Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome.

ABSTRACT: In Escherichia coli, the molecular chaperones DnaK and DnaJ cooperate to assist the folding of newly synthesized or unfolded polypeptides. DnaK and DnaJ bind to hydrophobic motifs in these proteins and they also bind to each other. Together, this system is thought to be sufficiently versatile to act on the entire proteome, which creates interesting challenges in understanding the interactions between DnaK, DnaJ and their thousands of potential substrates. To address this question, we computationally predicted the number and frequency of DnaK- and DnaJ-binding motifs in the E. coli proteome, guided by free energy-based binding consensus motifs. This analysis revealed that nearly every protein is predicted to contain multiple DnaK- and DnaJ-binding sites, with the DnaJ sites occurring approx

SUBMITTER: Srinivasan SR 

PROVIDER: S-EPMC3462289 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature