MUTATIONS IN PTS CAUSE CATABOLITE-RESISTANT SPORULATION AND ALTERED REGULATION OF SPO0H IN BACILLUS-SUBTILIS

A mutation in Bacillus subtilis, ggr-31, that relieves glucose-glutamine-dependent control of a spoVG-lacZ translational fusion was isolated and was subsequently found to confer a pleiotropic phenotype. Mutants cultured in glucose- and glutamine-rich media exhibited a Crs(-) (catabolite-resistant sporulation) phenotype; enhanced expression of the spoOH gene, encoding sigma(H), as evidenced by immunoblot analysis with anti-sigma(H) antiserum; and derepression of srfA, an operon involved in surfactin biosynthesis and competence development. In addition, ggr-31 mutants exhibited a significant increase in generation time when they were cultured in minimal glucose medium. The mutant phenotype was restored to the wild type by Campbell integration of a plasmid containing part of the ptsG (encoding the enzyme II/III glucose permease) gene, indicating that the mutation probably resides within ptsG and adversely affects glucose uptake. A deletion mutation within ptsI exhibited a phenotype similar to that of ggr-31.