ArticleApplied and environmental microbiology2006
Sec-mediated transport of posttranslationally dehydrated peptides in Lactococcus lactis.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.
- Advancements in the Application of Ribosomally Synthesized and Post-Translationally Modified Peptides (RiPPs).Biomolecules · 2024Pooled it
- Construction of Synthetic Probiotic Bacteria for In Situ Delivery of Anti-SARS-CoV-2 Nanobodies.Probiotics and antimicrobial proteins · 2026Article
- An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens.Nature communications · 2025Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- 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
- Microbial production of small peptide: pathway engineering and synthetic biology.Microbial biotechnology · 2021Review
- Article
- Article
- Biosynthesis of lanthionine-constrained agonists of G protein-coupled receptors.Biochemical Society transactions · 2020Review
- Probiotics at War Against Viruses: What Is Missing From the Picture?Frontiers in microbiology · 2020Review
- Development and Application of Yeast and Phage Display of Diverse Lanthipeptides.ACS central science · 2018Article
- Phage display and selection of lanthipeptides on the carboxy-terminus of the gene-3 minor coat protein.Nature communications · 2017Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- In vitro activity of the nisin dehydratase NisB.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Bacterial display and screening of posttranslationally thioether-stabilized peptides.Applied and environmental microbiology · 2011Article
- Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis.The Journal of biological chemistry · 2011Article
- Bioengineering of a Nisin A-producing Lactococcus lactis to create isogenic strains producing the natural variants Nisin F, Q and Z.Microbial biotechnology · 2011Article
- Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage.Applied and environmental microbiology · 2011Article
- Directionality and coordination of dehydration and ring formation during biosynthesis of the lantibiotic nisin.The Journal of biological chemistry · 2009Article
- Translocation of a thioether-bridged azurin peptide fragment via the sec pathway in Lactococcus lactis.Applied and environmental microbiology · 2009Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin is a lanthionine-containing antimicrobial peptide produced by Lactococcus lactis. Its (methyl)lanthionines are introduced by two posttranslational enzymatic steps involving the dehydratase NisB, which dehydrates serine and threonine residues, and the cyclase NisC, which couples these dehydrated residues to cysteines, yielding thioether-bridged amino acids called lanthionines. The prenisin is subsequently exported by the ABC transporter NisT and extracellularly processed by the peptidase NisP. L. lactis expressing the nisBTC genes can modify and secrete a wide range of nonlantibiotic peptides. Here we demonstrate that in the absence of NisT and NisC, the Sec pathway of L. lactis can be exploited for the secretion of dehydrated variants of therapeutic peptides. Furthermore, posttranslational modifications by NisB and NisC still occur even when the nisin leader is preceded by a Sec signal peptide or a Tat signal peptide 27 or 44 amino acids long, respectively. However, transport of fully modified prenisin via the Sec pathway is impaired. The extent of NisB-mediated dehydration could be improved by raising the intracellular concentration NisB or by modulating the export efficiency through altering the signal sequence. These data demonstrate that besides the traditional lantibiotic transporter NisT, the Sec pathway with an established broad substrate range can be utilized for the improved export of lantibiotic enzyme-modified (poly)peptides.
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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.