Search results for "Antiporter"

showing 10 items of 31 documents

Conversion of the sensor kinase DcuS ofEscherichia coliof the DcuB/DcuS sensor complex to the C4-dicarboxylate responsive form by the transporter DcuB

2016

Summary The sensor kinase DcuS of Escherichia coli co-operates under aerobic conditions with the C4-dicarboxylate transporter DctA to form the DctA/DcuS sensor complex. Under anaerobic conditions C4-dicarboxylate transport in fumarate respiration is catalyzed by C4-dicarboxylate/fumarate antiporter DcuB. (i) DcuB interacted with DcuS as demonstrated by a bacterial two-hybrid system (BACTH) and by co-chromatography of the solubilized membrane-proteins (mHPINE assay). (ii) In the DcuB/DcuS complex only DcuS served as the sensor since mutations in the substrate site of DcuS changed substrate specificity of sensing, and substrates maleate or 3-nitropropionate induced DcuS response without affec…

0301 basic medicineKinaseAntiporter030106 microbiologyTransporterBiologymedicine.disease_causeMicrobiology03 medical and health sciencesBiochemistrySolubilizationmedicineSubstrate specificityEscherichia coliEcology Evolution Behavior and SystematicsEnvironmental Microbiology
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A Thermodynamic Model of Monovalent Cation Homeostasis in the Yeast Saccharomyces cerevisiae

2016

Cationic and heavy metal toxicity is involved in a substantial number of diseases in mammals and crop plants. Therefore, the understanding of tightly regulated transporter activities, as well as conceiving the interplay of regulatory mechanisms, is of substantial interest. A generalized thermodynamic description is developed for the complex interplay of the plasma membrane ion transporters, membrane potential and the consumption of energy for maintaining and restoring specific intracellular cation concentrations. This concept is applied to the homeostasis of cation concentrations in the yeast cells of S. cerevisiae. The thermodynamic approach allows to model passive ion fluxes driven by the…

0301 basic medicinePhysiologyATPaseAntiporterYeast and Fungal ModelsPhysical ChemistryBiochemistryIon ChannelsCation homeostasisMedicine and Health SciencesHomeostasislcsh:QH301-705.5Membrane potentialEcologybiologyChemistryOrganic CompoundsPhysicsMonosaccharidesElectrophysiologyChemistryComputational Theory and MathematicsBiochemistryModeling and SimulationPhysical SciencesThermodynamicsProtonsAlgorithmsResearch ArticleChemical ElementsSaccharomyces cerevisiaeCarbohydratesSaccharomyces cerevisiaeResearch and Analysis MethodsMembrane PotentialModels Biological03 medical and health sciencesCellular and Molecular NeuroscienceSaccharomycesModel OrganismsCationsGeneticsMolecular BiologyEcology Evolution Behavior and SystematicsIon transporterNuclear PhysicsNucleonsIonsOrganic ChemistrySodiumChemical CompoundsOrganismsFungiBiology and Life SciencesComputational BiologyBiological Transportbiology.organism_classificationYeast030104 developmental biologyGlucoseMetabolismlcsh:Biology (General)SymporterActive transportbiology.proteinBiophysicsPLoS Computational Biology
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Bowel Dilation Diagnosed Prenatally.

2017

AdultDiarrheamedicine.medical_specialtyCongenital chloride diarrheaColonMEDLINEPrenatal diagnosisGestational AgeConservative TreatmentUltrasonography Prenatal03 medical and health sciences0302 clinical medicinePregnancy030225 pediatricsPrenatal DiagnosismedicineHumansChloride-Bicarbonate AntiportersPregnancy030219 obstetrics & reproductive medicinebusiness.industryObstetricsCesarean SectionFollow up studiesInfant NewbornPregnancy OutcomeGestational ageGene Expression Regulation Developmentalmedicine.diseaseDilatationMagnetic Resonance ImagingSulfate TransportersPediatrics Perinatology and Child HealthFemaleUltrasonographybusinessBowel dilationMetabolism Inborn ErrorsFollow-Up StudiesThe Journal of pediatrics
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Insulin-like growth factor 1 and sodium-lithium countertransport in essential hypertension and in hypertensive left ventricular hypertrophy

1993

The aim of this work was to study the insulin-like growth factor 1 (IGF1), a substance able to promote cell proliferation in vascular smooth muscle, in patients with mild-to-moderate hypertension and to analyse its relationship to sodium-lithium countertransport, a genetic marker of hypertension that is related to cardiovascular complications.We studied 32 hypertensive subjects, some with left ventricular hypertrophy, and 14 healthy subjects. Fasting plasma IGF1 was measured by means of a radioimmunoassay after octadecylsilica chromatography and Na(+)-Li+ countertransport was determined by the method of Canessa.Hypertensive patients had higher values of both IGF1 and Na(+)-Li+ countertransp…

AdultMalemedicine.medical_specialtyErythrocytesVascular smooth muscleLithium (medication)Heart diseasePhysiologymedicine.medical_treatmentEssential hypertensionLeft ventricular hypertrophyAntiportersMuscle hypertrophyInsulin-like growth factorReference ValuesInternal medicineInternal MedicineHumansMedicineInsulin-Like Growth Factor Ibusiness.industryGrowth factorMiddle Agedmedicine.diseaseEndocrinologyHypertensionFemaleHypertrophy Left VentricularCardiology and Cardiovascular Medicinebusinessmedicine.drug
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C4-dicarboxylate carriers and sensors in bacteria

2002

AbstractBacteria contain secondary carriers for the uptake, exchange or efflux of C4-dicarboxylates. In aerobic bacteria, dicarboxylate transport (Dct)A carriers catalyze uptake of C4-dicarboxylates in a H+- or Na+-C4-dicarboxylate symport. Carriers of the dicarboxylate uptake (Dcu)AB family are used for electroneutral fumarate:succinate antiport which is required in anaerobic fumarate respiration. The DcuC carriers apparently function in succinate efflux during fermentation. The tripartite ATP-independent periplasmic (TRAP) transporter carriers are secondary uptake carriers requiring a periplasmic solute binding protein. For heterologous exchange of C4-dicarboxylates with other carboxylic …

Aerobic bacteriaAntiporterSuccinic AcidBiophysicsOrganic Anion TransportersReceptors Cell Surfacemedicine.disease_causeBiochemistryFumarate (succinate) sensorTwo-component systemBacterial ProteinsFumaratesEscherichia colimedicineAmino Acid SequenceEscherichia coliDicarboxylate uptake SHistidine protein kinasePhylogenyHistidineDicarboxylic Acid TransportersDicarboxylate transport BbiologyEscherichia coli ProteinsBiological TransportPeriplasmic spaceCell Biologybiology.organism_classificationTwo-component regulatory systemBacteria AerobicModels ChemicalBiochemistryAntiportFumarate/succinate transportEffluxDicarboxylate uptake carrierProtein KinasesDicarboxylate transport A carrierBacteriaSignal TransductionBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Transport of C(4)-dicarboxylates in Wolinella succinogenes.

2000

ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…

Anaerobic respirationAntiporterPhysiology and MetabolismMutantMalatesBiologymedicine.disease_causeMicrobiologyCell membraneElectron TransportOxygen ConsumptionBacterial ProteinsFumaratesRespirationmedicineDicarboxylic AcidsAnaerobiosisMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidNitratesEscherichia coli ProteinsCell MembraneSodiumMembrane ProteinsBiological TransportSuccinatesFumarate reductaseElectron transport chainWolinellamedicine.anatomical_structureBiochemistryMutagenesisCarrier ProteinsGene DeletionJournal of bacteriology
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DctA- and Dcu-independent transport of succinate in Escherichia coli : contribution of diffusion and of alternative carriers

2001

Quintuple mutants of Escherichia coli deficient in the C4-dicarboxylate carriers of aerobic and anaerobic metabolism (DctA, DcuA, DcuB, DcuC, and the DcuC homolog DcuD, or the citrate/succinate antiporter CitT) showed only poor growth on succinate (or other C4-dicarboxylates) under oxic conditions. At acidic pH (pH 6) the mutants regained aerobic growth on succinate, but not on fumarate. Succinate uptake by the mutants could not be saturated at physiological succinate concentrations (≤5 mM), in contrast to the wild-type, which had a K m for succinate of 50 µM and a V max of 35 U/g dry weight at pH 6. At high substrate concentrations, the mutants showed transport activities (32 U/g dry weigh…

AntiporterMutantSuccinic AcidBiologymedicine.disease_causeBiochemistryMicrobiologyBacterial ProteinsFumaratesNitrilesEscherichia coliGeneticsmedicineMolecular BiologyEscherichia coliDicarboxylic Acid TransportersUncoupling AgentsEscherichia coli ProteinsBiological TransportGeneral MedicineMetabolismHydrogen-Ion ConcentrationFumarate reductasebiology.organism_classificationEnterobacteriaceaeBiochemistryMutationFermentationEffluxCarrier ProteinsArchives of Microbiology
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The Fumarate/Succinate Antiporter DcuB of Escherichia coli Is a Bifunctional Protein with Sites for Regulation of DcuS-dependent Gene Expression

2008

DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and s…

AntiporterMutantlac operonBiologymedicine.disease_causePeptide MappingBiochemistryAntiportersFumaratesEscherichia colimedicineMolecular BiologyEscherichia coliDerepressionDicarboxylic Acid TransportersIon TransportEscherichia coli ProteinsMutagenesisSuccinatesGene Expression Regulation BacterialCell BiologyPeriplasmic spaceFumarate reductaseDNA-Binding ProteinsSuccinate DehydrogenaseAmino Acid SubstitutionBiochemistryGene Knockdown TechniquesMutagenesis Site-DirectedProtein KinasesTranscription FactorsJournal of Biological Chemistry
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Interaction of theEscherichia colitransporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units

2012

The aerobic Escherichia coli C(4) -dicarboxylate transporter DctA and the anaerobic fumarate/succinate antiporter DcuB function as obligate co-sensors of the fumarate responsive sensor kinase DcuS under aerobic or anaerobic conditions respectively. Overproduction under anaerobic conditions allowed DctA to replace DcuB in co-sensing, indicating their functional equivalence in this capacity. In vivo interaction studies between DctA and DcuS using FRET or a bacterial two-hybrid system (BACTH) demonstrated their interaction. DctA-YFP bound to an affinity column and was able to retain DcuS. DctA shows substantial sequence and secondary structure conservation to Glt(Ph), the Na(+)/glutamate sympo…

AntiporterPlasma protein bindingBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyPyrococcus horikoshiiTransmembrane domainBiochemistryHelixSymportermedicineMolecular BiologyEscherichia coliProtein secondary structureMolecular Microbiology
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Functional characterization of ORCTL2--an organic cation transporter expressed in the renal proximal tubules.

1998

AbstractChromosome 11p15.5 harbors a gene or genes involved in Beckwith-Wiedemann syndrome that confer(s) susceptibility to Wilms' tumor, rhabdomyosarcoma, and hepatoblastoma. We have previously identified a transcript at 11p15.5 which encodes a putative membrane transport protein, designated organic cation transporter-like 2 (ORCTL2), that shares homology with tetracycline resistance proteins and bacterial multidrug resistance proteins. In this report, we have investigated the transport properties of ORCTL2 and show that this protein can confer resistance to chloroquine and quinidine when overexpressed in bacteria. Immunohistochemistry analyses performed with anti-ORCTL2 polyc.onal antibod…

Beckwith-Wiedemann SyndromeOrganic Cation Transport ProteinsTranscription GeneticMolecular Sequence DataBiophysicsTransfectionBiochemistryHomology (biology)11p15.5Kidney Tubules ProximalStructural BiologyGeneticsmedicineAnimalsHumansMolecular BiologyGeneTetracycline/H+ antiporterKidneyOrganic cation transport proteinsbiologyBacteriaBase SequenceMembrane transport proteinOrganic cation transporterMultidrug resistance-associated protein 2Chromosomes Human Pair 11Tetracycline ResistanceOrganic cation transporter like-2Chromosome MappingMembrane ProteinsBiological TransportChloroquineCell BiologyApical membraneTetracyclineMolecular biologyQuinidineDrug Resistance MultipleRecombinant ProteinsKineticsmedicine.anatomical_structureBiochemistryOligodeoxyribonucleotidesCOS Cellsbiology.proteinImmunohistochemistryCarrier ProteinsFEBS letters
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