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Volume 272, Number 47, Issue of November 21, 1997 pp. 29954-29957
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Characterization of the Reovirus 1 Protein RNA 5-Triphosphatase Activity

(Received for publication, July 16, 1997)

From the Département de Microbiologie et Immunologie, Université de Montréal, Montréal, Québec H3C 3J7, Canada

Characterization of the phosphohydrolytic activities of recombinant reovirus 1 protein demonstrates that, in addition to the previously reported nucleoside triphosphate phosphohydrolase and helicase activities, the protein also possesses RNA 5-triphosphatase activity. This activity was absolutely dependent on the presence of a divalent cation, Mg²⁺ or Mn²⁺, and specifically removes the 5--phosphate at the end of triphosphate-terminated RNAs. Kinetic competition analysis showed that nucleoside triphosphate phosphohydrolase and RNA 5-triphosphatase reactions are carried out at a common active site. These results strongly support the idea that, in addition to its role as an RNA helicase during transcription of the viral genome, 1 also participates during formation of the cap structure at the 5 end of newly synthesized reovirus mRNAs. The 1 protein represents only the third RNA triphosphatase whose primary structure is known and the first described in a double-stranded RNA virus.

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