Search results for " binding"

showing 10 items of 1758 documents

The Histone Marks Signature in Exonic and Intronic Regions Is Relevant in Early Response of Tomato Genes to Botrytis cinerea and in miRNA Regulation

2020

Research into the relationship between epigenetic regulation and resistance to biotic stresses provides alternatives for plant protection and crop improvement. To unravel the mechanisms underlying tomato responses to Botrytis cinerea, we performed a chromatin immunoprecipitation (ChIP) analysis showing the increase in H3K9ac mark along the early induced genes SlyDES, SlyDOX1, and SlyLoxD encoding oxylipin-pathway enzymes, and SlyWRKY75 coding for a transcriptional regulator of hormonal signaling. This histone mark showed a more distinct distribution than the previously studied H3K4me3. The RNAPol-ChIP analysis reflected the actual gene transcription associated with increased histone modific…

0106 biological sciences0301 basic medicinePseudomonas syringaeMiRNA bindingPlant ScienceBiology<i>pseudomonas syringae</i>01 natural sciencesTomato03 medical and health sciencesBotrytis cinerealcsh:BotanyTomàquetsTranscriptional regulationEpigeneticsGeneEcology Evolution Behavior and SystematicsBotrytis cinereamiRNAGeneticsEcologyHistone modificationsfungifood and beveragesFongs patògensbiology.organism_classificationChromatin immunoprecipitationlcsh:QK1-989030104 developmental biologyHistone<i>botrytis cinerea</i>biology.proteinRNAH3K4me3EpigeneticsChromatin immunoprecipitation010606 plant biology & botany
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ß-COP mutants show specific high sensitivity to chloride ions.

2021

Coat Protein I (COPI) consists of a complex (coatomer) formed by seven subunits (α-, β-, β’-, γ-, δ-, ε-, and ζ-COP) that is recruited to Golgi membranes to form vesicles that shuttle from the Golgi apparatus to the ER and between Golgi stacks. Recently, it has been described that loss of function mutants of the two Arabidopsis β-COP genes, β1-COP and β2-COP, showed increased sensitivity to salt stress (NaCl). Using a mixture of either Na(+) or Cl(−) salts, we have now found that β-COP mutants are specifically and highly sensitive to chloride ions.

0106 biological sciences0301 basic medicineShort CommunicationMutantArabidopsisSalt (chemistry)Plant ScienceBiology01 natural sciencesChlorideCoatomer Protein03 medical and health sciencessymbols.namesakeChloridesArabidopsismedicinechemistry.chemical_classificationIonsVesicleCOPIGolgi apparatusbiology.organism_classificationhumanitiesProtein Subunits030104 developmental biologyPhenotypechemistryCoatomerMutationsymbolsBiophysics010606 plant biology & botanymedicine.drugProtein BindingPlant signalingbehavior
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The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.

2017

IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contra…

0106 biological sciences0301 basic medicineVesicle-associated membrane protein 8ChloroplastsLipid BilayersBiophysicsBiology01 natural sciencesBiochemistryMembrane FusionThylakoidsArticle03 medical and health sciencesBacterial ProteinsProtein DomainsIntegral membrane proteinMembranesMembrane transport proteinPeripheral membrane proteinSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembrane proteinMembrane biogenesisbiology.protein010606 plant biology & botanyMembrane Fusion ActivityProtein BindingBiochimica et biophysica acta. Bioenergetics
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Characterization of the Heme Pocket Structure and ligand binding kinetics of non-symbiotic hemoglobins from the model legume Lotus japonicus

2017

14 Pags.- 6 Figs. This article is part of the Research Topic: Advances in legume research ( http://journal.frontiersin.org/researchtopic/4288/advances-in-legume-research ). Copyright of the Authors through a Creative Commons Attribution License. This Document is Protected by copyright and was first published by Frontiers. All rights reserved. it is reproduced with permission.

0106 biological sciences0301 basic medicineligand bindingLotus japonicusMutantPlant Science01 natural sciencesheme cavity03 medical and health scienceschemistry.chemical_compoundnon-symbiotic hemoglobinsBiologyHemebiologyChemistryNitrosylationHexacoordinateNitric oxide dioxygenaseLigand (biochemistry)biology.organism_classificationAffinitiesChemistry030104 developmental biologyBiochemistryLotus japonicusnitric oxide dioxygenase010606 plant biology & botany
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2019

RNA interference (RNAi) is a powerful tool for studying functions of candidate genes in both model and nonmodel organisms and a promising technique for therapeutic applications. Successful application of this technique relies on the accuracy and reliability of methods used to quantify gene knockdown. With the limitation in the availability of antibodies for detecting proteins, quantitative PCR (qPCR) remains the preferred method for quantifying target gene knockdown after dsRNA treatment. We evaluated how qPCR primer binding site and target gene expression levels affect quantification of intact mRNA transcripts following dsRNA-mediated RNAi. The use of primer pairs targeting the mRNA sequen…

0106 biological sciences0303 health sciencesGene knockdownEcologyBiology010603 evolutionary biology01 natural sciencesCell biology03 medical and health sciencesRNA silencingRNA interferenceGene expressionGene silencingPrimer (molecular biology)Primer binding siteGeneEcology Evolution Behavior and Systematics030304 developmental biologyNature and Landscape ConservationEcology and Evolution
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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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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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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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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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