Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation.

Molecular chaperones play a central role in maintaining protein homeostasis. The highly conserved Hsp70 family of chaperones have major functions in folding of nascent peptides, protein refolding, and protein aggregate disassembly. In yeast, loss of two Hsp70 proteins, Ssa1 and Ssa2, is associated with decreased cellular growth and shortened lifespan.

Implications of the Actin Cytoskeleton on the Multi-Step Process of [] Prion Formation.

Yeast prions are self-perpetuating misfolded proteins that are infectious. In yeast, [] is the prion form of the Sup35 protein. While the study of [] has revealed important cellular mechanisms that contribute to prion propagation, the underlying cellular factors that influence prion formation are not well understood.