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Reovirus gamma-1 protein: Affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif


, : Reovirus gamma-1 protein: Affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif. Journal of General Virology 75(11): 3261-3266

The reovirus lambda-1 protein, a major component of the inner capsid. has been shown to exhibit an affinity for dsRNA in a 'Northwestern' filter-binding assay. In the present study it was demonstrated that the protein can bind dsDNA as well as dsRNA. A bacterial expression system was used to study the protein region able to bind to nucleic acids. The amino-terminal 187 amino acids of lambda-1 were fused to the bacterial maltose-binding protein and shown to be sufficient for binding to nucleic acids. The putative zinc finger present on lambda-1 is not encompassed in this fragment of the protein. Site-directed mutagenesis also indicated that this zinc finger motif is unrelated to binding. In contrast, mutations introduced in a previously suggested nucleotide-binding motif almost completely prevented the binding. These data indicate that the amino-terminal end of lambda-1, encompassing its nucleotide-binding motif. is involved in the affinity of this protein for nucleic acids.

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