Abstract
The phage-shock-protein (psp) operon helps to ensure survival of Escherichia coli in late stationary phase at alkaline pH, and protects the cell against dissipation of its proton-motive force against challenge. It is strongly induced by filamentous phage pIV and its bacterial homologues, and by mutant porins that don't localize properly, as well as by a number of other stresses. Transcription of the operon is dependent on sigma54 and a constitutively active, autogenously controlled activator. psp-operon expression is controlled by one negatively and several positively acting regulators, none of which is a DNA-binding protein. The major product of the operon, PspA, may also serve as a negative regulator of an unusual porin, OmpG.
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