Goeckeler JL, et al. (2008) The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding. FEBS Lett 582(16):2393-6
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 K(D) of approximately 2nM. 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.
|Status: Published||Type: Journal Article||PubMed ID: 18539149|
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Number of different genes curated to this paper: 4
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