The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding

Goeckeler, Jennifer L.; Petruso, Anthony P.; Aguirre, Julia; Clement, Cristina C.; Chiosis, Gabriela; Brodsky, Jeffrey L.

doi:10.1016/j.febslet.2008.05.047

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Volume 582, Issue 16 , Pages 2393-2396, 9 July 2008

The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding

Edited by Felix Wieland

Jennifer L. Goeckeler
- University of Pittsburgh, Department of Biological Sciences, 274A Crawford Hall, Pittsburgh, PA 15260, USA
Anthony P. Petruso
- University of Pittsburgh, Department of Biological Sciences, 274A Crawford Hall, Pittsburgh, PA 15260, USA
Julia Aguirre
- Memorial Sloan-Kettering Cancer Center, Department of Medicine, New York, NY 10021, USA
Cristina C. Clement
- Memorial Sloan-Kettering Cancer Center, Department of Medicine, New York, NY 10021, USA
Gabriela Chiosis
- Memorial Sloan-Kettering Cancer Center, Department of Medicine, New York, NY 10021, USA
Jeffrey L. Brodsky
- University of Pittsburgh, Department of Biological Sciences, 274A Crawford Hall, Pittsburgh, PA 15260, USA
- Corresponding author. Fax: +1 412 624 4759.

Received 20 May 2008; received in revised form 27 May 2008; accepted 28 May 2008. published online 06 June 2008.

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 ∼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.