Mutations in pts cause catabolite-resistant sporulation and altered regulation of spoOH in Bacillus subtilis

D. Frisby, Peter Zuber

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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 spo0H gene, encoding σ(H), as evidenced by immunoblot analysis with anti-σ(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.

Original languageEnglish (US)
Pages (from-to)2587-2595
Number of pages9
JournalJournal of Bacteriology
Volume176
Issue number9
StatePublished - 1994
Externally publishedYes

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Bacillus subtilis
Phenotype
Glucose
Mutation
Glutamine
Sequence Deletion
Operon
Mental Competency
Immune Sera
Plasmids
Gene Expression
phosphoenolpyruvate-glucose phosphotransferase
Genes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Mutations in pts cause catabolite-resistant sporulation and altered regulation of spoOH in Bacillus subtilis. / Frisby, D.; Zuber, Peter.

In: Journal of Bacteriology, Vol. 176, No. 9, 1994, p. 2587-2595.

Research output: Contribution to journalArticle

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abstract = "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 spo0H gene, encoding σ(H), as evidenced by immunoblot analysis with anti-σ(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.",
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N2 - 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 spo0H gene, encoding σ(H), as evidenced by immunoblot analysis with anti-σ(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.

AB - 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 spo0H gene, encoding σ(H), as evidenced by immunoblot analysis with anti-σ(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.

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