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J Biol Chem, Vol. 274, Issue 35, 24531-24538, August 27, 1999
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From the The in vivo formation of disulfide
bonds, which is critical for the stability and/or activity of many
proteins, is catalyzed by thiol-disulfide oxidoreductases. In the
present studies, we show that the Gram-positive eubacterium
Bacillus subtilis contains three genes, denoted
bdbA, bdbB, and bdbC, for
thiol-disulfide oxidoreductases. Escherichia coli alkaline
phosphatase, containing two disulfide bonds, was unstable when secreted
by B. subtilis cells lacking BdbB or BdbC, and notably, the
expression levels of bdbB and bdbC appeared to
set a limit for the secretion of active alkaline phosphatase. Cells
lacking BdbC also showed decreased stability of cell-associated forms
of E. coli TEM- Department of Genetics,
-lactamase, containing one disulfide
bond. In contrast, BdbA was not required for the stability of alkaline
phosphatase or -lactamase. Because BdbB and BdbC are typical
membrane proteins, our findings suggest that they promote protein
folding at the membrane-cell wall interface. Interestingly,
pre--lactamase processing to its mature form was stimulated in cells
lacking BdbC, suggesting that the unfolded form of this precursor is a
preferred substrate for signal peptidase. Surprisingly, cells lacking
BdbC did not develop competence for DNA uptake, indicating the
involvement of disulfide bond-containing proteins in this process.
Unlike E. coli and yeast, none of the thiol-disulfide
oxidoreductases of B. subtilis was required for growth in
the presence of reducing agents. In conclusion, our observations
indicate that BdbB and BdbC have a general role in disulfide bond
formation, whereas BdbA may be dedicated to a specific process.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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