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A sigma E dependent operon subject to catabolite repression during sporulation in Bacillus subtilis.
Bryan, E M; Beall, B W; Moran, C P.
Afiliação
  • Bryan EM; Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
J Bacteriol ; 178(16): 4778-86, 1996 Aug.
Article em En | MEDLINE | ID: mdl-8759838
ABSTRACT
To identify genes expressed at intermediate stages of Bacillus subtilis sporulation, we screened for sigma E-dependent promoters. One promoter that we found drives expression of an operon consisting of at least five open reading frames (ORFs). The predicted products of the first three ORFs are very homologous to enzymes involved in fatty acid metabolism, including acetyl coenzyme A (acetyl-CoA) acetyltransferase (thiolase), 3-hydroxybutyryl-CoA dehydrogenase, and acyl-CoA dehydrogenase, respectively. We showed that the fourth ORF encoded a third isozyme of citrate synthase in B. subtilis. Genetic evidence and primer extension results showed that transcription of this operon is directed by the mother cell compartment-specific sigma factor, sigma E, and so the operon was named mmg (for mother cell metabolic genes). Furthermore, we found that a sequence (mmgO) with homology to a catabolite-responsive element mediates glucose repression of mmg promoter activity during sporulation and that this repression was lost in a ccpA mutant.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Óperon / Fator sigma / Bacillus subtilis / Fatores de Transcrição / Citrato (si)-Sintase Tipo de estudo: Prognostic_studies Idioma: En Revista: J Bacteriol Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Óperon / Fator sigma / Bacillus subtilis / Fatores de Transcrição / Citrato (si)-Sintase Tipo de estudo: Prognostic_studies Idioma: En Revista: J Bacteriol Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Estados Unidos