Search results for "Coat protein"

showing 10 items of 16 documents

Loss of

2020

The early secretory pathway involves bidirectional transport between the endoplasmic reticulum (ER) and the Golgi apparatus and is mediated by coat protein complex I (COPI)-coated and coat protein complex II (COPII)-coated vesicles. COPII vesicles are involved in ER to Golgi transport meanwhile COPI vesicles mediate intra-Golgi transport and retrograde transport from the Golgi apparatus to the ER. The key component of COPI vesicles is the coatomer complex, that is composed of seven subunits (α/β/β'/γ/δ/ε/ζ). In Arabidopsis two genes coding for the β-COP subunit have been identified, which are the result of recent tandem duplication. Here we have used a loss-of-function approach to study the…

0106 biological sciences0301 basic medicineProtein subunitArabidopsisPlant Sciencelcsh:Plant culture01 natural sciences03 medical and health sciencessymbols.namesakelcsh:SB1-1110coat protein II (COPII)Plantes Cèl·lules i teixitsCOPIICreixement (Plantes)Secretory pathwayOriginal Researchsalt stressChemistryEndoplasmic reticulumVesiclecoat protein I (COPI)plant growthCOPIGolgi apparatusCell biology030104 developmental biologyCoatomerβ-COPGolgi apparatussymbols010606 plant biology & botanyFrontiers in plant science
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Phylogeography and Molecular Evolution of Potato virus Y

2012

Potato virus Y (PVY) is an important plant pathogen, whose host range includes economically important crops such as potato, tobacco, tomato, and pepper. PVY presents three main strains (PVYO, PVYN and PVYC) and several recombinant forms. PVY has a worldwide distribution, yet the mechanisms that promote and maintain its population structure and genetic diversity are still unclear. In this study, we used a pool of 77 complete PVY genomes from isolates collected worldwide. After removing the effect of recombination in our data set, we used Bayesian techniques to study the influence of geography and host species in both PVY population structure and dynamics. We have also performed selection and…

0106 biological sciencesEvolutionary GeneticsAmino-acid sitesSelective constraintsPotyviruslcsh:Medicine01 natural sciencesAmino-Acid SitesRecombinant strainPlant RNA virusesNegative selectionMaximum-Likelihoodlcsh:Sciencepathologie végétaleSelective ConstraintsPhylogenyGenetics0303 health sciencesCoat proteinMultidisciplinaryNatural selectionVegetal BiologybiologyEcologyGenetic-structurePotyvirusfood and beveragesEuropePhylogeneticsVenous necrosisPhylogeographyPotato virus YBiogeographyVenous NecrosisSequence AnalysisResearch ArticlePlant RNA VirusesGenome ViralMicrobiologyEvolution Molecular03 medical and health sciencesGenetic-StructureMolecular evolutionVirologyMosaic-virus[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyEvolutionary SystematicsBiology030304 developmental biologySolanum tuberosumGenetic diversityEvolutionary BiologyMosaic virusHost (biology)Maximum-likelihoodlcsh:RComputational Biologyvirus à de la pomme de terreBayes Theoremlégumebiology.organism_classificationMutational analysisMosaic-VirusMutational AnalysisEvolutionary EcologyRecombinant StrainNorth Americalcsh:QBiologie végétalePopulation Genetics010606 plant biology & botany
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Abstracts of presentations on plant protection issues at the fifth international Mango Symposium Abstracts of presentations on plant protection issue…

1997

0106 biological sciencesZucchini yellow mosaic virusBarley stripe mosaic virusbiologyEcology (disciplines)Plant ScienceCoat proteinbiology.organism_classification01 natural sciencesCucumber mosaic virus010602 entomologyInsect ScienceInternational congressBotany010606 plant biology & botanyPhytoparasitica
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Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

2016

We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in …

0301 basic medicineModels MolecularRNA bacteriophageViral proteinCryo-electron microscopyProtein Conformation010402 general chemistrymedicine.disease_causeCrystallography X-Ray01 natural sciencesvirus-like particleBacteriophage03 medical and health sciencesStructural Biology[CHIM.ANAL]Chemical Sciences/Analytical chemistryLeviviridaemedicineRNA VirusesBacteriophages[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyProtein secondary structurebiologyCryoelectron MicroscopyRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologycircular permutationRNA PhagesCircular permutation in proteinsbiology.organism_classification3. Good health0104 chemical sciencesCrystallography030104 developmental biologycoat proteinBiophysicsLeviviridaeCapsid ProteinsJournal of molecular biology
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alpha 2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth

2017

[EN] COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the endoplasmic reticulum. These vesicles form through the action of the small GTPase ADP-ribosylation factor 1 (ARF1) and the COPI heptameric protein complex (coatomer), which consists of seven subunits (alpha-, beta-, beta' -, gamma-, delta-, epsilon- and xi-COP). In contrast to mammals and yeast, several isoforms for coatomer subunits, with the exception of gamma and delta, have been identified in Arabidopsis. To understand the role of COPI proteins in plant biology, we have identified and characterized a loss-of-function mutant of alpha 2-COP, an Arabidopsis alpha-COP isofo…

0301 basic medicineα2-COPPhysiologyUbiquitin-Protein LigasesProtein subunitMutantSEC31ArabidopsisPlant ScienceEndoplasmic ReticulumCoatomer ProteinP24 family protein03 medical and health sciencessymbols.namesakeBotanyBIOQUIMICA Y BIOLOGIA MOLECULARCOPIICOPIISecretory pathwayCOPICoat proteinArabidopsis ProteinsChemistryEndoplasmic reticulumAlpha 2-COPBiological TransportCOPIGolgi apparatusSEC31.Cell biologyAlpha 1-COPα1-COP030104 developmental biologyCoatomerGolgi apparatussymbolsCOPII Golgi apparatusResearch Paper
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Mosaic Qβ coats as a new presentation model

1998

The new protein carrier was developed on the basis of recombinant RNA phage Qbeta capsid. C-terminal UGA extension of the short form of Qbeta coat, so-called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qbeta particles. In conditions of enhanced UGA suppression, the proportion of A1-extended to short coats in mosaic particles dropped from 48% to 14%, with an increase of the length of A1 extension. A model insertion, short preS1 epitope 31-DPAFR-35 of hepatitis B surface antigen, demonstrated superficial location on the mosaic Qbeta particles and ensured specific antigenicity and immunogenicity.

AntigenicityRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHepatitis b surface antigenBiochemistryEpitopelaw.inventionCapsid assemblyMiceCapsidPhage QβPeptide LibraryStructural BiologylawGeneticsAnimalsHepatitis B virus preS1Cloning MolecularMolecular BiologyAllolevivirusMice Inbred BALB CCoat protein UGA suppressionVirus AssemblyImmunogenicityA1 extensionRNACell BiologyImmunogenicityVirologyMolecular biologyCapsidCarrier proteinCodon TerminatorRecombinant DNACapsid ProteinsFEBS Letters
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Experimental virus evolution reveals a role of plant microtubule dynamics and TORTIFOLIA1/SPIRAL2 in RNA trafficking.

2014

1 tabla y 2 figuras

ArabidopsisPlant ScienceMicrotubulesRNA Transport//purl.org/becyt/ford/1 [https]INFECTIONTobacco mosaic virusTOBACCO-MOSAIC-VIRUSMovement proteinCytoskeletonCytoskeletonGeneticsCoat proteinMultidisciplinaryTRANSGENIC PLANTSQREXPERIMENTAL EVOLUTIONARABIDOPSISBiological Evolution3. Good healthCell biologyMacromolecular assemblyTobacco Mosaic VirusMICROTUBULESMedical MicrobiologyTobamovirusesViral Pathogensdynamic plasticityHost-Pathogen InteractionsMedicineTobacco mosaic viruscortical microtubuleCellular Structures and OrganellesCortical microtubuleARABIDOPSIS CORTICAL MICROTUBULESCell wallsMicrotubule-Associated ProteinsCIENCIAS NATURALES Y EXACTASResearch ArticleEvolutionary ProcessesSciencePlant Cell BiologyPlant PathogensORGANIZATIONBiologyMicrobiologyPlant Viral PathogensCiencias BiológicasMOVEMENT PROTEINComplexesMicrotubuleEvolutionary Adaptation//purl.org/becyt/ford/1.6 [https]Microbial PathogensPlant DiseasesEvolutionary BiologyArabidopsis ProteinsBotánicaRNABiology and Life SciencesCell BiologyPlant PathologyTMVCytoplasmMutationRNAVirologíaHELICAL GROWTHPloS one
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Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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Transmissibility of Broad bean wilt virus 1 by aphids: influence of virus accumulation in plants, virus genotype and aphid species

2013

Broad bean wilt virus 1 (BBWV-1) is transmitted by several aphid species in a non-persistent manner. Transmission efficiency by vectors is a key factor for understanding virus epidemiology and applying disease control measures based on limiting virus spread. We evaluated the transmission rates of two genetically divergent BBWV-1 isolates (PV-132 from USA and Ben from Spain) infecting broad bean (Vicia faba L.) by isofemale lines of nine aphid species from eight different genera collected in Spain. Our analyses showed that: (a) the virus concentration in the source plant was a key factor in BBWV-1 transmissibility; (b) The Spanish isolate Ben was transmitted more efficiently than the America…

Fabavirucoat protein sequence.Secoviridaefood and beveragesvirus titreSettore AGR/12 - Patologia VegetalePlant viruvectorBBWV-1
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Retention mechanisms for ER and Golgi membrane proteins

2014

Unless there are mechanisms to selectively retain membrane proteins in the endoplasmic reticulum (ER) or in the Golgi apparatus, they automatically proceed downstream to the plasma or vacuole membranes. Two types of coat protein complex I (COPI)-interacting motifs in the cytosolic tails of membrane proteins seem to facilitate membrane retention in the early secretory pathway of plants: a dilysine (KKXX) motif (which is typical of p24 proteins) for the ER and a KXE/D motif (which occurs in the Arabidopsis endomembrane protein EMP12) for the Golgi apparatus. The KXE/D motif is highly conserved in all eukaryotic EMPs and is additionally present in hundreds of other proteins of unknown subcellu…

Golgi membraneSecretory PathwayKKXXMolecular Sequence DataGolgi ApparatusMembrane ProteinsGolgi TargetingPlant ScienceCOPIGolgi apparatusBiologyEndoplasmic ReticulumCoat Protein Complex ICell biologysymbols.namesakeMembrane proteinPlant CellssymbolsAmino Acid SequenceIntegral membrane proteinSecretory pathwayTrends in Plant Science
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