HEAT-SHOCK PROTEINS CAN SUBSTITUTE FOR SECB FUNCTION DURING PROTEIN EXPORT IN ESCHERICHIA-COLI

In this study we have shown that (i) induction of the heat-shock response can substitute for SecB function in Escherichia coli, (ii) SecB itself is not a heat-shock protein and (iii) a basal level of heat-shock proteins is required for cells to grow in the absence of a functional SecB protein. Overproduction of DnaK, or GroEL/ES, which were candidates for the heat-shock proteins that could substitute for SecB function, did not rescue the export defect caused when SecB was limiting or absent. In an attempt to identify the heat-shock protein(s) which could substitute for SecB function, unlinked suppressors of secB were isolated and characterized. Interestingly, most of the suppressors mapped to the rpoH locus. Since rpoH encodes sigma-32, the heat-shock transcription factor, it is likely that these suppressors affect the synthesis levels of heat-shock proteins that can substitute for SecB function. The remaining suppressors did not map to any known heat-shock or export genes. Collectively, our data suggest that these suppressors may represent unidentified heat-shock proteins or export factors that act in a manner similar to SecB in facilitating the export process in E. coli.