Modulation of KdpD phosphatase implicated in the physiological expression of the Kdp ATPase of Escherichia coli

DC FieldValueLanguage
dc.contributor.authorBrandon, L
dc.contributor.authorDorus, S
dc.contributor.authorEpstein, W
dc.contributor.authorAltendorf, K
dc.contributor.authorJung, K
dc.date.accessioned2021-12-23T16:07:10Z-
dc.date.available2021-12-23T16:07:10Z-
dc.date.issued2000
dc.identifier.issn0950382X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/7736-
dc.description.abstractThe KdpD sensor kinase and the KdpE response regulator control the expression of the kdpFABC operon, encoding the KdpFABC high-affinity K+ transport system of Escherichia coli. Low turgor pressure has been postulated to be the environmental stimulus to express KdpFABC. KdpD has autokinase, phosphotransferase and, like many sensor kinases, response regulator (phospho-KdpE) specific phosphatase activity. To determine which of these activities are altered in response to the environmental stimulus, we isolated and analysed six kdpD mutants that cause constitutive expression of KdpFABC. In three of the mutants, phosphatase activity was undetectable and, in two, phosphatase was reduced. Kinase activity was unaffected in four of the mutants, but elevated in one. In one mutant, a pseudorevertant of a kdpD null mutation, kinase and phosphatase were both reduced to 20% of the wild-type level. These findings suggest that initiation of signal transduction by KdpD is mediated by the inhibition of the phospho-KdpE-specific phosphatase activity of KdpD, leading to an accumulation of phospho-KdpE, which in turn activates the expression of the KdpFABC system. The data also suggest that levels of activity in vitro may differ from what occurs in vivo, because in vitro conditions cannot replicate those in vivo.
dc.description.sponsorshipNIGMS NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [1F32GM14810, GM22323, GM21823] Funding Source: Medline; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [F31GM014810, R01GM021823, R01GM022323] Funding Source: NIH RePORTER
dc.language.isoen
dc.publisherBLACKWELL SCIENCE LTD
dc.relation.ispartofMOLECULAR MICROBIOLOGY
dc.subject2 REGULATORY COMPONENTS
dc.subjectBiochemistry & Molecular Biology
dc.subjectK-12
dc.subjectMicrobiology
dc.subjectOPERON EXPRESSION
dc.subjectPHOSPHORYLATION
dc.subjectPHOSPHOTRANSFER
dc.subjectPROTEIN
dc.subjectSENSOR KINASE KDPD
dc.subjectSIGNAL TRANSDUCTION
dc.subjectSYSTEM
dc.subjectTURGOR SENSOR
dc.titleModulation of KdpD phosphatase implicated in the physiological expression of the Kdp ATPase of Escherichia coli
dc.typejournal article
dc.identifier.doi10.1046/j.1365-2958.2000.02219.x
dc.identifier.isiISI:000166576500014
dc.description.volume38
dc.description.issue5
dc.description.startpage1086
dc.description.endpage1092
dc.publisher.placeP O BOX 88, OSNEY MEAD, OXFORD OX2 0NE, OXON, ENGLAND
dcterms.isPartOf.abbreviationMol. Microbiol.
dcterms.oaStatusBronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidAlKa770-
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