Previous studies have shown that the reovirus λ1 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 λ1 using gene reassortment analysis. In this study, it was demonstrated that the recombinant λ1 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 λ1 protein is a nucleoside triphosphate phosphohydrolase/helicase and strongly support the idea that λ1 participates in transcription of the viral genome.
Characterization of the Nucleoside Triphosphate Phosphohydrolase and Helicase Activities of the Reovirus λ1 Protein*
M. Bisaillon,J. Bergeron,G. Lemay
Published 1997 in Journal of Biological Chemistry
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- Publication year
1997
- Venue
Journal of Biological Chemistry
- Publication date
1997-07-18
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
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- Source metadata
Semantic Scholar, PubMed
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