Yeast Hsp110 Has a Unique Substrate Binding Site Essential for Chaperone Activity

Abstract

110 kD Heat Shock proteins (Hsp110s) have unique chaperone activities in eukaryotic cytosol which assist in protein folding, transport and degradation, and preventing protein aggregation. They are chaperones by themselves and co-chaperones for Hsp70s, which is another essential class of molecular chaperones. Hsp110s show high activity in preventing protein aggregation through directly binding to polypeptide substrate and function to ensure the efficient folding activity of the Hsp70 chaperone machinery.