PMID:11931551

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Citation

Jung, K and Altendorf, K (2002) Towards an understanding of the molecular mechanisms of stimulus perception and signal transduction by the KdpD/KdpE system of Escherichia coli. J. Mol. Microbiol. Biotechnol. 4:223-8

Abstract

The membrane-bound histidine kinase KdpD is a putative turgor sensor that regulates, together with the response regulator KdpE, expression of the kdpFABC operon. This operon encodes the high affinity K+-uptake system KdpFABC of Escherichia coli. Expression of kdpFABC is induced under K+ limiting growth conditions and in response to an osmotic upshift. Various structural features of KdpD and KdpE, which are important for stimulus perception and/or signal transduction were identified and are described here. Furthermore, various studies undertaken to elucidate the nature of the stimulus for KdpD result in a new model for KdpD stimulus perception. According to this, autophosphorylation activity of KdpD is not a result of changes in turgor per se. Instead, various--mainly intracellular parameters--that are related to changes of environmental conditions influence the activities of KdpD.

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Keywords

Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Osmolar Concentration; Protein Kinases/genetics; Protein Kinases/metabolism; Signal Transduction; Trans-Activators/genetics; Trans-Activators/metabolism

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