Clarification of the structural and functional features of the osmoregulated kdp operon of Escherichia coli.
Expression of the Escherichia coli kdpABC operon, which is responsible for a high-affinity potassium-uptake system, is regulated in response to a change in the medium osmolarity. In this study, we clarified the structure and function of the kdpABC promoter including its regulatory sequence at the molecular level. The canonical -35 and -10 regions determined for the promoter were not fully functional, i.e. in addition to them, a cis-acting sequence located upstream of the -35 region was essential for full activation of the promoter. This upstream sequence was demonstrated to be the target site for the trans-acting activator, KdpE.
Sugiura
A
A
Laboratory of Microbiology, School of Agriculture, Nagoya University, Japan.
Nakashima
K
K
Tanaka
K
K
Mizuno
T
T
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D001692:Biological Transport; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D009876:Operon; D009994:Osmolar Concentration; D011188:Potassium / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D012045:Regulatory Sequences, Nucleic Acid; D015534:Trans-Activators / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D015534:Trans-Activators; C075615:kdpE protein, E coli; D011188:Potassium