Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.

Abstract excerpt

Protein translocation and folding in the endoplasmic reticulum of Saccharomyces cerevisiae involves two distinct Hsp70 chaperones, Lhs1p and Kar2p. Both proteins have the characteristic domain structure of the Hsp70 family consisting of a conserved N-terminal nucleotide binding domain and a C-terminal substrate binding domain. Kar2p is a canonical Hsp70 whose substrate binding activity is regulated by...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Adenosine Triphosphatases
• Share to Adenosine Triphosphate