Non-canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Markus Moerk-Moerkenstein
- Ralf Heermann
- Yvonne Goepel
- Kirsten Jung
- Boris Goerke
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000411284800004&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1111/mmi.13751
- eISSN
- 1365-2958
- Externe Identifier
- Clarivate Analytics Document Solution ID: FH6KI
- PubMed Identifier: 28714556
- ISSN
- 0950-382X
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- MOLECULAR MICROBIOLOGY
- Paginierung
- 54 - 73
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Titel
- Non-canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain
- Sub types
- Article
- Ausgabe der Zeitschrift
- 106
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:title>Summary</jats:title><jats:p>The two‐component system KdpD/KdpE governs K<jats:sup>+</jats:sup> homeostasis by controlling synthesis of the high affinity K<jats:sup>+</jats:sup> transporter KdpFABC. When sensing low environmental K<jats:sup>+</jats:sup> concentrations, the dimeric kinase KdpD autophosphorylates <jats:italic>in trans</jats:italic> and transfers the phosphoryl‐group to the response regulator KdpE, which subsequently activates <jats:italic>kdpFABC</jats:italic> transcription. In <jats:italic>Escherichia coli</jats:italic>, KdpD can also be activated by interaction with the non‐phosphorylated form of the accessory protein PtsN. PtsN stimulates KdpD kinase activity thereby increasing phospho‐KdpE levels. Here, we analyzed the interplay between KdpD/KdpE and PtsN. PtsN binds specifically to the catalytic DHp domain of KdpD, which is also contacted by KdpE. Accordingly, PtsN and KdpE compete for binding, providing a paradox. Low levels of non‐phosphorylated PtsN stimulate, whereas high amounts reduce <jats:italic>kdpFABC</jats:italic> expression by blocking access of KdpE to KdpD. Ligand fishing experiments provided insight as they revealed ternary complex formation of PtsN/KdpD<jats:sub>2</jats:sub>/KdpE <jats:italic>in vivo</jats:italic> demonstrating that PtsN and KdpE bind different protomers in the KdpD dimer. PtsN may bind one protomer to stimulate phosphorylation of the second KdpD protomer, which then phosphorylates bound KdpE. Phosphorylation of PtsN prevents its incorporation in ternary complexes. Interaction with the conserved DHp domain enables PtsN to regulate additional kinases such as PhoR.</jats:p>
- Autoren
- Markus Mörk‐Mörkenstein
- Ralf Heermann
- Yvonne Göpel
- Kirsten Jung
- Boris Görke
- DOI
- 10.1111/mmi.13751
- eISSN
- 1365-2958
- ISSN
- 0950-382X
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Molecular Microbiology
- Sprache
- en
- Online publication date
- 2017
- Paginierung
- 54 - 73
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Herausgeber
- Wiley
- Herausgeber URL
- http://dx.doi.org/10.1111/mmi.13751
- Datum der Datenerfassung
- 2023
- Titel
- Non‐canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain
- Ausgabe der Zeitschrift
- 106
Datenquelle: Crossref
- Abstract
- The two-component system KdpD/KdpE governs K<sup>+</sup> homeostasis by controlling synthesis of the high affinity K<sup>+</sup> transporter KdpFABC. When sensing low environmental K<sup>+</sup> concentrations, the dimeric kinase KdpD autophosphorylates in trans and transfers the phosphoryl-group to the response regulator KdpE, which subsequently activates kdpFABC transcription. In Escherichia coli, KdpD can also be activated by interaction with the non-phosphorylated form of the accessory protein PtsN. PtsN stimulates KdpD kinase activity thereby increasing phospho-KdpE levels. Here, we analyzed the interplay between KdpD/KdpE and PtsN. PtsN binds specifically to the catalytic DHp domain of KdpD, which is also contacted by KdpE. Accordingly, PtsN and KdpE compete for binding, providing a paradox. Low levels of non-phosphorylated PtsN stimulate, whereas high amounts reduce kdpFABC expression by blocking access of KdpE to KdpD. Ligand fishing experiments provided insight as they revealed ternary complex formation of PtsN/KdpD<sub>2</sub> /KdpE in vivo demonstrating that PtsN and KdpE bind different protomers in the KdpD dimer. PtsN may bind one protomer to stimulate phosphorylation of the second KdpD protomer, which then phosphorylates bound KdpE. Phosphorylation of PtsN prevents its incorporation in ternary complexes. Interaction with the conserved DHp domain enables PtsN to regulate additional kinases such as PhoR.
- Addresses
- Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna Biocenter (VBC), Vienna, Austria.
- Autoren
- Markus Mörk-Mörkenstein
- Ralf Heermann
- Yvonne Göpel
- Kirsten Jung
- Boris Görke
- DOI
- 10.1111/mmi.13751
- eISSN
- 1365-2958
- Externe Identifier
- PubMed Identifier: 28714556
- Funding acknowledgements
- Deutsche Forschungsgemeinschaft: GO1355/7‐1
- Open access
- false
- ISSN
- 0950-382X
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Molecular microbiology
- Schlüsselwörter
- Escherichia coli
- Potassium
- Phosphoenolpyruvate Sugar Phosphotransferase System
- Protein Kinases
- Escherichia coli Proteins
- Membrane Transport Proteins
- Trans-Activators
- Protein Subunits
- Signal Transduction
- Gene Expression Regulation, Bacterial
- Binding Sites
- Phosphorylation
- Histidine Kinase
- Protein Domains
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2017
- Paginierung
- 54 - 73
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Datum der Datenerfassung
- 2017
- Titel
- Non-canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 106
Datenquelle: Europe PubMed Central
- Abstract
- The two-component system KdpD/KdpE governs K+ homeostasis by controlling synthesis of the high affinity K+ transporter KdpFABC. When sensing low environmental K+ concentrations, the dimeric kinase KdpD autophosphorylates in trans and transfers the phosphoryl-group to the response regulator KdpE, which subsequently activates kdpFABC transcription. In Escherichia coli, KdpD can also be activated by interaction with the non-phosphorylated form of the accessory protein PtsN. PtsN stimulates KdpD kinase activity thereby increasing phospho-KdpE levels. Here, we analyzed the interplay between KdpD/KdpE and PtsN. PtsN binds specifically to the catalytic DHp domain of KdpD, which is also contacted by KdpE. Accordingly, PtsN and KdpE compete for binding, providing a paradox. Low levels of non-phosphorylated PtsN stimulate, whereas high amounts reduce kdpFABC expression by blocking access of KdpE to KdpD. Ligand fishing experiments provided insight as they revealed ternary complex formation of PtsN/KdpD2 /KdpE in vivo demonstrating that PtsN and KdpE bind different protomers in the KdpD dimer. PtsN may bind one protomer to stimulate phosphorylation of the second KdpD protomer, which then phosphorylates bound KdpE. Phosphorylation of PtsN prevents its incorporation in ternary complexes. Interaction with the conserved DHp domain enables PtsN to regulate additional kinases such as PhoR.
- Date of acceptance
- 2017
- Autoren
- Markus Mörk-Mörkenstein
- Ralf Heermann
- Yvonne Göpel
- Kirsten Jung
- Boris Görke
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/28714556
- DOI
- 10.1111/mmi.13751
- eISSN
- 1365-2958
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- Mol Microbiol
- Schlüsselwörter
- Binding Sites
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Histidine Kinase
- Membrane Transport Proteins
- Phosphoenolpyruvate Sugar Phosphotransferase System
- Phosphorylation
- Potassium
- Protein Domains
- Protein Kinases
- Protein Subunits
- Signal Transduction
- Trans-Activators
- Sprache
- eng
- Country
- England
- Paginierung
- 54 - 73
- Datum der Veröffentlichung
- 2017
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2017
- Titel
- Non-canonical activation of histidine kinase KdpD by phosphotransferase protein PtsN through interaction with the transmitter domain.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 106
Datenquelle: PubMed
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