Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D
- PMID: 15109718
- DOI: 10.1016/j.femsle.2004.03.011
Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D
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.
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