Mutagenesis of nisin’s leader peptide proline strongly modulates export of precursor nisin

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• 作者：Annechien Plat ; Anneke Kuipers ; Joe Crabb ; Rick Rink…
• 关键词：Lactococcus lactis ; Lanthionine ; Lanthipeptide ; Leader peptide ; Nisin ; Transporter
• 刊名：Antonie van Leeuwenhoek
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：110
• 期：3
• 页码：321-330
• 全文大小：
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Microbiology; Medical Microbiology; Plant Sciences; Soil Science & Conservation;
• 出版者：Springer International Publishing
• ISSN：1572-9699
• 卷排序：110

文摘

The lantibiotic nisin is produced by Lactococcus lactis as a precursor peptide comprising a 23 amino acid leader peptide and a 34 amino acid post-translationally modifiable core peptide. We previously demonstrated that the conserved FNLD part of the leader is essential for intracellular enzyme-catalyzed introduction of lanthionines in the core peptide and also for transporter-mediated export, whereas other positions are subject to large mutational freedom. We here demonstrate that, in the absence of the extracellular leader peptidase, NisP, export of precursor nisin via the modification and transporter enzymes, NisBTC, is strongly affected by multiple substitutions of the leader residue at position -2, but not by substitution of positions in the vicinity of this site. Export levels of precursor nisin increased by more than 70% for position -2 mutants Asp, Thr, Ser, Trp, Lys, Val and decreased more than 70% for Cys, His, Met. In a strain with leader peptidase, the Pro-2Lys and Pro-2Asp precursor nisins were less efficiently cleaved by NisP than wild type precursor nisin. Taken together, the wild type precursor nisin with a proline at position -2 allows balanced export and cleavage efficiencies by precursor nisin’s transporter and leader peptidase.