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Mol Microbiol. 1992 Jul;6(13):1769-76.

Clarification of the structural and functional features of the osmoregulated kdp operon of Escherichia coli.

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Laboratory of Microbiology, School of Agriculture, Nagoya University, Japan.


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.

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