Search results for "Binding Sites"

showing 10 items of 636 documents

Specific binding of Bacillus thuringiensis Cry1Ea toxin, and Cry1Ac and Cry1Fa competition analyses in Anticarsia gemmatalis and Chrysodeixis include…

2019

AbstractAnticarsia gemmatalis (velvetbean caterpillar) and Chrysodeixis includens (soybean looper) are two important defoliation pests of soybeans. In the present study, we have investigated the susceptibility and brush border membrane-binding properties of both species to Bacillus thuringiensis Cry1Ea toxin. Bioassays performed in first-instar larvae demonstrated potent activity against both soybean pests in terms of mortality or practical mortality. Competition-binding studies carried out with 125Iodine-labelled Cry1Ea, demonstrated the presence of specific binding sites on the midgut brush border membrane vesicles (BBMV) of both insect species. Heterologous competition-binding experiment…

0106 biological sciences0301 basic medicineBrush borderlcsh:MedicineMoths01 natural sciencesArticleMicrobiologyApplied microbiology03 medical and health sciencesHemolysin ProteinsBacterial ProteinsChrysodeixis includensBacillus thuringiensisEnvironmental biotechnologyAnimalsCaterpillarlcsh:ScienceMultidisciplinaryBinding SitesbiologyBacillus thuringiensis ToxinsMicrovillifungilcsh:Rfood and beveragesMidgutbiology.organism_classificationEndotoxins010602 entomologyAnticarsia gemmatalis030104 developmental biologyCry1AcBiological Control AgentsLarvaBiological Assaylcsh:QPEST analysisSoybeansScientific Reports
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Role of Bacillus thuringiensis Cry1A toxins domains in the binding to the ABCC2 receptor from Spodoptera exigua

2018

Abstract Cry proteins from Bacillus thuringiensis (Bt) have been used to control insect pests either as formulated sprays or as in Bt-crops. However, field-evolved resistance to Bt proteins is threatening the long-term use of Bt products. The SeABCC2 locus has been genetically linked to resistance to a Bt bioinsecticide (Xentari™) in Spodoptera exigua (a mutation producing a truncated form of the transporter lacking an ATP binding domain was found in the resistant insects). Here, we investigated the role of SeABCC2 in the mode of action of Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ca, and two Cry1A-1Ca hybrids by expressing the receptor in Sf21 and HEK293T cell lines. Cell toxicity assays showed that Sf2…

0106 biological sciences0301 basic medicineCell SurvivalBacillus thuringiensisGene ExpressionSpodopteraSpodopteraTransfection01 natural sciencesBiochemistryHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesBacterial ProteinsProtein DomainsBacillus thuringiensisExiguaSf9 CellsAnimalsHumansProtein IsoformsBinding siteReceptorMolecular BiologySf21Binding SitesBacillus thuringiensis Toxinsbiologyfungibiology.organism_classificationMultidrug Resistance-Associated Protein 2Recombinant ProteinsClone CellsEndotoxins010602 entomologyHEK293 Cells030104 developmental biologyBiochemistryCry1AcLarvaInsect ScienceMutationInsect ProteinsMultidrug Resistance-Associated ProteinsPlasmidsProtein BindingBinding domainInsect Biochemistry and Molecular Biology
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Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

2016

The transglycosylation activity of amylosucrase (ASase) has received significant attention owing to its use of an inexpensive donor, sucrose, and broad acceptor specificity, including glycone and aglycone compounds. The transglycosylation reaction of recombinant ASase from Deinococcus radiopugnans (DRpAS) was investigated using various phenolic compounds, and quercetin-3-O-rutinoside (rutin) was found to be the most suitable acceptor molecule used by DRpAS. Two amino acid residues in DRpAS variants (DRpAS Q299K and DRpAS Q299R), assumed to be involved in acceptor binding, were constructed by site-directed mutagenesis. Intriguingly, DRpAS Q299K and DRpAS Q299R produced 10-fold and 4-fold hig…

0106 biological sciences0301 basic medicineGlycosylationGlycosylationStereochemistryRutinAmino Acid Motifs01 natural sciencesApplied Microbiology and BiotechnologySubstrate Specificity03 medical and health sciencesRutinchemistry.chemical_compoundAmylosucraseGlucosyltransferasesBacterial Proteins010608 biotechnologyDeinococcusBinding siteBinding SitesbiologyGeneral Medicinebiology.organism_classificationAcceptorMolecular Docking SimulationKinetics030104 developmental biologyAglyconechemistryGlucosyltransferasesbiology.proteinDeinococcusBiotechnologyJournal of Microbiology and Biotechnology
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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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Binding Site Alteration Is Responsible for Field-Isolated Resistance to Bacillus thuringiensis Cry2A Insecticidal Proteins in Two Helicoverpa Species

2010

Background Evolution of resistance by target pests is the main threat to the long-term efficacy of crops expressing Bacillus thuringiensis (Bt) insecticidal proteins. Cry2 proteins play a pivotal role in current Bt spray formulations and transgenic crops and they complement Cry1A proteins because of their different mode of action. Their presence is critical in the control of those lepidopteran species, such as Helicoverpa spp., which are not highly susceptible to Cry1A proteins. In Australia, a transgenic variety of cotton expressing Cry1Ac and Cry2Ab (Bollgard II) comprises at least 80% of the total cotton area. Prior to the widespread adoption of Bollgard II, the frequency of alleles conf…

0106 biological sciencesCrops AgriculturalInsecticidesHelicoverpa punctigeraScienceUNESCO::CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología generalBacillus thuringiensisBacterial ProteinGenetically modified cropsHelicoverpa armigera01 natural sciencesMicrobiologyLepidoptera genitaliaInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanyBacillus thuringiensiBiotechnology/Applied MicrobiologyAnimalsMode of actionBiotechnology/Plant BiotechnologyHelicoverpaInsecticide030304 developmental biology0303 health sciencesMultidisciplinaryBinding SitesbiologyAnimalQfungiBinding SiteRbiology.organism_classificationBinding site alterationHelicoverpa speciesLepidoptera010602 entomologyCry1AcBacillus thuringiensis; Binding site alteration; Helicoverpa speciesMedicine:CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología general [UNESCO]Plant Biology/Agricultural BiotechnologyResearch ArticleProtein BindingPLoS ONE
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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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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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Diversity, evolution, and function of myriapod hemocyanins.

2018

Background Hemocyanin transports O2 in the hemolymph of many arthropod species. Such respiratory proteins have long been considered unnecessary in Myriapoda. As a result, the presence of hemocyanin in Myriapoda has long been overlooked. We analyzed transcriptome and genome sequences from all major myriapod taxa – Chilopoda, Diplopoda, Symphyla, and Pauropoda – with the aim of identifying hemocyanin-like proteins. Results We investigated the genomes and transcriptomes of 56 myriapod species and identified 46 novel full-length hemocyanin subunit sequences in 20 species of Chilopoda, Diplopoda, and Symphyla, but not Pauropoda. We found in Cleidogona sp. (Diplopoda, Chordeumatida) a hemocyanin-…

0301 basic medicineArthropodaEvolutionmedicine.medical_treatmentMyriapodaZoologychemical and pharmacologic phenomenacomplex mixturesHemocyaninPauropodaEvolution Molecular03 medical and health sciencesHemolymphmedicineQH359-425AnimalsAmino Acid SequenceRNA MessengerArthropodsEcology Evolution Behavior and SystematicsPhylogenyBinding SitesbiologyBase SequenceMonophenol MonooxygenaseMyriapodaGenetic VariationHemocyaninhemic and immune systemsbiology.organism_classificationRespiratory proteinOxygenProtein Subunits030104 developmental biologyHemocyaninsPhenoloxidaseSubunit diversityArthropodSymphylaCentipedeCopperResearch ArticleBMC evolutionary biology
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