Search results for "Biotecnologia agrícola"

showing 9 items of 9 documents

The targeted overexpression of SlCDF4 in the fruit enhances tomato size and yield involving gibberellin signalling

2020

AbstractTomato is one of the most widely cultivated vegetable crops and a model for studying fruit biology. Although several genes involved in the traits of fruit quality, development and size have been identified, little is known about the regulatory genes controlling its growth. In this study, we characterized the role of the tomato SlCDF4 gene in fruit development, a cycling DOF-type transcription factor highly expressed in fruits. The targeted overexpression of SlCDF4 gene in the fruit induced an increased yield based on a higher amount of both water and dry matter accumulated in the fruits. Accordingly, transcript levels of genes involved in water transport and cell division and expans…

0106 biological sciences0301 basic medicineAgricultural geneticsCell divisionPlant molecular biologyMolecular biologyTranscriptional regulatory elementsPlant physiologyBiotecnologia agrícolalcsh:MedicineMolecular engineering in plantsPlantesBiology01 natural sciencesArticle03 medical and health sciencesSolanum lycopersicumPlant hormonesDry matterlcsh:ScienceGeneTranscription factorRegulator genePlant ProteinsMultidisciplinaryWater transportlcsh:RGenètica vegetalfood and beveragesGibberellinsUp-Regulation02.- Poner fin al hambre conseguir la seguridad alimentaria y una mejor nutrición y promover la agricultura sostenibleRepressor ProteinsHorticulturePlant BreedingGENETICA030104 developmental biologyFruitGibberellinlcsh:QPlant biotechnologyFISIOLOGIA VEGETALSink (computing)Plant sciences010606 plant biology & botanyBiotechnologySignal Transduction
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Identification and molecular characterization of the high-affinity copper transporters family in Solanum lycopersicum

2021

Copper (Cu) plays a key role as cofactor in the plant proteins participating in essential cellular processes, such as electron transport and free radical scavenging. Despite high-affinity Cu transporters (COPTs) being key participants in Cu homeostasis maintenance, very little is known about COPTs in tomato (Solanum lycopersicum) even though it is the most consumed fruit worldwide and this crop is susceptible to suboptimal Cu conditions. In this study, a six-member family of COPT (SlCOPT1-6) was identified and characterized. SlCOPTs have a conserved architecture consisting of three transmembrane domains and β-strains. However, the presence of essential methionine residues, a methionine-enri…

0106 biological sciencesATPaseBiotecnologia agrícolaMolecular ConformationGene ExpressionCOPT01 natural sciencesBiochemistryTomatoStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundCopper Transport ProteinsSolanum lycopersicumStructural BiologyGene expressionTomàquetsAmino Acid SequenceHeavy metal stressMolecular BiologyConserved SequencePhylogenyPlant Proteins030304 developmental biology0303 health sciencesMethioninebiologyChemistryfood and beveragesGeneral MedicinePeroxisomeYeastComplementationTransmembrane domainBiochemistryMultigene Familybiology.proteinCopper010606 plant biology & botanyCysteineInternational Journal of Biological Macromolecules
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Common receptor for Bacillus thuringiensis toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea and Spodoptera exigua

2005

ABSTRACT Binding studies using 125 I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera , Helicoverpa zea , and Spodoptera exigua . Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

Bacterial ToxinsBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaReceptors Cell SurfaceSpodopteraHelicoverpa armigeraSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyInvertebrate MicrobiologyAnimalsBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungibiology.organism_classificationEndotoxinsLepidopteraCry1AcInsect ProteinsNoctuidaeHelicoverpa zeaFood ScienceBiotechnology
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Specific binding  of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

2008

ABSTRACT For a long time, it has been assumed that the mode of action of Cry2A toxins was unique and different from that of other three-domain Cry toxins due to their apparent nonspecific and unsaturable binding to an unlimited number of receptors. However, based on the homology of the tertiary structure among three-domain Cry toxins, similar modes of action for all of them are expected. To confirm this hypothesis, binding assays were carried out with 125 I-labeled Cry2Ab. Saturation assays showed that Cry2Ab binds in a specific and saturable manner to brush border membrane vesicles (BBMVs) of Helicoverpa armigera . Homologous-competition assays with 125 I-Cry2Ab demonstrated that this toxi…

BioquímicaBrush borderBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaPlasma protein bindingHelicoverpa armigeraApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteHelicoverpaBacillus thuringiensis ToxinsStaining and LabelingEcologybiologyfungiMidgutbiology.organism_classificationEndotoxinsGastrointestinal TractLepidopteraKineticsBiochemistryHelicoverpa zeaProteïnesProtein BindingFood ScienceBiotechnology
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Lack of Cry1Fa binding to the midgut brush border membrane in a resistant colony of Plutella xylostella moths with a mutaton in the ABCC2 locus

2012

ABSTRACT Previous studies reported “mode 1” Bacillus thuringiensis resistance in a colony of diamondback moths (NO-QA), and recently, this resistance has been mapped to an ABC transporter ( ABCC2 ) locus. We report the lack of binding of Cry1Fa to insects derived from this colony and compare our data with those from other insects with ABCC2 -associated resistance.

BioquímicaBrush borderBiotecnologia agrícolaDrug ResistanceResistència als plaguicidesLocus (genetics)ATP-binding cassette transporterDrug resistanceApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsPlagues ControlBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsGeneticsBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiPlutellaMidgutbiology.organism_classificationMultidrug Resistance-Associated Protein 2EndotoxinsLepidopteraMutationMultidrug Resistance-Associated ProteinsProtein BindingFood ScienceBiotechnology
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Interaction of Bacillus thuringiensis Cry1 and Vip3A Proteins with Spodoptera frugiperda Midgut Binding Sites

2009

ABSTRACT Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.

Bioquímicaanimal structuresBiotecnologia agrícolaBacillus thuringiensisPlasma protein bindingSpodopteraSpodopteraHemolysin ProteinsApplied Microbiology and BiotechnologyProtein–protein interactionMicrobiologyLethal Dose 50Hemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesMidgutbiology.organism_classificationBacillalesEndotoxinsGastrointestinal TractBiochemistryLarvasense organsProteïnesProtein BindingFood ScienceBiotechnologyApplied and Environmental Microbiology
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Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
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Vip3C, a novel class of vegetative insectidal proteins from Bacillus thuringiensis

2012

Three vip3 genes were identified in two Bacillus thuringiensis Spanish collections. Sequence analysis revealed a novel Vip3 protein class (Vip3C). Preliminary bioassays of larvae from 10 different lepidopteran species indicated that Vip3Ca3 caused more than 70% mortality in four species after 10 days at 4 οg/cm 2. © 2012, American Society for Microbiology.

DNA BacterialBioquímicaSequence analysisMolecular Sequence DataBiotecnologia agrícolaBacillus thuringiensisBiologyApplied Microbiology and BiotechnologyLepidoptera genitaliaBacterial proteinPlagues ControlBacterial ProteinsPhylogeneticsBacillus thuringiensisBotanyPlaguicidesInvertebrate MicrobiologyAnimalsBioassayGenePhylogenyLarvaSequence Homology Amino AcidEcologyfungiSequence Analysis DNAbiology.organism_classificationSurvival AnalysisVip3 genesLepidopteraSpainLarvaProteïnesFood ScienceBiotechnology
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