title: Transient structural ordering of the RNA-binding domain of carnation mottle virus p7 movement protein modulates nucleic acid binding.
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.
authors: Departament de Bioquímica i Biologia Molecular, Universitat de València, 46100 Burjassot, Spain.
authors: Marçal
authors: M
authors: Vilar
authors: Ana
authors: A
authors: Saurí
authors: Jose F
authors: JF
authors: Marcos
authors: Ismael
authors: I
authors: Mingarro
authors: Enrique
authors: E
authors: Pérez-Payá
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: C429546:P7 protein, Carnation mottle virus; D010455:Peptides; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D014764:Viral Proteins; D012313:RNA