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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