[HTML][HTML] Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo
J de Keyzer, GJ Steel, SJ Hale, D Humphries… - Journal of biological …, 2009 - ASBMB
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 cochaperones that promote either
ATP hydrolysis or nucleotide exchange. Lhs1p is a member of the Grp170/Lhs1p subfamily …
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 cochaperones that promote either
ATP hydrolysis or nucleotide exchange. Lhs1p is a member of the Grp170/Lhs1p subfamily …