Abstract
Plant viral movement proteins bind to RNA and participate in the intra- and intercellular movement of the RNAs from plant viruses. However, the role and magnitude of the conformational changes associated with the formation of RNA-protein complexes are not yet defined. Here we describe studies on the relevance of a preexisting nascent alpha-helix at the C terminus of the RNA-binding domain of p7, a movement protein from carnation mottle virus, to RNA binding. Synthetic peptide analogues and single amino acid mutation at the RNA-binding domain of recombinant p7 protein were used to correlate the transient structural order in aqueous solution with RNA-binding potential.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites / physiology
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Magnetic Resonance Spectroscopy
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Molecular Sequence Data
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Mutation
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Peptides / chemistry
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Peptides / metabolism
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Protein Structure, Tertiary / physiology
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RNA / metabolism*
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Spectrometry, Fluorescence
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Viral Proteins / chemistry*
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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P7 protein, Carnation mottle virus
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Peptides
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RNA-Binding Proteins
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Recombinant Proteins
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Viral Proteins
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RNA