Search results for "Carmovirus"

showing 6 items of 6 documents

In vivo detection, RNA-binding properties and characterization of the RNA-binding domain of the p7 putative movement protein from carnation mottle ca…

1999

Biochemical and structural characterization studies on the p7 putative movement protein from a Spanish isolate of carnation mottle carmovirus (CarMV) have been conducted. The CarMV p7 gene was fused to a sequence coding for a six-histidine tag and expressed in bacteria, allowing the purification of CarMV p7 and the production of a specific antiserum. This antiserum led to the immunological identification of CarMV p7 in infected leaf tissue from the experimental host Chenopodium quinoa. Putative nucleic acid-binding properties of the CarMV p7 have been explored and demonstrated with both electrophoretic mobility shift and RNA-protein blot in vitro assays using digoxigenin-labeled riboprobes.…

Binding SitesCarmovirusRecombinant Fusion ProteinsMolecular Sequence DataCooperative bindingRNARNA-Binding ProteinsBiologybiology.organism_classificationMolecular biologyPlant Viral Movement ProteinsViral ProteinsBiochemistryVirologyNucleic acidEscherichia coliCarmovirusAmino Acid SequenceMovement proteinPeptide sequenceGeneBinding domainVirology
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Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
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Double-spanning Plant Viral Movement Protein Integration into the Endoplasmic Reticulum Membrane Is Signal Recognition Particle-dependent, Translocon…

2005

The current model for cell-to-cell movement of plant viruses holds that transport requires virus-encoded movement proteins that intimately associate with endoplasmic reticulum membranes. We have examined the early stages of the integration into endoplasmic reticulum membranes of a double-spanning viral movement protein using photocross-linking. We have discovered that this process is cotranslational and proceeds in a signal recognition particle-dependent manner. In addition, nascent chain photocross-linking to Sec61alpha and translocating chain-associated membrane protein reveal that viral membrane protein insertion takes place via the translocon, as with most eukaryotic membrane proteins, …

BioquímicaSec61Vesicle-associated membrane protein 8Receptors PeptideLipid BilayersReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumBiochemistryViral ProteinsMembranes (Biologia)Escherichia coliMolecular BiologySignal recognition particle receptorSignal recognition particleMembrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsMembrane ProteinsSTIM1Cell BiologyTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMutagenesisRNA ViralCarmovirusSignal Recognition ParticleSEC Translocation Channels
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Membrane insertion and topology of the p7B movement protein of Melon Necrotic Spot Virus (MNSV)

2007

AbstractCell-to-cell movement of the Melon Necrotic Spot Virus (MNSV) is controlled by two small proteins working in trans, an RNA-binding protein (p7A) and an integral membrane protein (p7B) separated by an amber stop codon. p7B contains a single hydrophobic region. Membrane integration of this region was observed when inserted into model proteins in the presence of microsomal membranes. Furthermore, we explored the topology and targeting mechanisms of full-length p7B. Here we present evidence that p7B integrates in vitro into the ER membrane cotranslationally and with an Nt-cytoplasmic/Ct-luminal orientation. The observed topology was monitored in vivo by fusing GFP to the Ct of p7B, enab…

Green Fluorescent ProteinsPlant virusBiologyTopologyEndoplasmic ReticulumGreen fluorescent proteinViral ProteinsVirologyMovement proteinIntegral membrane proteinMelon necrotic spot virusEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane Proteinsbiology.organism_classificationMembrane integrationMembrane protein topologyVirusPlant Viral Movement ProteinsMovement proteinsCucurbitaceaeMembraneMembrane proteinCarmovirusMNSVVirology
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RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins

2006

AbstractAdvances in structural and biochemical properties of carmovirus movement proteins (MPs) have only been obtained in p7 and p9 from Carnation mottle virus (CarMV). Alignment of carmovirus MPs revealed a low conservation of amino acid identity but interestingly, similarity was elevated in regions associated with the functional secondary structure elements reported for CarMV which were conserved in all studied proteins. Nevertheless, some differential features in relation with CarMV MPs were identified in those from Melon necrotic virus (MNSV) (p7A and p7B). p7A was a soluble non-sequence specific RNA-binding protein, but unlike CarMV p7, its central region alone could not account for t…

Molecular Sequence DataSequence alignmentBiologyMembranes (Biologia)VirologyAmino Acid SequencePeptide sequenceProtein secondary structureIntegral membrane proteinPlant DiseasesMelon necrotic spot virusCarmovirusProteïnes de membranaRNA-Binding ProteinsRNAbiology.organism_classificationRNA-binding domainVirusPlant Viral Movement ProteinsCucurbitaceaeMovement proteinsBiochemistryCarnation mottle virusMelon plantsCarmovirusMNSVMembrane insertionSequence AlignmentGene DeletionVirology
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Membrane Insertion and Biogenesis of the Turnip Crinkle Virus p9 Movement Protein

2010

ABSTRACT Plant viral infection and spread depends on the successful introduction of a virus into a cell of a compatible host, followed by replication and cell-to-cell transport. The movement proteins (MPs) p8 and p9 of Turnip crinkle virus are required for cell-to-cell movement of the virus. We have examined the membrane association of p9 and found that it is an integral membrane protein with a defined topology in the endoplasmic reticulum (ER) membrane. Furthermore, we have used a site-specific photo-cross-linking strategy to study the membrane integration of the protein at the initial stages of its biosynthetic process. This process is cotranslational and proceeds through the signal recog…

VirologiavirusesImmunologyEndoplasmic ReticulumMicrobiologyVirusMembranes (Biologia)VirologyMovement proteinIntegral membrane proteinSignal recognition particlebiologyTurnip crinkle virusEndoplasmic reticulumProteïnes de membranaMembrane Proteinsbiology.organism_classificationVirus-Cell InteractionsVirusCell biologyPlant Viral Movement ProteinsMembrane proteinBiochemistryInsect ScienceBiosynthetic processCarmovirusSignal Recognition ParticleJournal of Virology
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