Search results for "BIMOLECULAR FLUORESCENCE COMPLEMENTATION"

showing 10 items of 12 documents

Molecular signatures of silencing suppression degeneracy from a complex RNA virus

2021

As genomic architectures become more complex, they begin to accumulate degenerate and redundant elements. However, analyses of the molecular mechanisms underlying these genetic architecture features remain scarce, especially in compact but sufficiently complex genomes. In the present study, we followed a proteomic approach together with a computational network analysis to reveal molecular signatures of protein function degeneracy from a plant virus (as virus-host protein-protein interactions). We employed affinity purification coupled to mass spectrometry to detect several host factors interacting with two proteins of Citrus tristeza virus (p20 and p25) that are known to function as RNA sil…

0106 biological sciences0301 basic medicineProteomicsCitrusInteraction NetworksPathogenesisPlant Sciencemedicine.disease_causePathology and Laboratory Medicine01 natural sciencesInteractomeBiochemistryBimolecular fluorescence complementationRNA interferenceRNA silencing supressorsCitrus tristeza virusMedicine and Health SciencesDegeneracy (biology)Protein Interaction MapsBiology (General)H20 Plant diseasesPlant ProteinsEcologybiologyPlant virusesEukaryotaArgonautePlantsSmall interfering RNANucleic acidsRNA silencingComputational Theory and MathematicsGenetic interferenceExperimental Organism SystemsModeling and SimulationProteomeArgonaute ProteinsHost-Pathogen InteractionsRNA ViralEpigeneticsResearch ArticleClosterovirusRNA virusViral proteinQH301-705.5Arabidopsis ThalianaPlant PathogensComputational biologyGenome ViralBrassicaResearch and Analysis MethodsModels BiologicalPlant Viral Pathogens03 medical and health sciencesCellular and Molecular NeuroscienceViral ProteinsModel OrganismsPlant and Algal ModelsTobaccomedicineGeneticsGenomesNon-coding RNAProtein InteractionsMolecular signaturesMolecular BiologyEcology Evolution Behavior and SystematicsPlant DiseasesHost Microbial InteractionsBiology and life sciencesMass spectrometryOrganismsComputational BiologyProteinsRNA virusPlant Pathologybiology.organism_classificationGene regulationRepressor Proteins030104 developmental biologyU30 Research methodsAnimal StudiesRNAGene expression010606 plant biology & botanyF30 Plant genetics and breeding
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Thioredoxin (Trxo1) interacts with proliferating cell nuclear antigen (PCNA) and its overexpression affects the growth of tobacco cell culture.

2017

Thioredoxins (Trxs), key components of cellular redox regulation, act by controlling the redox status of many target proteins, and have been shown to play an essential role in cell survival and growth. The presence of a Trx system in the nucleus has received little attention in plants, and the nuclear targets of plant Trxs have not been conclusively identified. Thus, very little is known about the function of Trxs in this cellular compartment. Previously, we studied the intracellular localization of PsTrxo1 and confirmed its presence in mitochondria and, interestingly, in the nucleus under standard growth conditions. In investigating the nuclear function of PsTrxo1 we identified proliferati…

0106 biological sciences0301 basic medicineTFs transcription factorsOverexpressionBiologíaBiFC bimolecular fluorescence complementationClinical BiochemistryCell Culture TechniquesTobacco BY-2 cells01 natural sciencesBiochemistryTBY-2 tobacco bright yellow-2DTT 14-dithiothreitolBimolecular fluorescence complementationThioredoxinsGene Expression Regulation PlantTrx thioredoxinlcsh:QH301-705.5GFP green fluorescent proteinlcsh:R5-920biologyProliferating cell nuclear antigen (PCNA)Cell cycleGlutathione3. Good healthCell biologyMitochondriaNTR NADPH thioredoxin reductaseProtein TransportDEM diethyl maleateRT-qPCR Reverse transcription quantitative polymerase chain reactionThioredoxinlcsh:Medicine (General)Oxidation-ReductionAMS 4-acetamido-4-maleimidylstilbene-22-disulfonic acidResearch PaperPCNA proliferating cell nuclear antigenOex overexpressingCell cycleNucleusThioredoxin o103 medical and health sciencesROS reactive oxygen speciesDownregulation and upregulationProliferating Cell Nuclear AntigenTobaccoDAPI 46-diamidine-2-phenylindolmCBM monochlorobimaneCellular compartmentCell NucleusCell growthOrganic ChemistryBotánicaPeasMolecular biologyYFP yellow fluorescent proteinProliferating cell nuclear antigenTBS Tris-buffered salineOD optical density030104 developmental biologylcsh:Biology (General)Cell cultureRNA reactive nitrogen speciesbiology.proteinPrx peroxiredoxinBSA bovine serum albumin010606 plant biology & botanyRedox biology
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The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor

2021

Mesencephalic astrocyte-derived neurotrophic factor (MANF) is an endoplasmic reticulum (ER)-stress-regulated protein exhibiting cytoprotective properties through a poorly understood mechanism in various in vitro and in vivo models of neuronal and non-neuronal damage. Although initially characterized as a secreted neurotrophic factor for midbrain dopamine neurons, MANF has recently gained more interest for its intracellular role in regulating the ER homeostasis, including serving as a cofactor of the chaperone glucose-regulated protein 78 (GRP78). We aimed for a better understanding of the neuroprotective mechanisms of MANF. Here we show for the first time that MANF promotes the survival of …

0301 basic medicineBiFC bimolecular fluorescence complementationMST microscale thermophoresisPDIA1 protein disulfide isomerase family A member 1ApoptosisNEUROTROPHIC FACTOR MANFEndoplasmic ReticulumBiochemistryprotein-protein interactionMiceBimolecular fluorescence complementationUPR unfolded protein responseENDOPLASMIC-RETICULUM STRESSMesencephalonNeurotrophic factorsInsulin-Secreting CellsProtein Interaction MappingBINDINGCOMPREHENSIVE RESOURCEATF6unfolded protein response (UPR)PDIA6 protein disulfide isomerase family A member 6PPIs protein-protein interactionsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsNPTN neuroplastinbiologyChemistryapoptosisunfolded protein responsedopamine neurons3. Good healthCell biologyGDNF glial cell line–derived neurotrophic factorIRE1-ALPHASBD substrate-binding domainendoplasmic reticulum stressMANF mesencephalic astrocyte-derived neurotrophic factorTm tunicamycinneuroprotectionResearch ArticleProtein BindingSignal TransductionGRP78Protein Disulfide-Isomerase FamilyCell SurvivalTH tyrosine hydroxylasePrimary Cell CultureSCG superior cervical ganglionProtein Disulfide-IsomerasesIRE1 inositol-requiring enzyme 1ER-STRESSER endoplasmic reticulum03 medical and health sciencesohjelmoitunut solukuolemaC-MANF C-terminal domain of MANFCSPs chemical shift perturbationsAnimalsHumansHSP70 Heat-Shock ProteinsNerve Growth FactorsNBD nucleotide-binding domainNMR nuclear magnetic resonanceMolecular Biology030102 biochemistry & molecular biologyBIPATF6Dopaminergic NeuronsGene Expression ProfilingBinding proteinneuronal cell deathDISSOCIATIONCell BiologyNEI nucleotide exchange inhibitorEmbryo MammalianadenosiinitrifosfaattiATPhermosolutmesencephalic astrocyte-derived neurotrophic factorprotein–protein interactionPERK protein kinase RNA-like ER kinaseHEK293 Cells030104 developmental biologyGene Expression RegulationChaperone (protein)Tg thapsigarginbiology.proteinUnfolded protein responseAP-MS affinity purification mass spectrometry1182 Biochemistry cell and molecular biologyGFP-SH SH-tagged GFPendoplasmic reticulum stress (ER stress)DA dopaminemesencephalic astrocyte-derived neurotrophic factor (MANF)proteiinitNeuroplastin
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Role of pulmonary surfactant protein Sp-C dimerization on membrane fragmentation: An emergent mechanism involved in lung defense and homeostasis.

2020

Surfactant protein C (SP-C) is a protein present in the pulmonary surfactant system that is involved in the biophysical properties of this lipoprotein complex, but it also has a role in lung defense and homeostasis. In this article, we propose that the link between both functions could rely on the ability of SP-C to induce fragmentation of phospholipid membranes and generate small vesicles that serve as support to present different ligands to cells in the lungs. Our results using bimolecular fluorescence complementation and tunable resistive pulse sensing setups suggest that SP-C oligomerization could be the triggering event that causes membrane budding and nanovesiculation. As shown by flu…

0301 basic medicineBiophysicsBiochemistryCell Line03 medical and health sciencesBimolecular fluorescence complementation0302 clinical medicinePulmonary surfactantProtein DomainsHumansAmino Acid SequenceFragmentation (cell biology)Unilamellar LiposomesChemistryVesicleSurfactant protein CCell BiologyMembrane buddingFlow CytometryPulmonary Surfactant-Associated Protein CEndocytosisRecombinant ProteinsCell biology030104 developmental biology030228 respiratory systemMembrane proteinStructural biologyMicroscopy FluorescencePeptidomimeticsProtein MultimerizationDimerizationBiochimica et biophysica acta. Biomembranes
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Confocal microscopy of single molecules of the green fluorescent protein

1998

Single molecule detection has been extended into life sciences by use of strongly fluorescent labels. The green fluorescent protein (GFP) as a self-fluorescent biomolecule has attracted considerable attention. Here, single molecules of the GFP-mutant Glu222Gln are immobilized in a polyvinylalcohol matrix and detected by confocal fluorescence microscopy. Although this mutant stabilizes one of both conformers of the wild-type GFP, the investigation of its fluorescence dynamics reveals strong signal fluctuations. This fluorescence behaviour is—at least partly—caused by reversible photochemical changes of the protein framework, that can relax into the fluorescent state on different timescales. …

ChemistryConfocalBiophysicsFluorescence in the life sciencesFluorescencelaw.inventionGreen fluorescent proteinCell biologyBimolecular fluorescence complementationConfocal microscopylawFluorescence microscopeBiophysicsRadiology Nuclear Medicine and imagingPhotoactivated localization microscopyBioimaging
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Inhibitory activities of short linear motifs underlie Hox interactome specificity in vivo

2015

Hox proteins are well-established developmental regulators that coordinate cell fate and morphogenesis throughout embryogenesis. In contrast, our knowledge of their specific molecular modes of action is limited to the interaction with few cofactors. Here, we show that Hox proteins are able to interact with a wide range of transcription factors in the live Drosophila embryo. In this context, specificity relies on a versatile usage of conserved short linear motifs (SLiMs), which, surprisingly, often restrains the interaction potential of Hox proteins. This novel buffering activity of SLiMs was observed in different tissues and found in Hox proteins from cnidarian to mouse species. Although th…

Embryo Nonmammalian[SDV]Life Sciences [q-bio]Amino Acid MotifsinteractomeInteractomeBimolecular fluorescence complementationMiceTARGET GENEDrosophila ProteinsCELL REGULATIONProtein Interaction MapsBiology (General)Hox genetranscription factorGeneticsD. melanogasterGeneral NeuroscienceQRINTERACTION MODULESGeneral MedicineREGIONSHoxTRANSCRIPTION FACTORSDrosophila melanogasterGenomics and Evolutionary BiologyOrgan Specificityembryonic structuresMedicineOligopeptidesProtein BindingResearch Articleanimal structuresQH301-705.5ScienceembryoContext (language use)Computational biology[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCell fate determinationBiologyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyFluorescenceProtein–protein interactionEvolution MolecularStructure-Activity Relationship[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsShort linear motif[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBiFCTranscription factor[SDV.BC] Life Sciences [q-bio]/Cellular BiologydevelopmentHomeodomain ProteinsABDOMINAL-AGeneral Immunology and MicrobiologyBIMOLECULAR FLUORESCENCE COMPLEMENTATIONREPRESSIONDNAPROTEIN INTERACTIONSIntrinsically Disordered ProteinsDROSOPHILA-MELANOGASTERMutationeLife
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Spectroscopic Methods for the Determination of Protein Interactions

2005

This unit provides guidelines on how to use steady-state fluorescence spectroscopy for the quantification of protein-protein interactions. The fluorescence of a protein is characterized by its excitation and emission spectra, quantum yield, and anisotropy. These parameters can change upon interaction with another protein and can be used to measure the extent of complex formation. The source of fluorescence can be an intrinsic fluorophore, such as tryptophan or tyrosine; a covalently attached fluorescent dye; or a fluorescent binding partner, such as a nucleotide or cofactor, that interacts specifically with the complex. Protocols are provided in this unit for determining affinity constants …

FluorophoreChemistryProteinsfood and beveragesQuantum yieldFluorescence in the life sciencesBiochemistryFluorescenceFluorescence spectroscopyProtein–protein interactionchemistry.chemical_compoundBimolecular fluorescence complementationCrystallographySpectrometry FluorescenceStructural BiologyBiophysicsTitrationProtein BindingCurrent Protocols in Protein Science
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A Protein-Interaction Array Inside a Living Cell

2013

Cell phenotype is determined by protein network states that are maintained by the dynamics of multiple protein interactions.1 Fluorescence microscopy approaches that measure protein interactions in individual cells, such as by Forster resonant energy transfer (FRET), are limited by the spectral separation of fluorophores and thus are most suitable to analyze a single protein interaction in a given cell. However, analysis of correlations between multiple protein interactions is required to uncover the interdependence of protein reactions in dynamic signal networks. Available protein-array technologies enable the parallel analysis of interacting proteins from cell extracts, however, they can …

ImmunoprecipitationRecombinant Fusion Proteinsprotein-protein interactionsImmobilized Nucleic AcidsProtein Array AnalysisreceptorsDNA Single-StrandedCatalysisProtein–protein interactionReceptors G-Protein-CoupledBimolecular fluorescence complementationProtein Array AnalysisChlorocebus aethiopsFluorescence microscopeFluorescence Resonance Energy TransferAnimalsProtein Interaction MapsProtein kinase Amultiplexed assayChemistryProteinsProtein-protein interactions Dip Pen Nanolithography Protein KinaseDNA directed immobilizationGeneral MedicineGeneral ChemistryCommunicationssurface-immobilizationKineticsLuminescent ProteinsFörster resonance energy transferBiochemistryMicroscopy FluorescenceCOS CellsBiophysicsSignal transductionAntibodies Immobilizedsignal transduction
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Aminopropyltransferases involved in polyamine biosynthesis localize preferentially in the nucleus of plant cells

2012

Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the…

Macromolecular AssembliesProteomicsS-AdenosylmethioninePlant anatomyImmunohistoquímicaArabidopsislcsh:MedicineSecondary MetabolismSpermineExpressionPlant ScienceSpermidine synthaseBiochemistrychemistry.chemical_compoundBimolecular fluorescence complementationCytosolMolecular Cell BiologyPolyaminesPlant Genomicslcsh:SciencePlant Growth and DevelopmentMultidisciplinarybiologyPlant BiochemistryArabidopsis-ThalianaGenomicsImmunohistochemistryMetabolismeFunctional GenomicsBiochemistrySpermine synthasePlant proteinPlant PhysiologyMechanismResearch ArticleHistologyAcyltransferasePlant Cell BiologyActive Transport Cell NucleusSpermidine SynthaseBimolecular fluorescence complementationProtein InteractionsBiologyCell NucleusCrystal-Structurelcsh:RHistologiaBotanyProtein interactionsSubcellular localizationAnatomia vegetalExpressió gènicaMolecular WeightSpermidineMetabolismchemistryDecarboxylasebiology.proteinPutrescineBotànicalcsh:QGene expressionSpermidine synthase
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Molecular and structural characterization of fluorescent human parvovirus B19 virus-like particles

2005

Although sharing a T = 1 icosahedral symmetry with other members of the Parvoviridae family, it has been suggested that the fivefold channel of the human parvovirus B19 VP2 capsids is closed at its outside end. To investigate the possibility of placing a relatively large protein moiety at this site of B19, fluorescent virus-like particles (fVLPs) of B19 were developed. The enhanced green fluorescent protein (EGFP) was inserted at the N-terminus of the structural protein VP2 and assembly of fVLPs from this fusion protein was obtained. Electron microscopy revealed that these fluorescent protein complexes were very similar in size when compared to wild-type B19 virus. Further, fluorescence cor…

Models MolecularImmunoprecipitationRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsFluorescence correlation spectroscopyEndosomesSpodopteraBiologyMicroscopy Atomic ForceBiochemistryFluorescenceCell LineGreen fluorescent proteinParvoviridae InfectionsBimolecular fluorescence complementationCell Line Tumorhemic and lymphatic diseasesParvovirus B19 HumanAnimalsHumansImmunoprecipitationMolecular BiologyParvoviridaeImmune SeraVirus AssemblyVirionvirus diseasesCell Biologybiology.organism_classificationFusion proteinMolecular biologyNanostructuresCell biologyTransport proteinProtein TransportCapsidCapsid Proteins
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