The bdbDC operon of bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development
2002
Meima, Rob | Eschevins, Caroline | Fillinger, Sabine, Helma | Bolhuis, Albert | Hamoen, Leendert W. | Dorenbos, Ronald | Quax, Wim J. | van Dijl, Jan Maarten | Provvedi, Roberta | Chen, Ines | Dubnau, David | Bron, Sierd | University of Groningen [Groningen] | DSM Food Specialties | Microbiologie et Génétique Moléculaire (MGM) ; Institut National de la Recherche Agronomique (INRA)-Institut National Agronomique Paris-Grignon (INA P-G)-Centre National de la Recherche Scientifique (CNRS) | University of Warwick [Coventry] | Department of Pharmaceutical Biology ; University of Groningen [Groningen] | Public Health Research Institute [Newark] (PHRI) | Università degli Studi di Siena = University of Siena (UNISI)
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Mostrar más [+] Menos [-]Inglés. The development of genetic competence in the Gram-positive eubacterium Bacillus subtilis is a complex postexponential process. Here we describe a new bicistronic operon, bdbDC, required for competence development, which was identified by the B. subtilis Systematic Gene Function Analysis program. Inactivation of either the bdbC or bdbD genes of this operon results in the loss of transformability without affecting recombination or the synthesis of ComK, the competence transcription factor. BdbC and BdbD are orthologs of enzymes known to be involved in extracytoplasmic disulfide bond formation. Consistent with this, BdbC and BdbD are needed for the secretion of theEscherichia coli disulfide bond-containing alkaline phosphatase, PhoA, by B. subtilis. Similarly, the amount of the disulfide bond-containing competence protein ComGC is severely reduced in bdbC or bdbD mutants. In contrast, the amounts of the competence proteins ComGA and ComEA remain unaffected by bdbDC mutations. Taken together, these observations imply that in the absence of either BdbC or BdbD, ComGC is unstable and that BdbC and BdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery.
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