Key result
Recombinant P1 protein of turnip mosaic potyvirus interacted with RNA, bound ssRNA, ssDNA, and dsRNA with similar affinity, but was not able to bind to dsDNA.
The P1 protein of turnip mosaic potyvirus demonstrates broad nucleic acid-binding capabilities, interacting with ssRNA, ssDNA, and dsRNA, but not dsDNA.
No immediate cardiology implications; leaves open relevance of potyvirus P1 to human viral research.
The N-terminal P1 protein of turnip mosaic potyvirus (TuMV) polyprotein was overexpressed in Escherichia coli, purified by metal chelation chromatography under denaturing conditions and renatured. U.v. cross-linking experiments indicated that the recombinant protein interacted with RNA, and gel retardation electrophoresis demonstrated that more than one molecule of P1 bound one molecule of RNA. Formation of the protein-RNA complexes was dependent on the conformational state of P1 and was stable at relatively high concentrations of NaCl. P1 had the ability to bind ssRNA and ssDNA, with similar affinity, but was not able to bind to dsDNA. The TuMV protein had the additional characteristic of binding dsRNA with affinity similar to that observed with single-stranded nucleic acids.
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Soumounou et al. (1994) studied this question. Recombinant P1 protein of turnip mosaic potyvirus was evaluated on Nucleic acid-binding properties. Recombinant P1 protein of turnip mosaic potyvirus interacted with RNA, bound ssRNA, ssDNA, and dsRNA with similar affinity, but was not able to bind to dsDNA.
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