Search results for "TPA"

showing 10 items of 770 documents

Phosphorylated intermediate of a transport ATPase and activity of protein kinase in membranes from corn roots

1983

A maize-root microsomal fraction was enriched in ATPase by treatment with Triton X-100. This activity, which reached 1.2-2.0/mumol Pi x min-1 x mg protein-1, was specific for ATP, very slightly stimulated by K+, inhibited by orthovanadate and diethylstilbestrol, resistant to oligomycin and azide, and had a Km of 1.2 mM MgATP. Incubation of the microsomal fraction with [gamma 32-P]ATP followed by electrophoresis in acid conditions revealed the presence of several phosphoproteins. The phosphorylation of a 110000-Mr polypeptide reached the steady-state level in less than 5 s and rapidly turned over the phosphate group. The phosphorylation level was an hyperbolic function of the [ATP] with a Km…

0106 biological sciencesOligomycinATPaseHydroxylamineHydroxylaminesZea mays01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundHydroxylamineCationsMicrosomes[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyVanadate[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPhosphorylationProtein kinase ADiethylstilbestrol030304 developmental biologyAdenosine Triphosphatases2. Zero hunger0303 health sciencesbiologyCell MembraneBiological TransportVanadiumMolecular biologyMembranechemistryBiochemistryPhosphoproteinbiology.proteinPhosphorylationVanadatesPeptidesProtein Kinases010606 plant biology & botany
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Inhibition of adenosine trephosphatase activity from a plasma membrane fraction of acer pseudoplatanus cells by 2,2,2-trichloroethyl 3,4-dichlorocarb…

1986

2,2,2-Trichloroethyl 3,4-dichlorocarbanilate (SW26) is toxic for Acer pseudoplatanus cell cultures. It inhibited the cellular proton extrusion and depolarized the plasmalemma. In vitro, it inhibited the plasma membrane ATPase. SW 26 was also inhibitory to membrane ATPases of other origins-plant (maize shoot), fungus (Schizosaccharomyces pombe), and animal (dog kidney)-with about the same efficiency (7.5 micromolar < I(50) < 22 micromolar). It did not inhibit the oligomycin-sensitive ATPase from purified plant mitochondria, nor molybdate-sensitive soluble phosphatases. SW26 was more specific for plasma membrane ATPases than diethylstilbestrol or vanadate. A Lineweaver-Burk plot analysis show…

0106 biological sciencesPhysiologyATPasePhosphatasePlant ScienceMitochondrion01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsVanadate030304 developmental biologyMembrane potentialchemistry.chemical_classification0303 health sciencesbiologyERABLE FAUX PLATANEBiological activityAcer pseudoplatanusbiology.organism_classificationEnzymechemistryBiochemistrybiology.protein010606 plant biology & botany
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The Tonoplast H+ -ATPase of Acer pseudoplatanus is a vacuolar-type ATPase that operates with a phosphoenzyme intermediate

1995

The tonoplast H+-ATPase of Acer pseudoplatanus has been purified from isolated vacuoles. After solubilization, the purification procedure included size-exclusion and ion-exchange chromatography. The H+-ATPase consists of at least eight subunits, of 95, 66, 56, 54, 40, 38, 31, and 16 kD, that did not cross-react with polyclonal antibodies raised to the plasmalemma ATPase of Arabidopsis thaliana. The 66-kD polypeptide cross-reacted with monoclonal antibodies raised to the 70-kD subunit of the vacuolar H+-ATPase of oat roots. The functional molecular size of the tonoplast H+-ATPase, analyzed in situ by radiation inactivation, was found to be around 400 kD. The 66-kD subunit of the tonoplast H+…

0106 biological sciencesPhysiologyATPaseProtein subunitPlant ScienceVacuole01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compoundHydroxylamineProton transport[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGenetics030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyAcer pseudoplatanusbiology.organism_classificationEnzymechemistryBiochemistryPolyclonal antibodiesbiology.protein010606 plant biology & botanyResearch Article
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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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Cercospora beticola Toxin Inhibits Vanadate-Sensitive H+ Transport in Corn Root Membrane Vesicles

1988

The effect of Cercospora beticola toxin on the transport of protons by vanadate-sensitive ATPase was studied with corn (Zea mays) root microsomal vesicles prepared by differential centrifugation, sedimentation through a sucrose cushion, and washing with Triton X-100 plus KBr. In these preparations, addition of ATP induced intravesicular H(+)-accumulation as evidenced by a rapid quenching of the fluorescence of 9-amino-6-chloro-2-methoxy acridine. This quenching was relatively unaffected by inhibitors of mitochondrial and tonoplast-type ATPases, but was strongly reduced by inhibitors of plasma membrane H(+)-ATPase. C. beticola toxin markedly inhibited ATP dependent H(+)-transport, and this e…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]ATPasePlant Sciencemedicine.disease_cause01 natural sciences03 medical and health sciencesGeneticsmedicineVanadateMembranes and BioenergeticsCERCOSPORA BETICULAComputingMilieux_MISCELLANEOUS030304 developmental biologyDifferential centrifugation0303 health sciencesQuenching (fluorescence)biologyToxinVesicleMembrane transportCercospora beticolabiology.organism_classification[SDV] Life Sciences [q-bio]Biochemistrybiology.protein010606 plant biology & botanyPlant Physiology
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Quantitative proteomics reveals a dynamic association of proteins to detergent-resistant membranes upon elicitor signaling in tobacco.

2009

International audience; A large body of evidence from the past decade supports the existence, in membrane from animal and yeast cells, of functional microdomains playing important roles in protein sorting, signal transduction, or infection by pathogens. In plants, as previously observed for animal microdomains, detergent-resistant fractions, enriched in sphingolipids and sterols, were isolated from plasma membrane. A characterization of their proteic content revealed their enrichment in proteins involved in signaling and response to biotic and abiotic stress and cell trafficking suggesting that these domains were likely to be involved in such physiological processes. In the present study, w…

0106 biological sciencesProteomicsGTPase-activating proteinQuantitative proteomicsDetergentsPlasma protein bindingBiologymedicine.disease_causeProteomics01 natural sciencesBiochemistryMass SpectrometryAnalytical ChemistryCell membraneFungal Proteins03 medical and health sciencesProtein targetingTobaccomedicine[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyPlant Proteins0303 health sciencesFungal proteinStaining and LabelingResearchAlgal ProteinsCell MembraneCell biologymedicine.anatomical_structureBiochemistryLuminescent MeasurementsSignal transductionPeptidesReactive Oxygen Species010606 plant biology & botanyProtein BindingSignal TransductionMolecularcellular proteomics : MCP
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Cercospora beticola toxins. IX. Relationship between structure of beticolins, inhibition of plasma membrane H+ -ATPase and partition in lipid membran…

1996

Beticolins are yellow toxins produced by the fungus Cercospora beticola. The effect of one of them, beticolin-1, has been investigated on corn root plasma membrane H + -ATPase (EC 3.6.1.35) at different purification levels (plasma membrane fraction. partially, or highly purified enzyme). The results obtained demonstrated that (1) the purified proton pump was inhibited directly by low amounts of the toxin (I 50 =1.62 ± 0.18 μM), (2) the biological effects of beticolin-1 were similar to those of CBT (Cercospora beticola toxin). Furthermore, it was established that the efficiency of the different beticolins was clearly related to their ability to interact with the lipid bilayers, determined by…

0106 biological sciencesSTRUCTUREPhysiologyATPasePlant Science010402 general chemistrymedicine.disease_cause01 natural sciencesProton transportGeneticsmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyLipid bilayerComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationLiposomeChromatographybiologyChemistryToxinCell BiologyGeneral MedicineCercospora beticolabiology.organism_classification0104 chemical sciencesMembraneEnzymeBiochemistrybiology.protein010606 plant biology & botany
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Active vanadate-sensitive H+ translocation in corn roots membrane vesicles and proteoliposomes

1988

Abstract A member fraction from corn roots which contains a vanadate-sensitive ATPase activity has been prepared. The specific activity at 38°C is between 3 and mol 12 μmol · min −1 · mg −1 , depending on the age of roots. Addition of ATP promotes a very rapid quenching of the fluorescence of 9-amino-6-chloro-3-methoxy-acridin (ACMA). Proton pumping exhibits a delayed sensitivity to vanadate but is strongly and instantaneously inhibited by the new inhibitor SW 26. Both proton pumping, measured by the initial quenching rate, and ATP hydrolysis show maximum activities at ATP concentrations in the millimolar range, but the apparent K m -value for hydrolysis is higher than that observed for pro…

0106 biological sciencesTrisMolar concentrationATPase[SDV]Life Sciences [q-bio]Plant Science01 natural sciences03 medical and health scienceschemistry.chemical_compoundHydrolysisATP hydrolysisProton transportGeneticsVanadateComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesQuenching (fluorescence)biologyGeneral Medicine[SDV] Life Sciences [q-bio]chemistryBiochemistrybiology.proteinBiophysicsAgronomy and Crop Science010606 plant biology & botany
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Influence of ATPase activity on PPi dependent H+-transport in tonoplast vesicles of Acer pseudoplatanus

1994

Abstract Tonoplast H + -ATPase and H + -pyrophosphatase (H + -PPase) were previously characterized in Acer pseudoplatanus cells (A. Pugin et al., Plant Sci., 73 (1991) 23–34; A. Fraichard et al., Plant Physiol. Biochem., 31 (1993) 349–359). The present study concerns the relationships between these two enzymes in vitro. ATP and PPi hydrolysis were additive and the inhibition of one did not affect the activity of the second one. ATP and PPi H + -transports were also additive. The H + -PPase inhibition did not change ATP-dependent H + -transport but H + -ATPase inhibition inhibited the PPi dependent H + -transport. Because H + -PPase was reported to transport H + and K + into the vacuole (Dav…

0106 biological sciencesTrisStereochemistryATPasePlant ScienceVacuole01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compoundProton transport[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsTRANSPORT D'IONSGeneticsComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesPyrophosphatasebiologyERABLE FAUX PLATANEGeneral MedicineAcer pseudoplatanusbiology.organism_classificationEnzymechemistryBiochemistrybiology.proteinPMSFAgronomy and Crop Science010606 plant biology & botany
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Solute transporters in plant thylakoid membranes

2010

International audience; Plants utilize sunlight to drive photosynthetic energy conversion in the chloroplast thylakoid membrane. Here are located four major photosynthetic complexes, about which we have great knowledge in terms of structure and function. However, much less we know about auxiliary proteins, such as transporters, ensuring an optimum function and turnover of these complexes. The most prominent thylakoid transporter is the proton-translocating ATP-synthase. Recently, four additional transporters have been identified in the thylakoid membrane of Arabidopsis thaliana, namely one copper-transporting P-ATPase, one chloride channel, one phosphate transporter, and one ATP/ADP carrier…

0106 biological sciences[SDV]Life Sciences [q-bio]thylakoidArabidopsisphotosystemReviewsPhotosynthesis01 natural sciences03 medical and health sciencescarrierArabidopsislight stressATPaseArabidopsis thalianaIon channelmembrane transporter030304 developmental biologyPhotosystem2. Zero hunger0303 health sciencesphotosynthesisbiologyfood and beveragesbiology.organism_classificationBiochemistryThylakoidion channelQuantasomeGeneral Agricultural and Biological Sciences010606 plant biology & botanyChloroplast thylakoid membraneCommunicative &amp; Integrative Biology
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