A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Sebastian Dintner
- Ralf Heermann
- Chong Fang
- Kirsten Jung
- Susanne Gebhard
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000342852800045&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1074/jbc.M114.596221
- eISSN
- 1083-351X
- Externe Identifier
- Clarivate Analytics Document Solution ID: AQ5MH
- PubMed Identifier: 25118291
- Ausgabe der Veröffentlichung
- 40
- Zeitschrift
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Schlüsselwörter
- ABC Transporter
- Antimicrobial Peptide (AMP)
- Histidine Kinase
- Membrane Protein
- Protein-Protein Interaction
- Bacitracin
- Paginierung
- 27899 - 27910
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Titel
- A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in <i>Bacillus subtilis</i>
- Sub types
- Article
- Ausgabe der Zeitschrift
- 289
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Sebastian Dintner
- Ralf Heermann
- Chong Fang
- Kirsten Jung
- Susanne Gebhard
- DOI
- 10.1074/jbc.m114.596221
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 40
- Zeitschrift
- Journal of Biological Chemistry
- Sprache
- en
- Paginierung
- 27899 - 27910
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1074/jbc.m114.596221
- Datum der Datenerfassung
- 2022
- Titel
- A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis
- Ausgabe der Zeitschrift
- 289
Datenquelle: Crossref
- 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.
- Addresses
- From the Department of Biology I, Microbiology, and.
- Autoren
- Sebastian Dintner
- Ralf Heermann
- Chong Fang
- Kirsten Jung
- Susanne Gebhard
- DOI
- 10.1074/jbc.m114.596221
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Identifier: 25118291
- PubMed Central ID: PMC4183823
- Open access
- false
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 40
- Zeitschrift
- The Journal of biological chemistry
- Schlüsselwörter
- Bacillus subtilis
- Bacitracin
- Protein Kinases
- Bacterial Proteins
- Membrane Transport Proteins
- ATP-Binding Cassette Transporters
- Anti-Bacterial Agents
- Drug Resistance, Bacterial
- Protein Binding
- Histidine Kinase
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2014
- Paginierung
- 27899 - 27910
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2014
- Titel
- A sensory complex consisting of an ATP-binding cassette transporter and a two-component regulatory system controls bacitracin resistance in Bacillus subtilis.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 289
Files
http://www.jbc.org/article/S0021925820484224/pdf https://europepmc.org/articles/PMC4183823?pdf=render
Datenquelle: Europe PubMed Central
- 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.
- Autoren
- Sebastian Dintner
- Ralf Heermann
- Chong Fang
- Kirsten Jung
- Susanne Gebhard
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/25118291
- DOI
- 10.1074/jbc.M114.596221
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Central ID: PMC4183823
- Ausgabe der Veröffentlichung
- 40
- Zeitschrift
- J Biol Chem
- Schlüsselwörter
- ABC Transporter
- Antimicrobial Peptide (AMP)
- Bacitracin
- Histidine Kinase
- Membrane Protein
- Protein-Protein Interaction
- ATP-Binding Cassette Transporters
- Anti-Bacterial Agents
- Bacillus subtilis
- Bacitracin
- Bacterial Proteins
- Drug Resistance, Bacterial
- Histidine Kinase
- Membrane Transport Proteins
- Protein Binding
- Protein Kinases
- Sprache
- eng
- Country
- United States
- Paginierung
- 27899 - 27910
- PII
- S0021-9258(20)48422-4
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2014
- Titel
- A sensory complex consisting of an ATP-binding cassette transporter and a two-component regulatory system controls bacitracin resistance in Bacillus subtilis.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 289
Datenquelle: PubMed
- Beziehungen:
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