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Reovirus 1 Protein: Affinity for Double-stranded Nucleic Acids by a Small Amino-terminal Region of the Protein Independent From the Zinc Finger Motif

Département de Microbiologie et Immunologie, Université de Montréal, P.O. Box 6128, Station Centre-ville, Montréal, Québec, Canada H3C 3J7

The reovirus 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 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 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 1, encompassing its nucleotide-binding motif, is involved in the affinity of this protein for nucleic acids.

Received 14 March 1994; accepted 22 June 1994.

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