ArticleFEBS open bio2013
Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC.
Article in FEBS open bio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Design and Biosynthesis of Ornithine 8-Containing Semaglutide Variants with a Click Chemistry-Modifiable Position 26.ACS synthetic biology · 2025Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- 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
- Article
- Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.Applied and environmental microbiology · 2021Review
- Article
- A Cell-Free Platform Based on Nisin Biosynthesis for Discovering Novel Lanthipeptides and Guiding their Overproduction In Vivo.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Impact of the nisin modification machinery on the transport kinetics of NisT.Scientific reports · 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
- RiPP antibiotics: biosynthesis and engineering potential.Current opinion in microbiology · 2018Review
- Investigation of Substrate Recognition and Biosynthesis in Class IV Lanthipeptide Systems.Journal of the American Chemical Society · 2018Article
- Specificity and Application of the Lantibiotic Protease NisP.Frontiers in microbiology · 2018Article
- Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products.ACS central science · 2017Article
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- Stoichiometry and structure of a lantibiotic maturation complex.Scientific reports · 2017Article
- New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.Cell chemical biology · 2016Review
- Identification of essential amino acid residues in the nisin dehydratase NisB.Frontiers in microbiology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin is the most prominent and applied bacteriocin that serves as a model for class I lantibiotics. The nisin leader peptide importantly determines interactions between precursor nisin and its modification enzymes NisB and NisC that mature nisin posttranslationally. NisB dehydrates serines and threonines, while NisC catalyzes the subsequent coupling of the formed dehydroamino acids to form lanthionines. Currently, little is known about how the nisin leader interacts with NisB and even less is known about its interactions with NisC. To investigate the nisin leader peptide requirements for functional interaction with the modification enzymes NisB and NisC, we systematically replaced six regions, of 2-4 amino acids each, with all-alanine regions. By performing NisB and NisC co-purification studies with these mutant leader peptides, we demonstrate that the nisin leader regions STKD(-22-19), FNLD(-18-15) and PR(-2-1) importantly contribute to the interactions of precursor nisin with both NisB and NisC, whereas the nisin leader region LVSV(-14-11) additionally contributes to the interaction of precursor nisin with NisC.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.