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

Mol Microbiol. 1992 Jul;6(13):1769-76. doi: 10.1111/j.1365-2958.1992.tb01349.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Biological Transport
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Molecular Sequence Data
  • Operon*
  • Osmolar Concentration
  • Potassium / metabolism*
  • Promoter Regions, Genetic*
  • Regulatory Sequences, Nucleic Acid
  • Trans-Activators / genetics
  • Trans-Activators / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Trans-Activators
  • kdpE protein, E coli
  • Potassium

Associated data

  • GENBANK/M36066