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1Department of Plant Pathology, One Shields Avenue, University of California, Davis, CA 95616, USA.
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Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D
Article first published online: 9 JAN 2006
DOI: 10.1111/j.1574-6968.2004.tb09511.x
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How to Cite
Moyne, A.-L., Cleveland, T. E. and Tuzun, S. (2004), Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D. FEMS Microbiology Letters, 234: 43–49. doi: 10.1111/j.1574-6968.2004.tb09511.x
Publication History
- Issue published online: 9 JAN 2006
- Article first published online: 9 JAN 2006
- Received 12 January 2004, Accepted 4 March 2004
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Keywords:
- Bacillus subtilis;
- Non-ribosomal peptide synthetase;
- Iturin;
- Antifungal lipopeptide;
- Gene inactivation
Abstract
Bacillus subtilis AU195 produces bacillomycin D, a cyclic lipopeptide that is an inhibitor of the aflatoxin producing fungus Aspergillus flavus. Sequence analysis of the bacillomycin D operon revealed four ORFs with the structural organization of the peptide synthetases. Disruption of ORF 2, which links the amino acid moiety to the b-amino fatty acid, resulted in the loss of antifungal activity. By comparing the sequence of bacillomycin D, iturin A and mycosubtilin operons, our results showed that intergenic module replacement have occurred between B. subtilis lipopeptide synthetases including the iturin family and the plipastatin and fengycin family.