Send to

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1997 Jul 18;272(29):18298-303.

Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein.

Author information

  • 1Département de Microbiologie et Immunologie, Université de Montréal, Montréal, Québec H3C 3J7, Canada.


Previous studies have shown that the reovirus lambda1 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 lambda1 using gene reassortment analysis. In this study, it was demonstrated that the recombinant lambda1 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 lambda1 protein is a nucleoside triphosphate phosphohydrolase/helicase and strongly support the idea that lambda1 participates in transcription of the viral genome.

[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center