Effects of pre-protein overexpression on SecB synthesis in Escherichia coli.

Protein translocation through the cytoplasmic membrane of Escherichia coli involves cytosolic chaperones. The export-dedicated chaperone SecB mediates targeting of a subset of pre-proteins. In this report, synthesis of SecB in response to plasmid-mediated overexpression of pre-proteins was studied. Overexpression of SecB-dependent pre-proteins stimulated synthesis of SecB under conditions where the cellular export capacity was saturated or uncomplexed SecB was trapped. On the contrary, overexpression of SecB-independent pre-beta-lactamase reduced the promoter activity of secB. The results suggest that uncomplexed SecB can be sequestered by synthesis of SecB-dependent pre-proteins. Furthermore, these data demonstrate the distinct action of the SecB- and signal recognition particle-dependent protein targeting pathways.

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