The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- R Heermann
- K Altendorf
- K Jung
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000187206300054&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1074/jbc.M303801200
- eISSN
- 1083-351X
- Externe Identifier
- Clarivate Analytics Document Solution ID: 752ZM
- PubMed Identifier: 14534307
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 51
- Zeitschrift
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Paginierung
- 51277 - 51284
- Datum der Veröffentlichung
- 2003
- Status
- Published
- Titel
- The N-terminal input domain of the sensor kinase KdpD of <i>Escherichia coli</i> stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site
- Sub types
- Article
- Ausgabe der Zeitschrift
- 278
Data source: Web of Science (Lite)
- Other metadata sources:
-
- Autoren
- Ralf Heermann
- Karlheinz Altendorf
- Kirsten Jung
- DOI
- 10.1074/jbc.m303801200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 51
- Zeitschrift
- Journal of Biological Chemistry
- Sprache
- en
- Paginierung
- 51277 - 51284
- Datum der Veröffentlichung
- 2003
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1074/jbc.m303801200
- Datum der Datenerfassung
- 2022
- Titel
- The N-terminal Input Domain of the Sensor Kinase KdpD of Escherichia coli Stabilizes the Interaction between the Cognate Response Regulator KdpE and the Corresponding DNA-binding Site
- Ausgabe der Zeitschrift
- 278
Data source: Crossref
- Abstract
- The sensor kinase/response regulator system KdpD/KdpE of Escherichia coli regulates expression of the kdpFABC operon, which encodes the high affinity K+ transport system KdpFABC. The membrane-bound sensor kinase KdpD consists of an N-terminal input domain (comprising a large cytoplasmic domain and four transmembrane domains) and a cytoplasmic C-terminal transmitter domain. Here we show that the cytoplasmic N-terminal domain of KdpD (KdpD/1-395) alone supports semi-constitutive kdpFABC expression, which becomes dependent on the extracellular K+ concentration under K+-limiting growth conditions. However, it should be noted that the non-phosphorylatable derivative KdpD/H673Q or the absence of KdpD abolishes kdpFABC expression completely. KdpD/1-395 mediated kdpFABC expression requires the corresponding response regulator KdpE with an intact phosphorylation site. Experiments with an Escherichia coli mutant unable to synthesize acetyl phosphate as well as transposon mutagenesis suggest that KdpE is phosphorylated in vivo by low molecular weight phosphodonors in the absence of the full-length sensor kinase. Various biochemical approaches provide first evidence that kdpFABC expression mediated by KdpD/1-395 is due to a stabilizing effect of this domain on the binding of KdpE approximately P to its corresponding DNA-binding site. Such a stabilizing effect of a sensor kinase domain on the DNA-protein interaction of the cognate response regulator has never been observed before for any other sensor kinase. It describes a new mechanism in bacterial two-component signal transduction.
- Addresses
- Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, D-49069 Osnabrück, Germany.
- Autoren
- Ralf Heermann
- Karlheinz Altendorf
- Kirsten Jung
- DOI
- 10.1074/jbc.m303801200
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Identifier: 14534307
- Open access
- false
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 51
- Zeitschrift
- The Journal of biological chemistry
- Schlüsselwörter
- Potassium
- Protein Kinases
- Bacterial Proteins
- Escherichia coli Proteins
- Cation Transport Proteins
- Trans-Activators
- DNA
- Transcription, Genetic
- Binding Sites
- Amino Acid Sequence
- Protein Structure, Tertiary
- Protein Binding
- Phosphorylation
- Adenosine Triphosphatases
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2003
- Paginierung
- 51277 - 51284
- Datum der Veröffentlichung
- 2003
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2003
- Titel
- The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 278
Data source: Europe PubMed Central
- Abstract
- The sensor kinase/response regulator system KdpD/KdpE of Escherichia coli regulates expression of the kdpFABC operon, which encodes the high affinity K+ transport system KdpFABC. The membrane-bound sensor kinase KdpD consists of an N-terminal input domain (comprising a large cytoplasmic domain and four transmembrane domains) and a cytoplasmic C-terminal transmitter domain. Here we show that the cytoplasmic N-terminal domain of KdpD (KdpD/1-395) alone supports semi-constitutive kdpFABC expression, which becomes dependent on the extracellular K+ concentration under K+-limiting growth conditions. However, it should be noted that the non-phosphorylatable derivative KdpD/H673Q or the absence of KdpD abolishes kdpFABC expression completely. KdpD/1-395 mediated kdpFABC expression requires the corresponding response regulator KdpE with an intact phosphorylation site. Experiments with an Escherichia coli mutant unable to synthesize acetyl phosphate as well as transposon mutagenesis suggest that KdpE is phosphorylated in vivo by low molecular weight phosphodonors in the absence of the full-length sensor kinase. Various biochemical approaches provide first evidence that kdpFABC expression mediated by KdpD/1-395 is due to a stabilizing effect of this domain on the binding of KdpE approximately P to its corresponding DNA-binding site. Such a stabilizing effect of a sensor kinase domain on the DNA-protein interaction of the cognate response regulator has never been observed before for any other sensor kinase. It describes a new mechanism in bacterial two-component signal transduction.
- Autoren
- Ralf Heermann
- Karlheinz Altendorf
- Kirsten Jung
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/14534307
- DOI
- 10.1074/jbc.M303801200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 51
- Zeitschrift
- J Biol Chem
- Schlüsselwörter
- Adenosine Triphosphatases
- Amino Acid Sequence
- Bacterial Proteins
- Binding Sites
- Cation Transport Proteins
- DNA
- Escherichia coli Proteins
- Phosphorylation
- Potassium
- Protein Binding
- Protein Kinases
- Protein Structure, Tertiary
- Trans-Activators
- Transcription, Genetic
- Sprache
- eng
- Country
- United States
- Paginierung
- 51277 - 51284
- PII
- S0021-9258(20)75386-X
- Datum der Veröffentlichung
- 2003
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2004
- Titel
- The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 278
Data source: PubMed
- Beziehungen:
- Property of