ArticleApplied and environmental microbiology2011
Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 96 citations in OpenAlex.
- A comparative framework of natural nisin variants: linking genetic basis to future bioengineering applications.Microbial cell factories · 2026Review
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Bioinformatic mining for RiPP biosynthetic gene clusters in Bacteroidales reveals possible new subfamily architectures and novel natural products.Frontiers in microbiology · 2023Article
- Mutational Studies of the Mersacidin Leader Reveal the Function of Its Unique Two-Step Leader Processing Mechanism.ACS synthetic biology · 2022Article
- Substrate Recognition by the Peptidyl-(ACS chemical biology · 2022Article
- Analysis of Cross-Functionality within LanBTC Synthetase Complexes from Different Bacterial Sources with Respect to Production of Fully Modified Lanthipeptides.Applied and environmental microbiology · 2022Article
- Recombinant production of the lantibiotic nisin using Corynebacterium glutamicum in a two-step process.Microbial cell factories · 2022Article
- Article
- Semisynthetic Macrocyclic Lipo-lanthipeptides Display Antimicrobial Activity Against Bacterial Pathogens.ACS synthetic biology · 2021Article
- Biosynthesis and Heterologous Expression of Cacaoidin, the First Member of the Lanthidin Family of RiPPs.Antibiotics (Basel, Switzerland) · 2021Article
- Biosynthesis of lanthionine-constrained agonists of G protein-coupled receptors.Biochemical Society transactions · 2020Review
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- Insights in the Antimicrobial Potential of the Natural Nisin Variant Nisin H.Frontiers in microbiology · 2020Article
- Kunkecin A, a New Nisin Variant Bacteriocin Produced by the Fructophilic Lactic Acid Bacterium,Frontiers in microbiology · 2020Article
- A Structural View on the Maturation of Lanthipeptides.Frontiers in microbiology · 2020Review
- Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Zn-dependent bifunctional proteases are responsible for leader peptide processing of class III lanthipeptides.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Systematic characterization of position one variants within the lantibiotic nisin.Scientific reports · 2019Article
- Article
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5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin A is a pentacyclic peptide antibiotic produced by Lactococcus lactis. The leader peptide of prenisin keeps nisin inactive and has a role in inducing NisB- and NisC-catalyzed modifications of the propeptide and NisT-mediated export. The highly specific NisP cleaves off the leader peptide from fully modified and exported prenisin. We present here a detailed mutagenesis analysis of the nisin leader peptide. For alternative cleavage, we successfully introduced a putative NisP autocleavage site and sites for thrombin, enterokinase, Glu-C, and factor Xa in the C-terminal part of the leader peptide. Replacing residue F-18 with Trp or Thr strongly reduced production. On the other hand, D-19A, F-18H, F-18M, L-16D, L-16K, and L-16A enhanced production. Substitutions within and outside the FNLD box enhanced or reduced the transport efficiency. None of the above substitutions nor even an internal 6His tag from positions -13 to -8 had any effect on the capacity of the leader peptide to induce NisB and NisC modifications. Therefore, these data demonstrate a large mutational freedom. However, simultaneous replacement of the FNLD amino acids by four alanines strongly reduced export and even led to a complete loss of the capacity to induce modifications. Reducing the leader peptide to MSTKDFNLDLR led to 3- or 4-fold dehydration. Taken together, the FNLD box is crucial for inducing posttranslational modifications.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.