The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding Journal Article
| Authors: | Goeckeler, J. L.; Petruso, A. P.; Aguirre, J.; Clement, C. C.; Chiosis, G.; Brodsky, J. L. |
| Article Title: | The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding |
| Abstract: | Hsp110s are divergent relatives of Hsp70 chaperones that hydrolyze ATP. Hsp110s serve as Hsp70 nucleotide exchange factors and act directly to maintain polypeptide solubility. To date, the impact of peptide binding on Hsp110 ATPase activity is unknown and an Hsp110/peptide affinity has not been measured. We now report on a peptide that binds to the yeast Hsp110, Sse1p, with a KD of ∼2 nM. Surprisingly, the binding of this peptide fails to stimulate Sse1p ATP hydrolysis. Moreover, an Hsp70-binding peptide is unable to associate with Sse1p, suggesting that Hsp70s and Hsp110s possess partially distinct peptide recognition motifs. © 2008 Federation of European Biochemical Societies. |
| Keywords: | nonhuman; binding affinity; sensitivity analysis; animal cell; phenotype; protein metabolism; fluorescence; protein binding; protein purification; protein synthesis; peptides; heat shock protein 70; yeast; saccharomyces cerevisiae proteins; adenosine triphosphate; enzyme specificity; adenosine triphosphatase; fluorescence analysis; adenosine triphosphatases; hydrolysis; hsp70; hsp70 heat-shock proteins; chaperone; nucleotide exchange factor; atpase; molecular chaperone; heat shock protein 110; ro antibody; stage specific embryo antigen 1; hsp110 heat-shock proteins; hsp40 heat-shock proteins |
| Journal Title: | FEBS Letters |
| Volume: | 582 |
| Issue: | 16 |
| ISSN: | 0014-5793 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2008-07-09 |
| Start Page: | 2393 |
| End Page: | 2396 |
| Language: | English |
| DOI: | 10.1016/j.febslet.2008.05.047 |
| PUBMED: | 18539149 |
| PROVIDER: | scopus |
| PMCID: | PMC2504362 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 9" - "Export Date: 17 November 2011" - "CODEN: FEBLA" - "Source: Scopus" |
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