The DnaK homologue of the marine Vibrio sp. strain S14 binds to the unprocessed form of a carbon starvation-specific periplasmic protein

The Escherichia coli DnaK homoiogue in Vibrio sp. strain S14 was shown to possess chaperone function for translocation during carbon starvation. This was demonstrated by using the method of co‐immunoprecipitation. DnaK co‐precipitated with the carbon starvation‐specific periplasmic space protein Csp5 three hours after the onset of carbon starvation. Pulse‐chasing of the protein with radiolabelled methlonine followed by the addition of an excess of unlabelled methionine demonstrated that the Csp5 protein was translocated across the inner membrane. Only the cytoplasmic unprocessed precursor form of Csp5 co‐precipitated with DnaK. The non‐covalent binding between the two proteins was found to be ATP‐dependent, as the addition of ATP released the interaction between DnaK and the precursor form of Csp5, as was shown both on silver‐stained SDS‐poly‐acrylamide gels and by Western blot analysis. We suggest that DnaK maintains the carbon starvatlon‐Inducible protein Csp5 in a translocation‐competent form In the cytoplasm. Copyright © 1994, Wiley Blackwell. All rights reserve