[HTML][HTML] J domain co-chaperone specificity defines the role of BiP during protein translocation
Hsp70 chaperones can potentially interact with one of several J domain-containing Hsp40
co-chaperones to regulate distinct cellular processes. However, features within Hsp70s that
determine Hsp40 specificity are undefined. To investigate this question, we introduced
mutations into the ER-lumenal Hsp70, BiP/Kar2p, and found that an R217A substitution in
the J domain-interacting surface of BiP compromised the physical and functional interaction
with Sec63p, an Hsp40 required for ER translocation. In contrast, interaction with Jem1p, an …
co-chaperones to regulate distinct cellular processes. However, features within Hsp70s that
determine Hsp40 specificity are undefined. To investigate this question, we introduced
mutations into the ER-lumenal Hsp70, BiP/Kar2p, and found that an R217A substitution in
the J domain-interacting surface of BiP compromised the physical and functional interaction
with Sec63p, an Hsp40 required for ER translocation. In contrast, interaction with Jem1p, an …