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Originally published In Press as doi:10.1074/jbc.M111380200 on December 13, 2001

J. Biol. Chem., Vol. 277, Issue 9, 6994-7001, March 1, 2002
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The bdbDC Operon of Bacillus subtilis Encodes Thiol-disulfide Oxidoreductases Required for Competence Development*

Rob Meimaabc, Caroline Eschevinsac, Sabine Fillingerde, Albert Bolhuisaf, Leendert W. Hamoena, Ronald Dorenbosg, Wim J. Quaxg, Jan Maarten van Dijlg, Roberta Provvedihi, Ines Chenh, David Dubnauh, and Sierd Bronaj

From the a Groningen Biomolecular Sciences and Biotechnology Institute, Department of Genetics, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, d Laboratoire de Génétique Moléculaire et Cellulaire, INRA INA-PG, Thiverval-Grignon F-78850, France, g Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands, and h Public Health Research Institute, New York, New York 10016

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 the Escherichia 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.

* This work was supported by the CEU projects BIO4-CT95-0278, QLG2-1999-014555, QLK3-CT-1999-00413, and QLK3-CT-1999-00917. The work done in New York was supported by National Institutes of Health Grant GM 43756.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b Present address: DSM Food Specialties, Wateringseweg 1, Postbus 1, 2600 MA Delft, The Netherlands.

c These authors contributed equally to this work.

e Present address: Unité de Phytopharmacie et Médiateurs Chimiques, INRA Versailles-Grignon, Route de St-Cyr, 78026 Versailles cedex, France.

f Present address: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.

i Present address: Laboratorio di Microbiologia Molecolare e Biotecnologia, Sezione di Microbiologia, Dipartimento di Biologia Molecolare, Università di Siena, Policlinico Le Scotte-lotto1, Viale Bracci, 53100, Siena, Italy.

j To whom correspondence should be addressed. Tel.: 31 50 363 2105; Fax: 31 50 363 2348; E-mail: S.Bron@biol.rug.nl.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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