Abstract:
:The heat shock protein (Hsp)70 family of molecular chaperones interacts with unfolded proteins through a C-terminal substrate-binding domain (SBD) that is controlled by nucleotide binding to the N-terminal domain. The ATPase cycle is regulated by cochaperones, including DnaJ proteins that accelerate ATP hydrolysis to stabilize the Hsp70-substrate complex. We found that R197 in hamster BiP, which resides at the surface of the nucleotide-binding domain, is critical for both association with endoplasmic reticulum DnaJ proteins and interaction with the SBD. Decreasing the positive charge at this residue enhanced basal ATPase activity, destabilized interaction with the SBD, and reduced substrate release both in vitro and in vivo. Mutation of three glutamic acids in the SBD mimicked many of these effects. Our data provide insights into communications between the two domains and suggest a mechanism by which DnaJ proteins increase ATP hydrolysis.
journal_name
Proc Natl Acad Sci U S Aauthors
Awad W,Estrada I,Shen Y,Hendershot LMdoi
10.1073/pnas.0702132105subject
Has Abstractpub_date
2008-01-29 00:00:00pages
1164-9issue
4eissn
0027-8424issn
1091-6490pii
0702132105journal_volume
105pub_type
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