ArticleThe Journal of biological chemistry2015
The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- The DdD protein confers intracellular and extracellular immunity to the leaderless bacteriocin enterocin DD14.PNAS nexus · 2026Article
- A comparative framework of natural nisin variants: linking genetic basis to future bioengineering applications.Microbial cell factories · 2026Review
- Turbidimetric bioassays: A solution to antimicrobial activity detection in asymptomatic bacteriuria isolates against uropathogenic Escherichia coli.MicrobiologyOpen · 2024Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Advances in Characterizing the Transport Systems of and Resistance to EntDD14, A Leaderless Two-Peptide Bacteriocin with Potent Inhibitory Activity.International journal of molecular sciences · 2023Article
- 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
- Current Knowledge of the Mode of Action and Immunity Mechanisms of LAB-Bacteriocins.Microorganisms · 2021Review
- Article
- Therapeutic Application of Lantibiotics and Other Lanthipeptides: Old and New Findings.Applied and environmental microbiology · 2021Review
- Gene-Trait Matching and Prevalence of Nisin Tolerance Systems inFrontiers in bioengineering and biotechnology · 2021Article
- Solution structure and RNA-binding of a minimal ProQ-homolog fromRNA (New York, N.Y.) · 2020Article
- Article
- NisI Maturation and Its Influence on Nisin Resistance in Lactococcus lactis.Applied and environmental microbiology · 2020Article
- A Leaderless Two-Peptide Bacteriocin, Enterocin DD14, Is Involved in Its Own Self-Immunity: Evidence and Insights.Frontiers in bioengineering and biotechnology · 2020Article
- Kunkecin A, a New Nisin Variant Bacteriocin Produced by the Fructophilic Lactic Acid Bacterium,Frontiers in microbiology · 2020Article
- Lipoproteins in Gram-Positive Bacteria: Abundance, Function, Fitness.Frontiers in microbiology · 2020Review
- LanI-Mediated Lantibiotic Immunity in Bacillus subtilis: Functional Analysis.Applied and environmental microbiology · 2019Article
- Systematic characterization of position one variants within the lantibiotic nisin.Scientific reports · 2019Article
- Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIPStructure (London, England : 1993) · 2018Article
- Crystal Structure of NisI in a Lipid-Free Form, the Nisin Immunity Protein, from Lactococcus lactis.Antimicrobial agents and chemotherapy · 2018Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many Gram-positive bacteria produce lantibiotics, genetically encoded and posttranslationally modified peptide antibiotics, which inhibit the growth of other Gram-positive bacteria. To protect themselves against their own lantibiotics these bacteria express a variety of immunity proteins including the LanI lipoproteins. The structural and mechanistic basis for LanI-mediated lantibiotic immunity is not yet understood. Lactococcus lactis produces the lantibiotic nisin, which is widely used as a food preservative. Its LanI protein NisI provides immunity against nisin but not against structurally very similar lantibiotics from other species such as subtilin from Bacillus subtilis. To understand the structural basis for LanI-mediated immunity and their specificity we investigated the structure of NisI. We found that NisI is a two-domain protein. Surprisingly, each of the two NisI domains has the same structure as the LanI protein from B. subtilis, SpaI, despite the lack of significant sequence homology. The two NisI domains and SpaI differ strongly in their surface properties and function. Additionally, SpaI-mediated lantibiotic immunity depends on the presence of a basic unstructured N-terminal region that tethers SpaI to the membrane. Such a region is absent from NisI. Instead, the N-terminal domain of NisI interacts with membranes but not with nisin. In contrast, the C-terminal domain specifically binds nisin and modulates the membrane affinity of the N-terminal domain. Thus, our results reveal an unexpected structural relationship between NisI and SpaI and shed light on the structural basis for LanI mediated lantibiotic immunity.
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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.