Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis
Nisin-producing Lactococcus lactisstrains show a high degree of resistance to the action of nisin, which is based upon expression of the self-protection (immunity) genesnisI, nisF, nisE, andnisG. Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive...
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description | Nisin-producing Lactococcus lactisstrains show a high degree of resistance to the action of nisin, which is based upon expression of the self-protection (immunity) genesnisI, nisF, nisE, andnisG. Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive Bacillus subtilishost strain under the control of an inducible promoter. For the recipient strain, the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes. But either the lipoprotein NisI or the ABC transporter-homologous system NisFEG, respectively, were also able to protect the Bacillus host cells. The acquired immunity was specific to nisin and provided no tolerance to subtilin, a closely related lantibiotic. Quantitative in vivo peptide release assays demonstrated that NisFEG diminished the quantity of cell-associated nisin, providing evidence that one role of NisFEG is to transport nisin from the membrane into the extracellular space. NisI solubilized from B. subtilis membrane vesicles and recombinant hexahistidine-tagged NisI from Escherichia coliinteracted specifically with nisin and not with subtilin. This suggests a function of NisI as a nisin-intercepting protein. |
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Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive Bacillus subtilishost strain under the control of an inducible promoter. For the recipient strain, the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes. But either the lipoprotein NisI or the ABC transporter-homologous system NisFEG, respectively, were also able to protect the Bacillus host cells. The acquired immunity was specific to nisin and provided no tolerance to subtilin, a closely related lantibiotic. Quantitative in vivo peptide release assays demonstrated that NisFEG diminished the quantity of cell-associated nisin, providing evidence that one role of NisFEG is to transport nisin from the membrane into the extracellular space. NisI solubilized from B. subtilis membrane vesicles and recombinant hexahistidine-tagged NisI from Escherichia coliinteracted specifically with nisin and not with subtilin. 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Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive Bacillus subtilishost strain under the control of an inducible promoter. For the recipient strain, the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes. But either the lipoprotein NisI or the ABC transporter-homologous system NisFEG, respectively, were also able to protect the Bacillus host cells. The acquired immunity was specific to nisin and provided no tolerance to subtilin, a closely related lantibiotic. Quantitative in vivo peptide release assays demonstrated that NisFEG diminished the quantity of cell-associated nisin, providing evidence that one role of NisFEG is to transport nisin from the membrane into the extracellular space. NisI solubilized from B. subtilis membrane vesicles and recombinant hexahistidine-tagged NisI from Escherichia coliinteracted specifically with nisin and not with subtilin. 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Different combinations of nisin immunity genes were integrated into the chromosome of a nisin-sensitive Bacillus subtilishost strain under the control of an inducible promoter. For the recipient strain, the highest level of acquired nisin tolerance was achieved after coordinated expression of all four nisin immunity genes. But either the lipoprotein NisI or the ABC transporter-homologous system NisFEG, respectively, were also able to protect the Bacillus host cells. The acquired immunity was specific to nisin and provided no tolerance to subtilin, a closely related lantibiotic. Quantitative in vivo peptide release assays demonstrated that NisFEG diminished the quantity of cell-associated nisin, providing evidence that one role of NisFEG is to transport nisin from the membrane into the extracellular space. NisI solubilized from B. subtilis membrane vesicles and recombinant hexahistidine-tagged NisI from Escherichia coliinteracted specifically with nisin and not with subtilin. 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subjects | Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - immunology ATP-Binding Cassette Transporters - metabolism Bacillus subtilis - drug effects Bacillus subtilis - genetics Bacillus subtilis - immunology Bacillus subtilis - metabolism Bacterial Proteins - genetics Bacterial Proteins - immunology Bacterial Proteins - metabolism Biological Transport - physiology Cell Fractionation Drug Resistance, Bacterial Gene Expression Regulation, Bacterial Genes, Bacterial Lactococcus lactis - drug effects Lactococcus lactis - genetics Lactococcus lactis - immunology Lipoproteins - genetics Lipoproteins - immunology Lipoproteins - metabolism Membrane Proteins Multigene Family Nisin - genetics Nisin - metabolism Nisin - pharmacology Operon Promoter Regions, Genetic Subtilisin - genetics Subtilisin - metabolism Subtilisin - pharmacology Transcription, Genetic |
title | Function of Lactococcus lactis Nisin Immunity Genes nisI and nisFEG after Coordinated Expression in the Surrogate Host Bacillus subtilis |
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