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Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source.
Masepohl, B; Führer, F; Klipp, W.
Afiliación
  • Masepohl B; Ruhr-Universität Bochum, Fakultät für Biologie, Lehrstuhl für Biologie der Mikroorganismen, D-44780 Bochum, Germany.
FEMS Microbiol Lett ; 205(1): 105-11, 2001 Nov 27.
Article en En | MEDLINE | ID: mdl-11728723
ABSTRACT
Rhodobacter capsulatus was shown to grow efficiently with taurine as sole source of sulfur. We identified a gene region exhibiting similarity to the Escherichia coli tauABC genes coding for a taurine-specific ABC transporter. The R. capsulatus tauABC genes were flanked by two putative operons (orf459-484-590 and cysE-srpI-nifS2) both reading in opposite direction relative to tauABC. Orf459 shows strong similarity to taurinepyruvate aminotransferase (Tpa) from Bilophila wadsworthia catalyzing the initial transamination during anaerobic taurine degradation, and Orf590 exhibits clear similarity to sulfoacetaldehyde sulfo-lyase from Desulfonispora thiosulfatigenes probably catalyzing the step following the taurinepyruvate aminotransferase (Tpa) reaction, whereas nifS2 might code for a putative cysteine desulfurase. Expression of R. capsulatus tauABC and nifS2 was inhibited by sulfate, suggesting that tauABC and nifS2 might belong to the same regulon. In contrast, transcription of orf459 was not inhibited by sulfate but was induced by taurine. A tauAB deletion mutant showed significantly reduced growth compared to the wild-type with taurine as sole sulfur source in the presence of serine as a nitrogen source, whereas normal growth was observed in the presence of taurine and ammonium. Deletion of orf459-484-590 completely abolished growth with taurine/serine. Single mutations in any of the three genes resulted in the same phenotype, indicating that all three genes of this putative operon are essential for taurine sulfur utilization in the presence of serine. A model for anaerobic taurine sulfur assimilation in R. capsulatus is discussed.
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Bases de datos: MEDLINE Asunto principal: Azufre / Taurina / Proteínas Bacterianas / Rhodobacter capsulatus / Transportadoras de Casetes de Unión a ATP Idioma: En Revista: FEMS Microbiol Lett Año: 2001 Tipo del documento: Article País de afiliación: Alemania
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Bases de datos: MEDLINE Asunto principal: Azufre / Taurina / Proteínas Bacterianas / Rhodobacter capsulatus / Transportadoras de Casetes de Unión a ATP Idioma: En Revista: FEMS Microbiol Lett Año: 2001 Tipo del documento: Article País de afiliación: Alemania