Format

Send to

Choose Destination
FEBS Lett. 2008 Jul 9;582(16):2393-6. doi: 10.1016/j.febslet.2008.05.047. Epub 2008 Jun 6.

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

Author information

1
University of Pittsburgh, Department of Biological Sciences, 274A Crawford Hall, Pittsburgh, PA 15260, USA.

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 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.

PMID:
18539149
PMCID:
PMC2504362
DOI:
10.1016/j.febslet.2008.05.047
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center