Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D

被引：71

作者：

Moyne, AL

Cleveland, TE

Tuzun, S

机构：

[1] Auburn Univ, Dept Entomol & Plant Pathol, Auburn, AL 36849 USA

[2] USDA ARS, So Reg Res Ctr, New Orleans, LA 70179 USA

来源：

FEMS MICROBIOLOGY LETTERS | 2004年 / 234卷 / 01期

关键词：

Bacillus subtilis; non-ribosomal peptide synthetase; iturin; antifungal lipopeptide; gene inactivation;

D O I：

10.1016/j.femsle.2004.03.011

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Bacillus subtilis AU195 produces bacillomycin D, a cyclic lipopeptide that is an inhibitor of the aflatoxin producing fungus Aspergillus flacus. 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. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：43 / 49

页数：7

共 27 条

[1] Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis [J].