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J. Biol. Chem., Vol. 277, Issue 19, 16682-16688, May 10, 2002
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From the Thiol-disulfide oxidoreductases are required for
disulfide bond formation in proteins that are exported from the
cytoplasm. Four enzymes of this type, termed BdbA, BdbB, BdbC, and
BdbD, have been identified in the Gram-positive eubacterium
Bacillus subtilis. BdbC and BdbD have been shown to be
critical for the folding of a protein required for DNA uptake during
natural competence. In contrast, no function has been assigned so far
to the BdbA and BdbB proteins. The bdbA and
bdbB genes are located in one operon that also contains the
genes specifying the lantibiotic sublancin 168 and the ATP-binding
cassette transporter SunT. Interestingly sublancin 168 contains
two disulfide bonds. The present studies demonstrate that SunT and
BdbB, but not BdbA, are required for the production of active sublancin
168. In addition, the BdbB paralogue BdbC is at least partly able to
replace BdbB in sublancin 168 production. These observations show the
unprecedented involvement of thiol-disulfide oxidoreductases in the
synthesis of a peptide antibiotic. Notably BdbB cannot complement BdbC
in competence development, showing that these two closely related
thiol-disulfide oxidoreductases have different, but partly overlapping,
substrate specificities.
Thiol-Disulfide Oxidoreductases Are Essential for the Production
of the Lantibiotic Sublancin 168*
,,
**,,, and
Department of Pharmaceutical Biology,
University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, the
Netherlands, the § Institut für Mikrobiologie, J. W. Goethe Universität, Marie-Curie-Str. 9, 60439 Frankfurt am
Main, Germany, ¶ Génétique Microbienne, Institut
National de la Recherche Agronomique-Domaine de Vilvert,
78352 Jouy en Josas cedex, France, and the Department of
Genetics, University of Groningen, Kerklaan 30, PO Box 14, 9750 AA
Haren, the Netherlands
*
Funding for the project, of which this work is a part, was
provided by the Commission of the European Union Projects
BIO4-CT98-0250, QLK3-CT-1999-00413, and QLK3-CT-1999-00917.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.
To whom correspondence should be addressed. Tel.:
31-50-363-3079; Fax: 31-50-363-3000; E-mail:
W.J.Quax@farm.rug.nl.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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