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Skin Pharmacol Physiol 2007,20(3):162–166.CrossRefPubMed Authors’ contributions AW, HB, and AK participated in the design and coordination of the study, supervised the study, and analyzed the data. RS performed most www.selleckchem.com/products/LY294002.html of the laboratory work with the assistance of ChM and HB. ChS carried out the statistical analysis. AW wrote the ever manuscript. All authors read and approved the final version

of the manuscript.”
“Background K+ plays an important role in turgor maintenance in bacteria [1]. KdpFABC is a high affinity K+ uptake system that serves as an emergency system to scavenge K+ when other transporters cannot sustain the cellular requirement for K+. The corresponding kdpFABC operon is under control of the two-component system KdpD/KdpE, which induces kdpFABC expression under K+ limiting conditions or under osmotic stress imposed by a salt [2, 3]. Upon stimulus perception, KdpD undergoes autophosphorylation and subsequently, the phosphoryl group is transferred to the cytoplasmic response regulator KdpE [4]. Phosphorylated KdpE exhibits increased affinity for a 23-base pair sequence upstream of the canonical -35 and -10 regions of the kdpFABC promoter and triggers kdpFABC expression [5]. The enzymatic activities of purified KdpD and KdpE were determined in vitro [4]. All data known thus far indicate that KdpD does not sense a single specific parameter, but integrates the information of intracellular parameters imposed by K+ limitation or salt stress.