PMID:12535080
| Citation |
Heermann, R, Fohrmann, A, Altendorf, K and Jung, K (2003) The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation. Mol. Microbiol. 47:839-48 |
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| Abstract |
The sensor kinase/response regulator system KdpD/KdpE of Escherichia coli regulates the expression of the kdpFABC operon, which encodes the high affinity K+ transport system KdpFABC. The membrane-bound sensor kinase KdpD consists of four transmembrane domains, a large cytoplasmic N-terminal domain and a cytoplasmic C-terminal transmitter domain. To elucidate the role of the four transmembrane domains, various deletions were introduced in kdpD and the activities of the resulting truncated derivatives of KdpD were determined. A KdpD protein lacking all four transmembrane domains was able to sense low K+ concentrations, whereas at higher K+ concentrations kdpFABC expression was constitutive. These and further results with various truncated KdpD proteins lacking distinct parts of the transmembrane domains or derivatives in which a linker peptide or two transmembrane domains of PutP, the Na+/proline transporter of Escherichia coli, replaced the missing part indicated that the transmembrane domains are not essential for sensing of K+ limitation, but may be important for the correct positioning of the large N- and C-terminal cytoplasmic domains to each other. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Cytoplasm; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Genes, Bacterial; Mutagenesis, Site-Directed; Mutation; Phosphoric Monoester Hydrolases/metabolism; Phosphorylation; Potassium/metabolism; Protein Kinases/chemistry; Protein Kinases/genetics; Protein Kinases/metabolism; Signal Transduction |
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