Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein.

ABSTRACT: Protein folding is a prominent chaperone function of the Hsp70 system. Refolding of an unfolded protein is efficiently mediated by the Hsc70 system with either type 1 DnaJ protein, DjA1 or DjA2, and a nucleotide exchange factor. A surface plasmon resonance technique was applied to investigate substrate recognition by the Hsc70 system and demonstrated that multiple Hsc70 proteins and a dimer of DjA1 initially bind independently to an unfolded protein. The association rate of the Hsc70 was faster than that of DjA1 under folding-compatible conditions. The Hsc70 binding involved a conformational change, whereas the DjA1 binding was bivalent and substoichiometric. Consistently, we found that the bound (14)C-labeled Hsc70 to the unfolded protein became more resistant to tryptic digestion. The ge

SUBMITTER: Terada K 

PROVIDER: S-EPMC2878007 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature