Search results for "protein binding"

showing 10 items of 870 documents

The Greenland shark Somniosus microcephalus—Hemoglobins and ligand-binding properties

2017

A large amount of data is currently available on the adaptive mechanisms of polar bony fish hemoglobins, but structural information on those of cartilaginous species is scarce. This study presents the first characterisation of the hemoglobin system of one of the longest-living vertebrate species (392 +/- 120 years), the Arctic shark Somniosus microcephalus. Three major hemoglobins are found in its red blood cells and are made of two copies of the same a globin combined with two copies of three very similar beta subunits. The three hemoglobins show very similar oxygenation and carbonylation properties, which are unaffected by urea, a very important compound in marine elasmobranch physiology.…

---0301 basic medicinegenetic structuresProtein ConformationGreenlandlcsh:MedicineRESONANCE RAMAN-SPECTRAHETERODONTUS-PORTUSJACKSONISpectrum Analysis RamanBiochemistrychemistry.chemical_compoundHemoglobinsProtein structureAMINO-ACID SEQUENCEAnimal CellsSequence Analysis ProteinRed Blood CellsUreaNOTOTHENIOID FISHESPost-Translational Modificationlcsh:ScienceHemeChondrichthyesMultidisciplinarybiologyChemistryOrganic CompoundsChemical ReactionsVertebrateEukaryotaMOLECULAR ADAPTATIONSMicrocephalusGlobinsChemistryBiochemistryOptical EquipmentVertebratesPhysical SciencesEngineering and TechnologyCellular TypesResearch ArticleEnvironmental MonitoringProtein BindingQUATERNARY STRUCTURESAllosteric regulationEquipmentSTRETCHING FREQUENCIESHeme03 medical and health sciencesOXYGEN-BINDINGbiology.animalAnimals14. Life underwaterGlobinHemoglobinPhotolysisBlood Cells030102 biochemistry & molecular biologyLaserslcsh:ROrganic ChemistryOrganismsChemical CompoundsBiology and Life SciencesProteinsxxxCell Biologybiology.organism_classificationCARTILAGINOUS FISHOxygen030104 developmental biologySomniosusFishSharkslcsh:QHemoglobinProtein MultimerizationELASMOBRANCH HEMOGLOBINElasmobranchiiPLoS ONE
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MD Simulation Investigation on the Binding Process of Smoke-Derived Germination Stimulants to Its Receptor

2019

Karrikins (KARs) are a class of smoke-derived seed germination stimulants with great significance in both agriculture and plant biology. By means of direct binding to the receptor protein KAI2, the compounds can initiate the KAR signal transduction pathway, hence triggering germination of the dormant seeds in the soil. In the research, several molecular dynamics (MD) simulation techniques were properly integrated to investigate the binding process of KAR1 to KAI2 and reveal the details of the whole binding event. The calculated binding free energy, -7.00 kcal/mol, is in good agreement with the experimental measurement, -6.83 kcal/mol. The obtained PMF profile indicates the existence of thre…

010304 chemical physicsProtein ConformationChemistryGeneral Chemical EngineeringGerminationGeneral ChemistryPlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesLigand (biochemistry)01 natural sciences0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistryMolecular dynamicsProtein structure0103 physical sciencesMoleBiophysicsThermodynamicsMoleculeSignal transductionReceptorPlant ProteinsProtein BindingJournal of Chemical Information and Modeling
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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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The Odorant-Binding Proteins of the Spider Mite Tetranychus urticae

2021

Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in Tetranychus urticae. As in other species of Chelicerata, the four OBPs of T. urticae contain six conserved cysteines paired in a pattern (C1–C6, C2–C3, C4–C5) differing from that of insect counterparts (C1–C3, C2–C5, C4–C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to T. urticae. A three-dimensional model of TurtOBP1, built on the recent X-ray structure of Varroa destruc…

0106 biological sciences0301 basic medicineModels MolecularProteomicsProteomeOdorant bindingProtein ConformationInsectLigandsReceptors Odorant01 natural scienceschemistry.chemical_compoundTetranychus urticaeBiology (General)SpectroscopyPhylogenymedia_commonmass spectrometryGeneticsbiologyligand-bindingMolecular Structurespider mitesGeneral MedicineTetranychus urticaeComputer Science ApplicationsChemistryConiferyl aldehydedisulfide bridgesTetranychidaeProtein Bindingspider mites.QH301-705.5media_common.quotation_subjectodorant-binding proteinsCatalysisArticleInorganic Chemistry03 medical and health sciencesSpider mite<i>Tetranychus urticae</i>AnimalsAmino Acid SequencePhysical and Theoretical ChemistryQD1-999Molecular BiologySpiderOrganic Chemistrybiology.organism_classification010602 entomology030104 developmental biologychemistryVarroa destructorOdorantsChelicerataInternational Journal of Molecular Sciences
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Functional characterization of the chaperon-like protein Cdc48 in cryptogein-induced immune response in tobacco

2017

SPEIPMUBINRASUPDATDOCT; Cdc48, a molecular chaperone conserved in different kingdoms, is a member of the AAA+ family contributing to numerous processes in mammals including proteins quality control and degradation, vesicular trafficking, autophagy and immunity. The functions of Cdc48 plant orthologues are less understood. We previously reported that Cdc48 is regulated by S-nitrosylation in tobacco cells undergoing an immune response triggered by cryptogein, an elicitin produced by the oomycete Phytophthora cryptogea. Here, we inv estigated the function of NtCdc48 in cryptogein signalling and induced hypersensitive-like cell death. NtCdc48 was found to accumulate in elicited cells at both th…

0106 biological sciences0301 basic medicineProgrammed cell deathPhysiologyImmunoprecipitationNitrosation[SDV]Life Sciences [q-bio]PopulationPlant ScienceBiologyBioinformatics01 natural sciencesdefence responsescryptogeinFungal Proteins03 medical and health sciencesImmune systemGene Expression Regulation PlantValosin Containing ProteinPlant CellsTobaccoRNA MessengereducationPlant ProteinsRegulation of gene expressioneducation.field_of_studyFungal protein[ SDV ] Life Sciences [q-bio]AutophagyElicitinCell biology030104 developmental biologycell deathChromatography GelCdc48 partnersNtCdc48Protein Binding010606 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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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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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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