Dynamics of an Interactive Network Composed of a Bacterial Two-Component System, a Transporter and K+ as Mediator
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Ralf Heermann
- Katja Zigann
- Stefan Gayer
- Maria Rodriguez-Fernandez
- Julio R Banga
- Andreas Kremling
- Kirsten Jung
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000332396200069&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1371/journal.pone.0089671
- Externe Identifier
- Clarivate Analytics Document Solution ID: AC3DW
- PubMed Identifier: 24586952
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLOS ONE
- Artikelnummer
- ARTN e89671
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Titel
- Dynamics of an Interactive Network Composed of a Bacterial Two-Component System, a Transporter and K<SUP>+</SUP> as Mediator
- Sub types
- Article
- Ausgabe der Zeitschrift
- 9
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Ralf Heermann
- Katja Zigann
- Stefan Gayer
- Maria Rodriguez-Fernandez
- Julio R Banga
- Andreas Kremling
- Kirsten Jung
- DOI
- 10.1371/journal.pone.0089671
- Editoren
- Hendrik W van Veen
- eISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLoS ONE
- Sprache
- en
- Online publication date
- 2014
- Paginierung
- e89671 - e89671
- Status
- Published online
- Herausgeber
- Public Library of Science (PLoS)
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pone.0089671
- Datum der Datenerfassung
- 2022
- Titel
- Dynamics of an Interactive Network Composed of a Bacterial Two-Component System, a Transporter and K+ as Mediator
- Ausgabe der Zeitschrift
- 9
Datenquelle: Crossref
- Abstract
- KdpD and KdpE form a histidine kinase/response regulator system that senses K(+) limitation and induces the kdpFABC operon, which encodes a high-affinity K(+) uptake complex. To define the primary stimulus perceived by KdpD we focused in this study on the dynamics of the Kdp response. Escherichia coli cells were subjected to severe K(+) limitation, and all relevant parameters of the Kdp response, i.e., levels of kdpFABC transcripts and KdpFABC proteins, as well as extra- and intracellular K(+) concentrations, were quantitatively analysed over time (0 to 180 min). Unexpectedly, induction of kdpFABC was found to follow a non-monotonic time-course. To interpret this unusual behaviour, a mathematical model that adequately captures the dynamics of the Kdp system was established and used for simulations. We found a strong correlation between KdpD/KdpE activation and the intracellular K(+) concentration, which is influenced by the uptake of K(+) via the KdpFABC complex. Based on these results a model is proposed in which KdpD/KdpE phosphorylation is inversely correlated with the intracellular K(+) concentration. To corroborate this hypothesis an isogenic mutant that produces a defective KdpFABC complex, and the trans-complemented mutant that expresses the KtrAB high-affinity K(+) uptake system of Vibrio alginolyticus were quantitatively analysed. Experimental data and simulations for the mutants consistently support the tight correlation between KdpD/KdpE activation and the intracellular K(+) concentration. This study presents a striking example of the non-intuitive dynamics of a functional unit comprising signalling proteins and a transporter with K(+) as mediator.
- Addresses
- Center for Integrated Protein Science Munich (CiPSM) at the Department Biology I, Microbiology, Ludwig-Maximilians-Universität München, Martinsried, Germany.
- Autoren
- Ralf Heermann
- Katja Zigann
- Stefan Gayer
- Maria Rodriguez-Fernandez
- Julio R Banga
- Andreas Kremling
- Kirsten Jung
- DOI
- 10.1371/journal.pone.0089671
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Identifier: 24586952
- PubMed Central ID: PMC3938482
- Open access
- true
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PloS one
- Schlüsselwörter
- Escherichia coli
- Potassium
- Membrane Transport Proteins
- Gene Expression Regulation, Bacterial
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2014
- Open access status
- Open Access
- Paginierung
- e89671
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2014
- Titel
- Dynamics of an interactive network composed of a bacterial two-component system, a transporter and K+ as mediator.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 9
Files
https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089671&type=printable https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586952/pdf/?tool=EBI https://europepmc.org/articles/PMC3938482?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- KdpD and KdpE form a histidine kinase/response regulator system that senses K(+) limitation and induces the kdpFABC operon, which encodes a high-affinity K(+) uptake complex. To define the primary stimulus perceived by KdpD we focused in this study on the dynamics of the Kdp response. Escherichia coli cells were subjected to severe K(+) limitation, and all relevant parameters of the Kdp response, i.e., levels of kdpFABC transcripts and KdpFABC proteins, as well as extra- and intracellular K(+) concentrations, were quantitatively analysed over time (0 to 180 min). Unexpectedly, induction of kdpFABC was found to follow a non-monotonic time-course. To interpret this unusual behaviour, a mathematical model that adequately captures the dynamics of the Kdp system was established and used for simulations. We found a strong correlation between KdpD/KdpE activation and the intracellular K(+) concentration, which is influenced by the uptake of K(+) via the KdpFABC complex. Based on these results a model is proposed in which KdpD/KdpE phosphorylation is inversely correlated with the intracellular K(+) concentration. To corroborate this hypothesis an isogenic mutant that produces a defective KdpFABC complex, and the trans-complemented mutant that expresses the KtrAB high-affinity K(+) uptake system of Vibrio alginolyticus were quantitatively analysed. Experimental data and simulations for the mutants consistently support the tight correlation between KdpD/KdpE activation and the intracellular K(+) concentration. This study presents a striking example of the non-intuitive dynamics of a functional unit comprising signalling proteins and a transporter with K(+) as mediator.
- Date of acceptance
- 2014
- Autoren
- Ralf Heermann
- Katja Zigann
- Stefan Gayer
- Maria Rodriguez-Fernandez
- Julio R Banga
- Andreas Kremling
- Kirsten Jung
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/24586952
- DOI
- 10.1371/journal.pone.0089671
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Central ID: PMC3938482
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLoS One
- Schlüsselwörter
- Escherichia coli
- Gene Expression Regulation, Bacterial
- Membrane Transport Proteins
- Potassium
- Sprache
- eng
- Country
- United States
- Paginierung
- e89671
- PII
- PONE-D-13-48653
- Datum der Veröffentlichung
- 2014
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2014
- Titel
- Dynamics of an interactive network composed of a bacterial two-component system, a transporter and K+ as mediator.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 9
Datenquelle: PubMed
- Beziehungen:
- Eigentum von