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The relative amounts of the OmpF and OmpC proteins in the outer membrane of Escherichia coli K-12 are affected differentially by high concentrations of substances like sucrose in culture media in such a manner that a decrease in the amount of the OmpF protein appears to be compensated for by a reciprocal increase in the OmpC protein. When an ompF mutation was introduced, OmpC synthesis became almost independent of sucrose and occurred at the fully induced level even in the absence of sucrose. On the other hand, introduction of an ompC mutation did not affect the sucrose-dependent profile of OmpF synthesis. The effect of the ompF mutation was also examined with the ompC-lac fusion strain, in which expression of beta-galactosidase is under the control of the ompC promoter. The expression of beta-galactosidase coded for by the ompC-lac fusion in the ompF+ and ompF- strains was essentially the same as that of the OmpC protein, being sucrose dependent in the ompF+ strain and sucrose-independent in the ompF mutant. From these results we conclude that sucrose in the medium primarily regulates ompF gene expression, which in turn regulates ompC gene expression at the transcriptional level. This sequential regulatory mechanism is discussed in relation to the function of the ompB locus.

Regulation of outer membrane porin protein synthesis in Escherichia coli K-12: ompF regulates the expression of ompC