Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.

ABSTRACT: The 90-kDa heat shock protein (Hsp90) is a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent protein remodeling in both eukaryotes and prokaryotes. It functions in conjunction with Hsp70 and the Hsp70 cochaperones, an Hsp40 (J-protein) and a nucleotide exchange factor. In Escherichia coli, the functional collaboration between Hsp90_Ec and Hsp70, DnaK, requires that the two chaperones directly interact. We used molecular docking to model the interaction of Hsp90_Ec and DnaK. The top-ranked docked model predicted that a region in the nucleotide-binding domain (NBD) of DnaK interacted with a region in the middle domain of Hsp90_Ec. We then made substitution mutants in DnaK residues suggested by the model to interact with Hsp90

SUBMITTER: Kravats AN 

PROVIDER: S-EPMC5357148 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature