Towards an understanding of the molecular mechanisms of stimulus perception and signal transduction by the KdpD/KdpE system of Escherichia coli

Autor(en): Jung, K
Altendorf, K 
Stichwörter: Biotechnology & Applied Microbiology; INTERMOLECULAR COMPLEMENTATION; KDPABC OPERON; Microbiology; OPERON EXPRESSION; OSMOSENSOR; OSMOTIC-STRESS; PHOSPHATASE-ACTIVITY; RAPID INACTIVATION; RECONSTITUTION; SENSOR KINASE KDPD; TURGOR SENSOR
Erscheinungsdatum: 2002
Herausgeber: KARGER
Journal: JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
Volumen: 4
Ausgabe: 3, SI
Startseite: 223
Seitenende: 228
Zusammenfassung: 
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.
ISSN: 14641801

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