Search results for "binding"

showing 10 items of 3896 documents

ABP1 Mediates Auxin Inhibition of Clathrin-Dependent Endocytosis in Arabidopsis

2010

SummarySpatial distribution of the plant hormone auxin regulates multiple aspects of plant development. These self-regulating auxin gradients are established by the action of PIN auxin transporters, whose activity is regulated by their constitutive cycling between the plasma membrane and endosomes. Here, we show that auxin signaling by the auxin receptor AUXIN-BINDING PROTEIN 1 (ABP1) inhibits the clathrin-mediated internalization of PIN proteins. ABP1 acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis. Auxin binding to ABP1 interferes with this action and leads to the inhibition of clathrin-mediated endocytosis. Our study demonstrates th…

0106 biological sciencesEndosomemedia_common.quotation_subjectArabidopsisReceptors Cell SurfaceEndocytosis01 natural sciencesClathrinGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesAuxinheterocyclic compoundsPIN proteinsInternalization030304 developmental biologymedia_commonPlant Proteinschemistry.chemical_classificationAuxin binding0303 health sciencesbiologyIndoleacetic AcidsBiochemistry Genetics and Molecular Biology(all)Arabidopsis ProteinsCell MembranefungiMembrane Transport Proteinsfood and beveragesReceptor-mediated endocytosisClathrinEndocytosisCell biologychemistrybiology.protein010606 plant biology & botanyCell
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Wild

2021

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0106 biological sciencesGermplasmPhytochemistryTPCC total phenolic contentElderberry flowerISSR inter-simple sequence repeatElderberry fruitIC50 the half maximal inhibitory concentrationBerrySambucus nigra01 natural sciencesArticleTFC total flavonoid contentDW dry weightSARS-CoV2 severe acute respiratory syndrome coronavirus 2Rutinchemistry.chemical_compoundBotanyELISA enzyme linked immunosorbent assayCultivarAntiviralComputingMethodologies_COMPUTERGRAPHICSGenetic diversityACE2 angiotensin converting enzyme 2biology010405 organic chemistryPVPP polyvinylpyrrolidoneSambucus nigra L.biology.organism_classification0104 chemical scienceschemistryHPLC high-performance liquid chromatographyTEAC trolox equivalent anti-radical capacityGene poolAgronomy and Crop Science010606 plant biology & botanyBinding domainIndustrial crops and products
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Tobacco cells contain a protein, immunologically related to the neutrophil small G protein Rac2 and involved in elicitor-induced oxidative burst.

1997

Abstract Suspension-cultured cells of Nicotiana tabacum generated active oxygen species (AOS) when they were treated with the proteinaceous elicitor, cryptogein. This response was blocked by diphenylene iodonium, an inhibitor of the neutrophil NADPH oxidase. When microsomal extracts of tobacco cells were probed with an antibody directed against the human small G protein Rac2, two immunoreactive proteins were detected at 18.5 and 20.5 kDa. The same experiment performed with cytosolic extracts of tobacco cells led to the observation of a strong immunoreactive protein at 21.5 kDa only in the cryptogein-treated cells. The appearance of this cytosolic protein was related to the production of AOS…

0106 biological sciencesHypersensitive responseNicotiana tabacumBlotting WesternBiophysicsSmall G Protein01 natural sciencesBiochemistrySuperoxide dismutaseFungal Proteins03 medical and health sciencesStructural BiologyGTP-Binding ProteinsTobaccoGeneticsMolecular BiologyCells Cultured030304 developmental biologyRespiratory Burst0303 health sciencesNADPH oxidasebiologyNADPH oxidaseNicotiana tabacumAlgal Proteinsfood and beveragesCell Biologybiology.organism_classificationMolecular biologyOxidative burst3. Good healthElicitorRespiratory burstrac GTP-Binding ProteinsSmall G proteinCytosolPlants ToxicBiochemistrybiology.proteinCryptogeinReactive Oxygen Species010606 plant biology & botanyRac2FEBS letters
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Coupling transcriptomics and behaviour to unveil the olfactory system of Spodoptera exigua larvae

2020

AbstractChemoreception in insects is crucial for many aspects related to food seeking, enemy avoidance, and reproduction. Different families of receptors and binding proteins interact with chemical stimuli, including odorant receptors (ORs), ionotropic receptors (IRs), gustatory receptors (GRs), odorant binding proteins (OBPs) and chemosensory proteins (CSPs). In this work, we describe the chemosensory-related gene repertoire of the worldwide spread pest Spodoptera exigua (Lepidoptera: Noctuide) focusing on the transcripts expressed in larvae, which feed on many horticultural crops producing yield losses. A comprehensive de novo assembly that includes reads from chemosensory organs of larva…

0106 biological sciencesMaleOlfactory systemanimal structuresOdorant bindingmedia_common.quotation_subject[SDV]Life Sciences [q-bio]Gene ExpressionOlfactionInsectSpodopteraSpodopteraReceptors Odorant01 natural sciencesBiochemistryLepidoptera genitaliaTranscriptomeBeet armywormExiguaAnimalsRNA-SeqPheromone bindingAcroleinGeneEcology Evolution Behavior and SystematicsComputingMilieux_MISCELLANEOUSmedia_commonGeneticsGenomic LibraryPropiophenonesbiologyGene Expression ProfilingfungiGeneral Medicinebiology.organism_classification010602 entomologyOrgan SpecificityLarvaOdorantsNoctuidaeInsect ProteinsFemaleHexanolsTranscriptome010606 plant biology & botany
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Molecular Bases for Sensitivity to Tubulin-Binding Herbicides in Green Foxtail

2004

Abstract We investigated the molecular bases for resistance to several classes of herbicides that bind tubulins in green foxtail (Setaria viridis L. Beauv.). We identified two α- and two β-tubulin genes in green foxtail. Sequence comparison between resistant and sensitive plants revealed two mutations, a leucine-to-phenylalanine change at position 136 and a threonine-to-isoleucine change at position 239, in the gene encoding α2-tubulin. Association of mutation at position 239 with herbicide resistance was demonstrated using near-isogenic lines derived from interspecific pairings between green foxtail and foxtail millet (Setaria italica L. Beauv.), and herbicide sensitivity bioassays combine…

0106 biological sciencesModels MolecularSetariaPhysiologyProtein ConformationMolecular Sequence DataSetaria PlantDrug ResistancePlant Sciencemedicine.disease_cause01 natural sciencesTubulin binding[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesFocus Issue on the Plant CytoskeletonSpecies SpecificityTubulin[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsBotanyGeneticsmedicineBioassayAmino Acid SequenceGeneCross-resistancePhylogenyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesMutationbiologyBase SequenceSetaria viridisHerbicidesbiology.organism_classificationBiochemistryFoxtail010606 plant biology & botanyProtein Binding
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Evidence for specific, high-affinity binding sites for a proteinaceous elicitor in tobacco plasma membrane

1995

Abstract Binding of cryptogein, a proteinaceous elicitor, was studied on tobacco plasma membrane. The binding of the [125I]cryptogein was saturable, reversible and specific with an apparent Kd of 2 nM. A single class of cryptogein binding sites was found with a sharp optimum pH for binding at about pH 7.0. The high-affinity correlates with cryptogein concentrations required for biological activity in vivo.

0106 biological sciencesNicotiana tabacumBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular Biology01 natural sciencesBiochemistryFungal Proteins03 medical and health sciencesStructural BiologyIn vivoTobaccoGeneticsBinding siteReceptor[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesBinding SitesbiologyNicotiana tabacumChemistryAlgal ProteinsCell MembraneElicitinBiological activityCell BiologyElicitorbiology.organism_classification3. Good healthElicitorKineticsPlants ToxicMembraneBiochemistryCryptogeinPlasma membraneReceptor010606 plant biology & botany
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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Molecular Bases for Sensitivity to Acetyl-Coenzyme A Carboxylase Inhibitors in Black-Grass

2005

Abstract In grasses, residues homologous to residues Ile-1,781 and Ile-2,041 in the carboxyl-transferase (CT) domain of the chloroplastic acetyl-coenzyme A (CoA) carboxylase (ACCase) from the grass weed black-grass (Alopecurus myosuroides [Huds.]) are critical determinants for sensitivity to two classes of ACCase inhibitors, aryloxyphenoxypropionates (APPs) and cyclohexanediones. Using natural mutants of black-grass, we demonstrated through a molecular, biological, and biochemical approach that residues Trp-2,027, Asp-2,078, and Gly-2,096 are also involved in sensitivity to ACCase inhibitors. In addition, residues Trp-2,027 and Asp-2,078 are very likely involved in CT activity. Using three-…

0106 biological sciencesPhysiologyCoenzyme AMutantPlant Sciencemedicine.disease_cause01 natural scienceschemistry.chemical_compound[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyGeneticsmedicineVULPIN[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding siteComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationMutationbiologyAlopecurus myosuroidesfood and beveragesActive site04 agricultural and veterinary sciencesbiology.organism_classificationPyruvate carboxylaseEnzymechemistryBiochemistry040103 agronomy & agriculturebiology.protein0401 agriculture forestry and fisheries010606 plant biology & botanyPlant Physiology
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Comparison of binding properties and early biological effects of elicitins in tobacco cells

1998

Abstract Elicitins are a family of small proteins secreted by Phytophthora species that have a high degree of homology and elicit defense reactions in tobacco (Nicotiana tabacum). They display acidic or basic characteristics, the acidic elicitins being less efficient in inducing plant necrosis. In this study we compared the binding properties of four elicitins (two basic and two acidic) and early-induced signal transduction events (Ca2+ influx, extracellular medium alkalinization, and active oxygen species production). The affinity for tobacco plasma membrane-binding sites and the number of binding sites were similar for all four elicitins. Furthermore, elicitins compete with one another fo…

0106 biological sciencesPhysiologyNicotiana tabacumPlant Science01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesCell surface receptor[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsExtracellularBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologyBinding proteinElicitinTECHNIQUE DES TRACEURSbiology.organism_classificationElicitorBiochemistryCULTURE DE CELLULESignal transduction010606 plant biology & botanyResearch Article
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Elicitins, proteinaceous elicitors of plant defense, are a new class of sterol carrier proteins

1998

Some phytopathogenic fungi within Phytophthora species are unable to synthesize sterols and therefore must pick them up from the membranes of their host-plant, using an unknown mechanism. These pseudo-fungi secrete elicitins which are small hydrophilic cystein-rich proteins. The results show that elicitins studied interact with dehydroergosterol in the same way, but with some time-dependent differences. Elicitins have one binding site with a similar strong affinity for dehydroergosterol. Using a non-steroid hydrophobic fluorescent probe, we showed that phytosterols are able to similarly bind to elicitins. Moreover, elicitins catalyze sterol transfer between phospholipidic artificial membran…

0106 biological sciencesPhytophthora[SDV]Life Sciences [q-bio]Biophysics01 natural sciencesBiochemistryFungal Proteins03 medical and health sciencesNaphthalenesulfonatesErgosterolPlant defense against herbivoryExtracellularSecretionBinding sitePERSPECTIVEMolecular BiologyPhospholipidsComputingMilieux_MISCELLANEOUS030304 developmental biologyFluorescent Dyes0303 health sciencesBinding SitesbiologyfungiAlgal ProteinsPhytosterolsElicitinBiological TransportCell BiologyPlantsbiology.organism_classificationSterolCell biology[SDV] Life Sciences [q-bio]KineticsMembraneSpectrometry FluorescenceBiochemistryPhytophthoraCarrier Proteins010606 plant biology & botanyProtein Binding
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