains and the recent findings that Sgt1p interacts with Hsp90 has led to the speculation that Sgt1p and Hsp90 form a co-chaperone complex- To test this possibility, we have used purified recombinant proteins to characterize the in vitro interactions between yeast Sgt1p and Hsp82p -an Hsp90 homologue in yeast-- We show that Sgt1p interacts directly with Hsp82p via its p23 homology region in a nucleotide-dependent manner- However, Sgt1p binding does not alter the enzymatic activity of Hsp82p, suggesting that it is distinct from other co-chaperones- We find that Sgt1p can form a ternary chaperone complex with Hsp82p and Sti1p, a well characterized Hsp90 co-chaperone- Sgt1p interacts with its binding partner Skp1p through its TPR domains and links Skp1p to the core Hsp82p-Sti1p co-chaperone complex- The multidomain nature of Sgt1p and its ability to bridge the interaction between Skp1p and Hsp82p argue that Sgt1p acts as a "client adaptor" recruiting specific clients to Hsp82p co-chaperone complexes- | |
| [PUBMED: 16945921] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| 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. |