|
|
| Biochemistry Dec (2006); 45(50):15075-84 | |
| Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1- | |
| Shaner L, Sousa R, Morano KA | |
| Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030, USA- | |
| Abstract: SSE1 and SSE2 encode the essential yeast members of the Hsp70-related Hsp110 molecular chaperone family- Both mammalian Hsp110 and the Sse proteins functionally interact with cognate cytosolic Hsp70s as nucleotide exchange factors- We demonstrate here that Sse1 forms high-affinity -Kd approximately 10-8 M- heterodimeric complexes with both yeast Ssa and mammalian Hsp70 chaperones and that binding of ATP to Sse1 is required for binding to Hsp70s- Sse1-Hsp70 heterodimerization confers resistance to exogenously added protease, indicative of conformational changes in Sse1 resulting in a more compact structure- The nucleotide binding domains of both Sse1-2 and the Hsp70s dictate interaction specificity and are sufficient for mediating heterodimerization with no discernible contribution from the peptide binding domains- In support of a strongly conserved functional interaction between Hsp110 and Hsp70, Sse1 is shown to associate with and promote nucleotide exchange on human Hsp70- Nucleotide exchange activity by Sse1 is physiologically significant, as deletion of both SSE1 and the Ssa ATPase stimulatory protein YDJ1 is synthetically lethal- The Hsp110 family must therefore be considered an essential component of Hsp70 chaperone biology in the eukaryotic cell- | |
| [PUBMED: 17154545] |   |
| 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. |