Search results for "Response regulator"

showing 5 items of 25 documents

Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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Survival of Listeria monocytogenes in Soil Requires AgrA-Mediated Regulation

2015

ABSTRACT In a recent paper, we demonstrated that inactivation of the Agr system affects the patterns of survival of Listeria monocytogenes (A.-L. Vivant, D. Garmyn, L. Gal, and P. Piveteau, Front Cell Infect Microbiol 4:160, http://dx.doi.org/10.3389/fcimb.2014.00160 ). In this study, we investigated whether the Agr-mediated response is triggered during adaptation in soil, and we compared survival patterns in a set of 10 soils. The fate of the parental strain L. monocytogenes L9 (a rifampin-resistant mutant of L. monocytogenes EGD-e) and that of a Δ agrA deletion mutant were compared in a collection of 10 soil microcosms. The Δ agrA mutant displayed significantly reduced survival in these b…

RNA UntranslatedTranscription GeneticSurvivalMutantPopulationDynamicATP-binding cassette transporterBiology[SDV.SA.SDS]Life Sciences [q-bio]/Agricultural sciences/Soil studymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyTranscriptome03 medical and health sciencesSoilListeria monocytogenesBacterial Proteins[ SDV.SA.AGRO ] Life Sciences [q-bio]/Agricultural sciences/AgronomymedicineEnvironmental MicrobiologyGeneSoil Microbiology030304 developmental biology2. Zero hunger0303 health sciencesMicrobial ViabilityEcology[ SDV ] Life Sciences [q-bio]030306 microbiologyGene Expression ProfilingWild typeGene Expression Regulation BacterialListeria MonocytogenesResponse regulator[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyTranscriptomeSoil microbiologyGene DeletionFood ScienceBiotechnologyTranscription Factors
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Production of Norspermidine Contributes to Aminoglycoside Resistance in pmrAB Mutants of Pseudomonas aeruginosa

2019

Emergence of resistance to polymyxins in Pseudomonas aeruginosa is mainly due to mutations in two-components systems, that promote addition of 4-amino-4-deoxy-L-arabinose to the lipopolysaccharide (LPS) through upregulation of operon arnBCADTEF-ugd (arn) expression. Here, we demonstrate that mutations occurring in different domains of histidine kinase PmrB or in response regulator PmrA result in coresistance to aminoglycosides and colistin. All seventeen clinical strains tested exhibiting such a cross-resistance phenotype were found to be pmrAB mutants. As shown by gene deletion experiments, the decreased susceptibility of the mutants to aminoglycosides was independent from operon arn but r…

Spectrometry Mass Electrospray IonizationOperonSpermidineMutantMicrobial Sensitivity TestsMicrobiology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsMechanisms of Resistance[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]PolyaminesPharmacology (medical)GeneComputingMilieux_MISCELLANEOUS030304 developmental biologyPharmacology0303 health sciences030306 microbiologyColistinNorspermidineHistidine kinaseGene Expression Regulation Bacterial[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyAnti-Bacterial AgentsResponse regulatorInfectious DiseasesAminoglycosideschemistryPseudomonas aeruginosaEffluxBacterial outer membraneTranscription Factors
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Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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The NreA Protein Functions as a Nitrate Receptor in the Staphylococcal Nitrate Regulation System

2013

Staphylococci are able to use nitrate as an alternative electron acceptor during anaerobic respiration. The regulation of energy metabolism is dependent on the presence of oxygen and nitrate. Under anaerobic conditions, staphylococci employ the nitrate regulatory element (Nre) for transcriptional activation of genes involved in reduction and transport of nitrate and nitrite. Of the three proteins that constitute the Nre system, NreB has been characterized as an oxygen sensor kinase and NreC has been characterized as its cognate response regulator. Here, we present structural and functional data that establish NreA as a new type of nitrate receptor. The structure of NreA with bound nitrate w…

chemistry.chemical_classificationAnaerobic respirationStaphylococcusIodideIsothermal titration calorimetryGene Expression Regulation BacterialElectron acceptorCrystallography X-RayResponse ElementsNitrate reductaseNitrate ReductaseProtein Structure SecondaryBacteria Anaerobicchemistry.chemical_compoundResponse regulatorNitratechemistryBiochemistryStructural BiologyMutationBinding siteMolecular BiologyJournal of Molecular Biology
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