PMID:19589130
| Citation |
Heermann, R, Lippert, ML and Jung, K (2009) Domain swapping reveals that the N-terminal domain of the sensor kinase KdpD in Escherichia coli is important for signaling. BMC Microbiol. 9:133 |
|---|---|
| Abstract |
The KdpD/KdpE two-component system of Escherichia coli regulates expression of the kdpFABC operon encoding the high affinity K+ transport system KdpFABC. The input domain of KdpD comprises a domain that belongs to the family of universal stress proteins (Usp). It has been previously demonstrated that UspC binds to this domain, resulting in KdpD/KdpE scaffolding under salt stress. However the mechanistic significance of this domain for signaling remains unclear. Here, we employed a "domain swapping" approach to replace the KdpD-Usp domain with four homologous domains or with the six soluble Usp proteins of E. coli. |
| Links |
PubMed PMC2714519 Online version:10.1186/1471-2180-9-133 |
| Keywords |
Amino Acid Sequence; Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Potassium/metabolism; Protein Interaction Domains and Motifs; Protein Kinases/genetics; Protein Kinases/metabolism; Protein Structure, Tertiary; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment; Signal Transduction; Sodium Chloride/metabolism; Stress, Physiological |
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