UNSPECIFIED. (2002) Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168. JOURNAL OF BIOLOGICAL CHEMISTRY, 277 (19). pp. 16682-16688. ISSN 0021-9258

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Abstract

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	JOURNAL OF BIOLOGICAL CHEMISTRY
Publisher:	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN:	0021-9258
Date:	10 May 2002
Volume:	277
Number:	19
Number of Pages:	7
Page Range:	pp. 16682-16688
Identification Number:	10.1074/jbc.M201158200
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/10956

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