Search results for "Proton Pumps"

showing 5 items of 5 documents

Requirement for the Proton-Pumping NADH Dehydrogenase I of Escherichia Coli in Respiration of NADH to Fumarate and Its Bioenergetic Implications

1997

In Escherichia coli the expression of the nuo genes encoding the proton pumping NADH dehydrogenase I is stimulated by the presence of fumarate during anaerobic respiration. The regulatory sites required for the induction by fumarate, nitrate and O2 are located at positions around –309, –277, and downstream of –231 bp, respectively, relative to the transcriptional-start site. The fumarate regulator has to be different from the O2 and nitrate regulators ArcA and NarL. For growth by fumarate respiration, the presence of NADH dehydrogenase I was essential, in contrast to aerobic or nitrate respiration which used preferentially NADH dehydrogenase II. The electron transport from NADH to fumarate …

Anaerobic respirationAcetatesmedicine.disease_causeBiochemistryElectron TransportFumaratesEscherichia colimedicineDimethyl SulfoxideNADH NADPH OxidoreductasesAnaerobiosisEscherichia colichemistry.chemical_classificationElectron Transport Complex IEthanolbiologyNADH dehydrogenaseGene Expression Regulation BacterialProton PumpsElectron acceptorFumarate reductaseNADElectron transport chainGlycerol-3-phosphate dehydrogenaseBiochemistrychemistryElectron Transport Complex Ibiology.proteinEnergy MetabolismEuropean Journal of Biochemistry
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Organelle pH studies using targeted avidin and fluorescein–biotin

2000

Abstract Background: Mammalian organelles of the secretory pathway are of differing pH. The pH values form a decreasing gradient: the endoplasmic reticulum (ER) is nearly neutral, the Golgi is mildly acidic and the secretory granules are more acidic still (∼pH 5). The mechanisms that regulate pH in these organelles are still unknown. Results: Using a novel method, we tested whether differences in H + ‘leak' and/or counterion conductances contributed to the pH difference between two secretory pathway organelles. A pH-sensitive, membrane-permeable fluorescein–biotin was targeted to endoplasmic-reticulum- and Golgi-localized avidin-chimera proteins in HeLa cells. In live, intact cells, ER pH (…

Clinical BiochemistryBiotinGolgi ApparatusEndoplasmic ReticulumBiochemistrysymbols.namesakechemistry.chemical_compoundChloridesBiotinOrganelleDrug DiscoveryHumansMicroscopy ImmunoelectronMolecular BiologySecretory pathwayFluorescent DyesOrganellesPharmacologyIon TransportFlubi-2ChemistryEndoplasmic reticulumBafilomycinIntracellular MembranesGeneral MedicineHydrogen-Ion ConcentrationProton PumpsGolgi apparatusAvidinCytosolTargeted fluorescenceMembraneBiochemistryH+ pumpPotassiumsymbolsMolecular MedicineFluoresceinHeLa CellsH+ leakChemistry & Biology
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Differential salinity-induced variations in the activity of H+-pumps and Na+/H+ antiporters that are involved in cytoplasm ion homeostasis as a funct…

2011

The characterisation of cellular responses to salinity in staple crops is necessary for the reliable identification of physiological markers of salinity tolerance. Under saline conditions, variations in proton gradients that are generated by membrane-bound H⁺ pumps are crucial for maintaining cytoplasm homeostasis. We examined short (15 h) and longer term effects (4 days) of NaCl stress on the H⁺ pumping activities that are associated with the plasma membrane (P-ATPase) and the tonoplast (V-ATPase and V-PPase) in rice (Oryza sativa L.) callus lines that displayed different levels of NaCl tolerance and were established from two japonica rice cultivars. The applied stress conditions were base…

CytoplasmSalinitySodium-Hydrogen ExchangersGenotypePhysiologyAntiporterPlant ScienceVacuoleSodium ChlorideBiologyCell Linechemistry.chemical_compoundSpecies SpecificityStress PhysiologicalBotanyGeneticsHomeostasisAdenosine TriphosphatasesOryza sativaHydrolysisCell MembraneSodiumfood and beveragesBiological TransportOryzaSalt ToleranceProton PumpsPlants Genetically ModifiedGenetically modified riceEnzyme ActivationSalinityIon homeostasischemistryCytoplasmBiophysicsX-GlucPlant Physiology and Biochemistry
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Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide

2011

DAPIT (Diabetes Associated Protein in Insulin-sensitive Tissues) is a small, phylogenetically conserved, 58 amino acid peptide that was previously shown to be down-regulated at mRNA level in insulin-sensitive tissues of type 1 diabetes rats. In this study we characterize a custom made antibody against DAPIT and confirm the mitochondrial presence of DAPIT on cellular level. We also show that DAPIT is localized in lysosomes of HUVEC and HEK 293T cells. In addition, we describe the histological expression of DAPIT in several tissues of rat and man and show that it is highly expressed especially in cells with high aerobic metabolism and epithelial cells related to active transport of nutrients …

HistologyCellular respirationProtein subunitBiophysicsPeptideV-ATPaseBiologyMitochondrionAntibodiesMitochondrial ProteinsHuman Umbilical Vein Endothelial CellsV-ATPaseAnimalsHumansmitochondrionta315lcsh:QH301-705.5PhylogenyDAPIT mitochondrion V-ATPase type 1 diabeteschemistry.chemical_classificationRegulation of gene expressionOriginal Papertype 1 diabetes.HEK 293 cellsMembrane ProteinsCell BiologyProton PumpsCell biologyMitochondriaRatsHEK293 CellsMembrane proteinchemistryBiochemistryGene Expression Regulationlcsh:Biology (General)Organ SpecificityLysosomesDAPITEuropean Journal of Histochemistry
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Kinetics of proton release and uptake by channelrhodopsin-2

2012

Electrophysiological experiments showed that the light-activated cation channel channelrhodopsin-2 (ChR2) pumps protons in the absence of a membrane potential. We determined here the kinetics of transient pH change using a water-soluble pH-indicator. It is shown that ChR2 released protons prior to uptake with a stoichiometry of 0.3 protons per ChR2. Comparison to the photocycle kinetics revealed that proton release and uptake match rise and decay of the View the MathML sourceP3520 intermediate. As the View the MathML sourceP3520 state also represents the conductive state of cation channeling, the concurrence of proton pumping and channel gating implies an intimate mechanistic link of the tw…

Models MolecularRhodopsinProtonKineticsBiophysicsAnalytical chemistryChannelrhodopsinBacteriorhodopsinBiochemistry530Protein Structure SecondaryProton transferStructural BiologyGeneticsMolecular BiologyIon channelMembrane potentialbiologyChemistryfungiBacteriorhodopsinBiological TransportCell BiologyHydrogen-Ion ConcentrationProton PumpsOptogeneticsKineticsRhodopsinBiophysicsbiology.proteinProtonsIon channelStoichiometry
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