0000000000292299

AUTHOR

Frederic Aparicio

0000-0002-1586-9978

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The coat protein of prunus necrotic ringspot virus specifically binds to and regulates the conformation of its genomic RNA

2003

AbstractBinding of coat protein (CP) to the 3′ nontranslated region (3′-NTR) of viral RNAs is a crucial requirement to establish the infection of Alfamo- and Ilarviruses. In vitro binding properties of the Prunus necrotic ringspot ilarvirus (PNRSV) CP to the 3′-NTR of its genomic RNA using purified E. coli- expressed CP and different synthetic peptides corresponding to a 26-residue sequence near the N-terminus were investigated by electrophoretic mobility shift assays. PNRSV CP bound to, at least, three different sites existing on the 3′-NTR. Moreover, the N-terminal region between amino acid residues 25 to 50 of the protein could function as an independent RNA-binding domain. Single exchan…

Molecular Sequence DataElectrophoretic Mobility Shift AssayPlasma protein bindingBiologyIlarvirusProtein structureVirologyElectrophoretic mobility shift assayMagnesiumAmino Acid SequencePeptide sequence3' Untranslated RegionsIlarvirusBase SequenceCircular DichroismRNA ConformationRNAbiology.organism_classificationMolecular biologyProtein Structure TertiaryBiochemistryPrunus necrotic ringspot virusNucleic Acid ConformationRNA ViralCapsid ProteinsPrunusProtein BindingVirology
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