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Volume 272, Number 29, Issue of July 18, 1997 pp. 18298-18303
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Characterization of the Nucleoside Triphosphate Phosphohydrolase and Helicase Activities of the Reovirus lambda 1 Protein

(Received for publication, January 31, 1997, and in revised form, May 12, 1997)

Martin Bisaillon , Josée Bergeron and Guy Lemay

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

Previous studies have shown that the reovirus lambda 1 core protein harbors a putative nucleotide-binding motif and exhibits an affinity for nucleic acids. In addition, a nucleoside triphosphate phosphohydrolase activity present in reovirus cores has been recently assigned to lambda 1 using gene reassortment analysis. In this study, it was demonstrated that the recombinant lambda 1 protein, expressed in the yeast Pichia pastoris, is able to hydrolyze nucleoside 5'-triphosphates or deoxynucleoside 5'-triphosphates. This activity was absolutely dependent on the presence of a divalent cation, Mg2+ or Mn2+. The protein can also unwind double-stranded nucleic acid molecules in the presence of a nucleoside 5'-triphosphate or deoxynucleoside 5'-triphosphate. These results provide the first biochemical evidence that the reovirus lambda 1 protein is a nucleoside triphosphate phosphohydrolase/helicase and strongly support the idea that lambda 1 participates in transcription of the viral genome.


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