ArticleThe Journal of biological chemistry2014
A sensory complex consisting of an ATP-binding cassette transporter and a two-component regulatory system controls bacitracin resistance in Bacillus subtilis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 80 citations in OpenAlex.
- Article
- From Host-Derived Pressures to the Environmental Anti-Antimicrobial Peptides Resistome: Mechanisms, Reservoirs and Implications for Therapeutic Peptide Design.Marine drugs · 2026Review
- A conserved residue in the histidine kinase BceS tunes bacitracin stress responses in Bacillus subtilis.Access microbiology · 2026Article
- The unique histidine kinase, AtcS, regulates motility and pathogenicity of the periodontal pathobiont,Infection and immunity · 2025Article
- The extracellular domain ofFrontiers in microbiology · 2025Article
- Guarding the walls: the multifaceted roles of Bce modules in cell envelope stress sensing and antimicrobial resistance.Journal of bacteriology · 2024Review
- Perception and protection: The role of Bce-modules in antimicrobial peptide resistance.Biochimica et biophysica acta. Biomembranes · 2024Review
- TheJournal of bacteriology · 2024Article
- Cross-regulation of Aps-promoters in Lacticaseibacillus paracasei by the PsdR response regulator in response to lantibiotics.Scientific reports · 2024Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Architecture of a complete Bce-type antimicrobial peptide resistance module.Nature communications · 2023Article
- Microbial synthesis of bacitracin: Recent progress, challenges, and prospects.Synthetic and systems biotechnology · 2023Review
- Antimicrobial Resistance: Two-Component Regulatory Systems and Multidrug Efflux Pumps.Antibiotics (Basel, Switzerland) · 2023Review
- Conformational snapshots of the bacitracin sensing and resistance transporter BceAB.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification of a two-component regulatory system involved in antimicrobial peptide resistance in Streptococcus pneumoniae.PLoS pathogens · 2022Article
- A Comparative Analysis ofInternational journal of molecular sciences · 2022Article
- New insights into the resistance mechanism for the BceAB-type transporter SaNsrFP.Scientific reports · 2022Article
- Proteomic analysis of the regulatory networks of ClpX in a model cyanobacteriumFrontiers in plant science · 2022Article
- Lactococcus lactis Resistance to Aureocin A53- and Enterocin L50-Like Bacteriocins and Membrane-Targeting Peptide Antibiotics Relies on the YsaCB-KinG-LlrG Four-Component System.Antimicrobial agents and chemotherapy · 2021Article
- A single system detects and protects the beneficial oral bacterium Streptococcus sp. A12 from a spectrum of antimicrobial peptides.Molecular microbiology · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance against antimicrobial peptides in many Firmicutes bacteria is mediated by detoxification systems that are composed of a two-component regulatory system (TCS) and an ATP-binding cassette (ABC) transporter. The histidine kinases of these systems depend entirely on the transporter for sensing of antimicrobial peptides, suggesting a novel mode of signal transduction where the transporter constitutes the actual sensor. The aim of this study was to investigate the molecular mechanisms of this unusual signaling pathway in more detail, using the bacitracin resistance system BceRS-BceAB of Bacillus subtilis as an example. To analyze the proposed communication between TCS and the ABC transporter, we characterized their interactions by bacterial two-hybrid analyses and could show that the permease BceB and the histidine kinase BceS interact directly. In vitro pulldown assays confirmed this interaction, which was found to be independent of bacitracin. Because it was unknown whether BceAB-type transporters could detect their substrate peptides directly or instead recognized the peptide-target complex in the cell envelope, we next analyzed substrate binding by the transport permease, BceB. Direct and specific binding of bacitracin by BceB was demonstrated by surface plasmon resonance spectroscopy. Finally, in vitro signal transduction assays indicated that complex formation with the transporter influenced the autophosphorylation activity of the histidine kinase. Taken together, our findings clearly show the existence of a sensory complex composed of TCS and ABC transporters and provide the first functional insights into the mechanisms of stimulus perception, signal transduction, and antimicrobial resistance employed by Bce-like detoxification systems.
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