Search results for "Proton-Translocating ATPases"

showing 10 items of 33 documents

Activation of the plant plasma membrane H+ -ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzy…

1996

The antagonistic effects of the fungal toxin beticolin-1 and of L-alpha-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme (aha2delta92). Phosphohydrolytic activities of both enzymes were inhibited by beticolin-1, with very similar 50% inhibitory concentrations, indicating that the toxin action does not involve the C-terminal located autoinhibitory domain of the proton pump. Egg lysoPC, a compound that activates the H+-ATPase by a mechanism involving the C-terminal part of the protein, was found to be able to reverse the inhibi…

0106 biological sciencesATPaseArabidopsismedicine.disease_cause01 natural sciencesBiochemistrychemistry.chemical_compoundStructural BiologyArabidopsis thalianaComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesbiologyPlantsRecombinant ProteinsIsoenzymesBeticolinProton-Translocating ATPasesLysophosphatidylcholineMembraneBiochemistryPlasma membrane H+-ATPase activationGene isoformAutoinhibitory domainDetergentsBiophysicsSaccharomyces cerevisiae[SDV.BC]Life Sciences [q-bio]/Cellular BiologyHeterocyclic Compounds 4 or More RingsStructure-Activity Relationship03 medical and health sciencesGeneticsmedicine[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesToxinCell MembraneLysophosphatidylcholinesCell BiologyMycotoxinsbiology.organism_classificationYeastEnzyme Activationl-α-LysophosphatidylcholineEnzymechemistryLiposomesbiology.protein010606 plant biology & botany
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Functional reconstitution of a proton-translocating system responsive to fusicoccin

1988

Crude fusicoccin binding proteins and a partially purified plasma membrane H+-transporting ATPase (EC 3.6.1.34), both solubilized from maize tissues, were simultaneously inserted into liposomes by the freeze-thaw method. ATP-driven intravesicular acidification in the proteoliposomes, measured by the fluorescence quenching of the dye 9-amino-6-chloro-2-methoxyacridine, markedly increased upon addition of fusicoccin to the reconstituted system. This effect could not be observed when binding sites and ATPase preparations were separately reconstituted into the proteoliposomes, thus demonstrating that fusicoccin binding to its receptor is a prerequisite for ATPase stimulation.

0106 biological sciencesATPase[SDV]Life Sciences [q-bio]01 natural sciences03 medical and health scienceschemistry.chemical_compoundProton transportGlycosidesBinding siteComputingMilieux_MISCELLANEOUSFluorescent Dyes030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeBinding SitesMultidisciplinarybiologyAminoacridinesCell MembraneBiological activityPlants[SDV] Life Sciences [q-bio]Proton-Translocating ATPasesMembraneEnzymeSolubilitychemistryBiochemistryFusicoccinLiposomesbiology.proteinResearch Article010606 plant biology & botany
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Ultrastructure of regions containing homologous loci in polytene chromosomes of Drosophila melanogaster and Drosophila subobscura.

1998

We have used a new approach involving in situ hybridisation and electron microscopy to establish ultrastructural homologies between polytene chromosome regions of Drosophila melanogaster and Drosophila subobscura. Twelve probes were chosen to cover all the chromosomal elements: the myospheroid gene, the collagen type IV gene, the collagen-like gene, the w26 homeobox gene, the beta3 tubulin gene, the kinesin heavy chain gene, the tryptophan hydrolase gene, the Hsp82, Hsp22-26 and Hsp23-28, Hsp68, Hsp70 genes and the beta unit of the F0-F1 ATPase gene. Most of these loci were previously undescribed in D. subobscura and imprecisely located in D. melanogaster. We have demonstrated here, by an u…

0106 biological sciencesIntegrinsHSP30 Heat-Shock ProteinsKinesinsMuscle ProteinsLocus (genetics)Genes InsectTryptophan Hydroxylase010603 evolutionary biology01 natural sciencesHomology (biology)Chromosomes03 medical and health sciencesTubulinSequence Homology Nucleic AcidGeneticsMelanogasterAnimalsDrosophila ProteinsHSP20 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsGeneGenetics (clinical)Heat-Shock Proteins030304 developmental biologyGenetics0303 health sciencesPolytene chromosomebiologyMembrane Proteinsbiology.organism_classificationDrosophila subobscuraChromosome BandingProton-Translocating ATPasesDrosophila melanogasterChromosomal regionCollagenDrosophila melanogasterDNA ProbesIntegrin alpha ChainsChromosoma
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Distinct lytic vacuolar compartments are embedded inside the protein storage vacuole of dry and germinating Arabidopsis thaliana seeds.

2011

International audience; Plant cell vacuoles are diverse and dynamic structures. In particular, during seed germination, the protein storage vacuoles are rapidly replaced by a central lytic vacuole enabling rapid elongation of embryo cells. In this study, we investigate the dynamic remodeling of vacuolar compartments during Arabidopsis seed germination using immunocytochemistry with antibodies against tonoplast intrinsic protein (TIP) isoforms as well as proteins involved in nutrient mobilization and vacuolar acidification. Our results confirm the existence of a lytic compartment embedded in the protein storage vacuole of dry seeds, decorated by γ-TIP, the vacuolar proton pumping pyrophospha…

0106 biological sciencesPhysiologyProtein storage vacuoleProton-pumping pyrophosphataseArabidopsisPlant ScienceVacuoleUNIQUEMESH: Protein Isoforms01 natural sciencesPYROPHOSPHATASEArabidopsisProtein IsoformsMESH: ArabidopsisH+-ATPASETONOPLAST INTRINSIC PROTEINPLANT-CELLSCation Transport ProteinsIN-VIVOPlant Proteinschemistry.chemical_classification0303 health sciencesMESH: Plant ProteinsGeneral MedicineCell biologyProtein TransportVacuolar acidificationLytic cycleSeedsPREVACUOLAR COMPARTMENTMESH: DesiccationVacuolar Proton-Translocating ATPasesMESH: Protein TransportMESH: Vacuolar Proton-Translocating ATPasesGerminationMESH: Arabidopsis ProteinsMESH: GerminationBiologyAquaporinsMESH: Vacuoles03 medical and health sciencesMESH: AquaporinsMESH: Cation Transport ProteinsStorage protein[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyLytic vacuoleDesiccation030304 developmental biologySeedArabidopsis ProteinsCell Biologybiology.organism_classificationTRANSPORTchemistryMESH: SeedsVacuolesVacuoleMEMBRANEMOBILIZATION010606 plant biology & botany
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Methylmercury-induced developmental toxicity is associated with oxidative stress and cofilin phosphorylation. Cellular and human studies

2017

Environmental exposure to methylmercury (MeHg) during development is of concern because it is easily incorporated in children’s body both pre- and post-natal, it acts at several levels of neural pathways (mitochondria, cytoskeleton, neurotransmission) and it causes behavioral impairment in child. We evaluated the effects of prolonged exposure to 10–600 nM MeHg on primary cultures of mouse cortical (CCN) and of cerebellar granule cells (CGC) during their differentiation period. In addition, it was studied if prenatal MeHg exposure correlated with altered antioxidant defenses and cofilin phosphorylation in human placentas (n = 12) from the INMA cohort (Spain). Exposure to MeHg for 9 days in v…

0301 basic medicineDevelopmental DisabilitiesGlutathione reductaseCiencias de la SaludMitochondrionMETHYLMERCURYToxicologymedicine.disease_causeProtein CarbonylationMiceCytosolMITOCHONDRIAPregnancyPhosphorylationOXIDATIVE STRESSCells Culturedchemistry.chemical_classificationNeuronsbiologyGeneral NeuroscienceGlutathione peroxidaseCOFILINBrainMethylmercuryEnvironmental exposureCofilinMethylmercury CompoundsMitochondrial Proton-Translocating ATPasesGlutathioneCell biologyMitochondriaGlutathione ReductaseActin Depolymerizing FactorsCofilinPhosphorylationFemaleHuman placentaactinCortactinCIENCIAS MÉDICAS Y DE LA SALUDmacromolecular substancesACTIN03 medical and health sciencesCultured neuronsmedicineAnimalsHumansCULTURED NEURONSGlutathione PeroxidaseSalud OcupacionalHUMAN PLACENTAMolecular biology030104 developmental biologychemistryAnimals NewbornOxidative stressbiology.proteinOxidative stress
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Actin Filaments Are Involved in the Coupling of V0-V1 Domains of Vacuolar H+-ATPase at the Golgi Complex*

2016

We previously reported that actin-depolymerizing agents promote the alkalization of the Golgi stack and the trans-Golgi network. The main determinant of acidic pH at the Golgi is the vacuolar-type H+-translocating ATPase (V-ATPase), whose V1 domain subunits B and C bind actin. We have generated a GFP-tagged subunit B2 construct (GFP-B2) that is incorporated into the V1 domain, which in turn is coupled to the V0 sector. GFP-B2 subunit is enriched at distal Golgi compartments in HeLa cells. Subcellular fractionation, immunoprecipitation, and inversal FRAP experiments show that the actin depolymerization promotes the dissociation of V1-V0 domains, which entails subunit B2 translocation from Go…

0301 basic medicineVacuolar Proton-Translocating ATPasesGolgi ApparatusBiologyMicrofilamentBiochemistry03 medical and health sciencessymbols.namesakeCytosolHumansActin-binding proteinMolecular BiologyLipid raftActinGolgi membraneCell BiologyIntracellular MembranesGolgi apparatusHydrogen-Ion ConcentrationActin cytoskeletonCell biologyProtein Structure TertiaryCytosolActin Cytoskeleton030104 developmental biologysymbolsbiology.proteinHeLa Cells
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Reconstitution of bacteriorhodopsin and ATP synthase from Micrococcus luteus into liposomes of the purified main tetraether lipid from Thermoplasma a…

1995

The archaebacterium Thermoplasma acidophilum is cultivated at 59 degrees C in a medium containing sulfuric acid of pH 2. The purified bipolar membrane spanning main phospholipid (MPL) of this organism can be used to produce stable liposomes of 100-500 nm in diameter either using a French pressure cell detergent dialysis or sonication. Despite a potassium diffusion potential of 186 mV very low ionic permeability of sonicated MPL liposomes was measured using the potassium binding fluorescent indicator benzofuran isophthalate PBF1, which measures net K+ uptake. The latter also remained very low, in the presence of the K(+) ionophore valinomycin and palmitic acid. Addition of valinomycin and th…

Carbonyl Cyanide p-TrifluoromethoxyphenylhydrazoneLightOctoxynolThermoplasmaBiochemistryPermeabilityPyranineValinomycinchemistry.chemical_compoundAdenosine TriphosphateProton transportParticle SizeMolecular BiologyPhospholipidsLiposomeChromatographyValinomycinbiologyIonophoresVesicleOrganic ChemistryFatty AcidsTemperatureThermoplasma acidophilumMembrane ProteinsPhospholipid EthersBacteriorhodopsinCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationMicrococcus luteusProton-Translocating ATPaseschemistryBacteriorhodopsinsLiposomesbiology.proteinGramicidinPotassiumProtonsChemistry and physics of lipids
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Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus.

2007

The Asian tiger mosquito, Aedes albopictus, is commonly infected by the gregarine parasite Ascogregarina taiwanensis, which develops extracellularly in the midgut of infected larvae. The intracellular trophozoites are usually confined within a parasitophorous vacuole, whose acidification is generated and controlled by the V(1)V(O) ATPase. This proton pump is driven by ATP hydrolysis, catalyzed inside the major subunit A. The subunit A encoding gene of the Aedes albopictus V(1)V(O) ATPase was cloned in pET9d1-His(3) and the recombinant protein, expressed in the Escherichia coli Rosetta 2 (DE3) strain, purified by immobilized metal affinity- and ion-exchange chromatography. The purified prote…

Circular dichroismVacuolar Proton-Translocating ATPasesATPaseProtein subunitGene ExpressionGenes InsectBiologyIn Vitro Techniquesmedicine.disease_causelaw.inventionAdenosine TriphosphateATP hydrolysislawAedesCatalytic DomainmedicineAnimalsNucleotideCloning MolecularEscherichia coliDNA Primerschemistry.chemical_classificationPhotoaffinity labelingBase SequenceMolecular biologyProtein SubunitsSpectrometry FluorescenceBiochemistrychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinRecombinant DNAInsect ProteinsBiotechnologyProtein expression and purification
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Molecular Systematics of Aphids and Their Primary Endosymbionts

2001

Abstract Aphids constitute a monophyletic group within the order Homoptera (i.e., superfamily Aphidoidea). The Aphidoidea originated in the Jurassic about 150 my ago from some aphidiform ancestor whose origin can be traced back to about 250 my ago. They exhibit a mutualistic association with intracellular bacteria ( Buchnera sp.) related to Escherichia coli. Buchnera is usually considered the aphids' primary endosymbiont. The association is obligate for both partners. The 16S rDNA-based phylogeny of Buchnera from four aphid families showed complete concordance with the morphology-based phylogeny of their aphid hosts, which pointed to a single original infection in a common ancestor of aphid…

DNA BacterialMolecular Sequence DataGenes InsectEvolution MolecularMonophylyBuchneraPhylogeneticsRNA Ribosomal 16SBotanyGeneticsAnimalsSymbiosisMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsAphidObligatebiologyfood and beveragesAphididaeDNASequence Analysis DNAbiochemical phenomena metabolism and nutritionbiology.organism_classificationProton-Translocating ATPasesSister groupGenes BacterialEvolutionary biologyAphidsMolecular phylogeneticsBuchneraMolecular Phylogenetics and Evolution
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Correction: DAPIT Over-Expression Modulates Glucose Metabolism and Cell Behaviour in HEK293T Cells

2015

Introduction Diabetes Associated Protein in Insulin-sensitive Tissues (DAPIT) is a subunit of mitochondrial ATP synthase and has also been found to associate with the vacuolar H+-ATPase. Its expression is particularly high in cells with elevated aerobic metabolism and in epithelial cells that actively transport nutrients and ions. Deletion of DAPIT is known to induce loss of mitochondrial ATP synthase but the effects of its over-expression are obscure. Results In order to study the consequences of high expression of DAPIT, we constructed a transgenic cell line that constitutively expressed DAPIT in human embryonal kidney cells, HEK293T. Enhanced DAPIT expression decreased mtDNA content and …

Epithelial-Mesenchymal Transitionmitochondrial metabolismBiolääketieteet - BiomedicineCellActive Transport Cell NucleusGene DosageRespiratory chainlcsh:MedicineGene ExpressionMitochondrionta3111glukoosiNeoplasmsmedicineHumansLactic Acidglucoselcsh:ScienceTranscription factorMultidisciplinaryATP synthasebiologyCell growthta1184lcsh:RHEK 293 cellsCorrectionMitochondrial Proton-Translocating ATPasesMitochondriaCell biologyHEK293 CellsDiabetes Associated Protein in Insulin-sensitive Tissuesmedicine.anatomical_structureCell culturebiology.proteinATP synthaselcsh:QResearch ArticlePLOS ONE
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