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Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42

Lantibiotics are small peptide antibiotics that contain the characteristic thioether amino acids lanthionine and methyllanthionine. As ribosomally synthesized peptides, lantibiotics possess biosynthetic gene clusters which contain the structural gene (lanA) as well as the other genes which are invol...

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Autores principales: Herzner, Anna Maria, Dischinger, Jasmin, Szekat, Christiane, Josten, Michaele, Schmitz, Stephanie, Yakéléba, Anja, Reinartz, Ricarda, Jansen, Andrea, Sahl, Hans-Georg, Piel, Jörn, Bierbaum, Gabriele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3141056/
https://www.ncbi.nlm.nih.gov/pubmed/21811596
http://dx.doi.org/10.1371/journal.pone.0022389
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author Herzner, Anna Maria
Dischinger, Jasmin
Szekat, Christiane
Josten, Michaele
Schmitz, Stephanie
Yakéléba, Anja
Reinartz, Ricarda
Jansen, Andrea
Sahl, Hans-Georg
Piel, Jörn
Bierbaum, Gabriele
author_facet Herzner, Anna Maria
Dischinger, Jasmin
Szekat, Christiane
Josten, Michaele
Schmitz, Stephanie
Yakéléba, Anja
Reinartz, Ricarda
Jansen, Andrea
Sahl, Hans-Georg
Piel, Jörn
Bierbaum, Gabriele
author_sort Herzner, Anna Maria
collection PubMed
description Lantibiotics are small peptide antibiotics that contain the characteristic thioether amino acids lanthionine and methyllanthionine. As ribosomally synthesized peptides, lantibiotics possess biosynthetic gene clusters which contain the structural gene (lanA) as well as the other genes which are involved in lantibiotic modification (lanM, lanB, lanC, lanP), regulation (lanR, lanK), export (lanT(P)) and immunity (lanEFG). The lantibiotic mersacidin is produced by Bacillus sp. HIL Y-85,54728, which is not naturally competent. METHODOLOGY/PRINCIPAL FINDINGS: The aim of these studies was to test if the production of mersacidin could be transferred to a naturally competent Bacillus strain employing genomic DNA of the producer strain. Bacillus amyloliquefaciens FZB42 was chosen for these experiments because it already harbors the mersacidin immunity genes. After transfer of the biosynthetic part of the gene cluster by competence transformation, production of active mersacidin was obtained from a plasmid in trans. Furthermore, comparison of several DNA sequences and biochemical testing of B. amyloliquefaciens FZB42 and B. sp. HIL Y-85,54728 showed that the producer strain of mersacidin is a member of the species B. amyloliquefaciens. CONCLUSIONS/SIGNIFICANCE: The lantibiotic mersacidin can be produced in B. amyloliquefaciens FZB42, which is closely related to the wild type producer strain of mersacidin. The new mersacidin producer strain enables us to use the full potential of the biosynthetic gene cluster for genetic manipulation and downstream modification approaches.
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spelling pubmed-31410562011-08-02 Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42 Herzner, Anna Maria Dischinger, Jasmin Szekat, Christiane Josten, Michaele Schmitz, Stephanie Yakéléba, Anja Reinartz, Ricarda Jansen, Andrea Sahl, Hans-Georg Piel, Jörn Bierbaum, Gabriele PLoS One Research Article Lantibiotics are small peptide antibiotics that contain the characteristic thioether amino acids lanthionine and methyllanthionine. As ribosomally synthesized peptides, lantibiotics possess biosynthetic gene clusters which contain the structural gene (lanA) as well as the other genes which are involved in lantibiotic modification (lanM, lanB, lanC, lanP), regulation (lanR, lanK), export (lanT(P)) and immunity (lanEFG). The lantibiotic mersacidin is produced by Bacillus sp. HIL Y-85,54728, which is not naturally competent. METHODOLOGY/PRINCIPAL FINDINGS: The aim of these studies was to test if the production of mersacidin could be transferred to a naturally competent Bacillus strain employing genomic DNA of the producer strain. Bacillus amyloliquefaciens FZB42 was chosen for these experiments because it already harbors the mersacidin immunity genes. After transfer of the biosynthetic part of the gene cluster by competence transformation, production of active mersacidin was obtained from a plasmid in trans. Furthermore, comparison of several DNA sequences and biochemical testing of B. amyloliquefaciens FZB42 and B. sp. HIL Y-85,54728 showed that the producer strain of mersacidin is a member of the species B. amyloliquefaciens. CONCLUSIONS/SIGNIFICANCE: The lantibiotic mersacidin can be produced in B. amyloliquefaciens FZB42, which is closely related to the wild type producer strain of mersacidin. The new mersacidin producer strain enables us to use the full potential of the biosynthetic gene cluster for genetic manipulation and downstream modification approaches. Public Library of Science 2011-07-21 /pmc/articles/PMC3141056/ /pubmed/21811596 http://dx.doi.org/10.1371/journal.pone.0022389 Text en Herzner et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Herzner, Anna Maria
Dischinger, Jasmin
Szekat, Christiane
Josten, Michaele
Schmitz, Stephanie
Yakéléba, Anja
Reinartz, Ricarda
Jansen, Andrea
Sahl, Hans-Georg
Piel, Jörn
Bierbaum, Gabriele
Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title_full Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title_fullStr Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title_full_unstemmed Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title_short Expression of the Lantibiotic Mersacidin in Bacillus amyloliquefaciens FZB42
title_sort expression of the lantibiotic mersacidin in bacillus amyloliquefaciens fzb42
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3141056/
https://www.ncbi.nlm.nih.gov/pubmed/21811596
http://dx.doi.org/10.1371/journal.pone.0022389
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