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The yeast Hsp110, Sse1p, exhibits high‐affinity peptide binding
Author(s) -
Goeckeler Jennifer L.,
Petruso Anthony P.,
Aguirre Julia,
Clement Cristina C.,
Chiosis Gabriela,
Brodsky Jeffrey L.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.05.047
Subject(s) - peptide , atp hydrolysis , yeast , biochemistry , hsp70 , atpase , hydrolysis , chemistry , biology , enzyme , heat shock protein , gene
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 ∼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.