Structural and Functional Characterization of Gene Clusters Directing Nonribosomal Synthesis of Bioactive Cyclic Lipopeptides in Bacillus amyloliquefaciens Strain FZB42
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| Published in | Journal of Bacteriology Vol. 186; no. 4; pp. 1084 - 1096 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
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Washington, DC
American Society for Microbiology
01.02.2004
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The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We sampled sequenced the genome of FZB42 and identified 2,947 genes with >50% identity on the amino acid level to the corresponding genes of Bacillus subtilis 168. Six large gene clusters encoding nonribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) occupied 7.5% of the whole genome. Two of the PKS and one of the NRPS encoding gene clusters were unique insertions in the FZB42 genome and are not present in B. subtilis 168. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis revealed expression of the antibiotic lipopeptide products surfactin, fengycin, and bacillomycin D. The fengycin ( fen ) and the surfactin ( srf ) operons were organized and located as in B. subtilis 168. A large 37.2-kb antibiotic DNA island containing the bmy gene cluster was attributed to the biosynthesis of bacillomycin D. The bmy island was found inserted close to the fen operon. The responsibility of the bmy , fen , and srf gene clusters for the production of the corresponding secondary metabolites was demonstrated by cassette mutagenesis, which led to the loss of the ability to produce these peptides. Although these single mutants still largely retained their ability to control fungal spread, a double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner. The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We sampled sequenced the genome of FZB42 and identified 2,947 genes with >50% identity on the amino acid level to the corresponding genes of Bacillus subtilis 168. Six large gene clusters encoding nonribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) occupied 7.5% of the whole genome. Two of the PKS and one of the NRPS encoding gene clusters were unique insertions in the FZB42 genome and are not present in B. subtilis 168. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis revealed expression of the antibiotic lipopeptide products surfactin, fengycin, and bacillomycin D. The fengycin (fen) and the surfactin (srf) operons were organized and located as in B. subtilis 168. A large 37.2-kb antibiotic DNA island containing the bmy gene cluster was attributed to the biosynthesis of bacillomycin D. The bmy island was found inserted close to the fen operon. The responsibility of the bmy, fen, and srf gene clusters for the production of the corresponding secondary metabolites was demonstrated by cassette mutagenesis, which led to the loss of the ability to produce these peptides. Although these single mutants still largely retained their ability to control fungal spread, a double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner. The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We sampled sequenced the genome of FZB42 and identified 2,947 genes with >50% identity on the amino acid level to the corresponding genes of Bacillus subtilis 168. Six large gene clusters encoding nonribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) occupied 7.5% of the whole genome. Two of the PKS and one of the NRPS encoding gene clusters were unique insertions in the FZB42 genome and are not present in B. subtilis 168. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis revealed expression of the antibiotic lipopeptide products surfactin, fengycin, and bacillomycin D. The fengycin (fen) and the surfactin (srf) operons were organized and located as in B. subtilis 168. A large 37.2-kb antibiotic DNA island containing the bmy gene cluster was attributed to the biosynthesis of bacillomycin D. The bmy island was found inserted close to the fen operon. The responsibility of the bmy, fen, and srf gene clusters for the production of the corresponding secondary metabolites was demonstrated by cassette mutagenesis, which led to the loss of the ability to produce these peptides. Although these single mutants still largely retained their ability to control fungal spread, a double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner.The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We sampled sequenced the genome of FZB42 and identified 2,947 genes with >50% identity on the amino acid level to the corresponding genes of Bacillus subtilis 168. Six large gene clusters encoding nonribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) occupied 7.5% of the whole genome. Two of the PKS and one of the NRPS encoding gene clusters were unique insertions in the FZB42 genome and are not present in B. subtilis 168. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis revealed expression of the antibiotic lipopeptide products surfactin, fengycin, and bacillomycin D. The fengycin (fen) and the surfactin (srf) operons were organized and located as in B. subtilis 168. A large 37.2-kb antibiotic DNA island containing the bmy gene cluster was attributed to the biosynthesis of bacillomycin D. The bmy island was found inserted close to the fen operon. The responsibility of the bmy, fen, and srf gene clusters for the production of the corresponding secondary metabolites was demonstrated by cassette mutagenesis, which led to the loss of the ability to produce these peptides. Although these single mutants still largely retained their ability to control fungal spread, a double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner. The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We sampled sequenced the genome of FZB42 and identified 2,947 genes with >50% identity on the amino acid level to the corresponding genes of Bacillus subtilis 168. Six large gene clusters encoding nonribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) occupied 7.5% of the whole genome. Two of the PKS and one of the NRPS encoding gene clusters were unique insertions in the FZB42 genome and are not present in B. subtilis 168. Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis revealed expression of the antibiotic lipopeptide products surfactin, fengycin, and bacillomycin D. The fengycin (fen) and the surfactin (srf) operons were organized and located as in B. subtilis 168. A large 37.2-kb antibiotic DNA island containing the bmy gene cluster was attributed to the biosynthesis of bacillomycin D. The bmy island was found inserted close to the fen operon. The responsibility of the bmy, fen, and srf gene clusters for the production of the corresponding secondary metabolites was demonstrated by cassette mutagenesis, which led to the loss of the ability to produce these peptides. Although these single mutants still largely retained their ability to control fungal spread, a double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner. [PUBLICATION ABSTRACT] |
| Author | Joachim Vater Rainer Borriss Heiko Liesegang Gabriele Hitzeroth Peter Franke Xiao-Hua Chen Anke Henne Alexandra Koumoutsi |
| AuthorAffiliation | Institut für Biologie, Humboldt Universität Berlin, 1 Goettingen Genomics Laboratory, 2 Institut für Chemie, Technische Universität Berlin, 3 Institut für Biochemie der Freien Universität, Berlin, Germany 4 |
| AuthorAffiliation_xml | – name: Institut für Biologie, Humboldt Universität Berlin, 1 Goettingen Genomics Laboratory, 2 Institut für Chemie, Technische Universität Berlin, 3 Institut für Biochemie der Freien Universität, Berlin, Germany 4 |
| Author_xml | – sequence: 1 givenname: Alexandra surname: Koumoutsi fullname: Koumoutsi, Alexandra organization: Institut für Biologie, Humboldt Universität Berlin – sequence: 2 givenname: Xiao-Hua surname: Chen fullname: Chen, Xiao-Hua organization: Institut für Biologie, Humboldt Universität Berlin – sequence: 3 givenname: Anke surname: Henne fullname: Henne, Anke organization: Goettingen Genomics Laboratory – sequence: 4 givenname: Heiko surname: Liesegang fullname: Liesegang, Heiko organization: Goettingen Genomics Laboratory – sequence: 5 givenname: Gabriele surname: Hitzeroth fullname: Hitzeroth, Gabriele organization: Institut für Chemie, Technische Universität Berlin – sequence: 6 givenname: Peter surname: Franke fullname: Franke, Peter organization: Institut für Biochemie der Freien Universität, Berlin, Germany – sequence: 7 givenname: Joachim surname: Vater fullname: Vater, Joachim organization: Institut für Chemie, Technische Universität Berlin – sequence: 8 givenname: Rainer surname: Borriss fullname: Borriss, Rainer organization: Institut für Biologie, Humboldt Universität Berlin |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15860485$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/14762003$$D View this record in MEDLINE/PubMed |
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Mendeley... The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We... The environmental strain Bacillus amyloliquefaciens FZB42 promotes plant growth and suppresses plant pathogenic organisms present in the rhizosphere. We... |
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| SubjectTerms | Amino acids bacillomycin D Bacillus - genetics Bacillus amyloliquefaciens Bacteria Bacteriology Base Sequence Biological and medical sciences Biosynthesis bmy gene Chemical synthesis Chromosomes, Bacterial fen gene fengycin Fens Fundamental and applied biological sciences. Psychology Genes Genome, Bacterial Ionization Lipoproteins - biosynthesis Lipoproteins - chemistry Mass spectrometry Meeting Presentations Metabolites Microbiology Miscellaneous Molecular Sequence Data Multienzyme Complexes - genetics Multigene Family nonribosomal peptide synthase Nucleic Acid Hybridization Operon Peptide Synthases - genetics Peptides Peptides, Cyclic - biosynthesis Peptides, Cyclic - chemistry Plant growth polyketide synthase Rhizosphere Secondary metabolites srf gene surfactin |
| Title | Structural and Functional Characterization of Gene Clusters Directing Nonribosomal Synthesis of Bioactive Cyclic Lipopeptides in Bacillus amyloliquefaciens Strain FZB42 |
| URI | http://jb.asm.org/content/186/4/1084.abstract https://www.ncbi.nlm.nih.gov/pubmed/14762003 https://www.proquest.com/docview/227108626 https://www.proquest.com/docview/19255536 https://www.proquest.com/docview/80141573 https://pubmed.ncbi.nlm.nih.gov/PMC344220 |
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