Abstract
Most positive strand RNA viruses infecting plants and animals encode proteins containing the so-called nucleotide binding motif (NTBM) (1) in their amino acid sequences (2). As suggested from the high level of sequence similarity of these viral proteins with the recently described superfamilies of helicase-like proteins (3-5), the NTBM-containing cylindrical inclusion (CI) protein from plum pox virus (PPV), which belongs to the potyvirus group of positive strand RNA viruses, is shown to be able to unwind RNA duplexes. This activity was found to be dependent on the hydrolysis of NTP to NDP and Pi, and thus it can be considered as an RNA helicase activity. In the in vitro assay used, the PPV CI protein was only able to unwind double strand RNA substrates with 3' single strand overhangs. This result indicates that the helicase activity of the PPV CI protein functions in the 3' to 5' direction (6). To our knowledge, this is the first report on a helicase activity associated with a protein encoded by an RNA virus.
MeSH Terms
Adenosine Triphosphate/metabolism
Base Sequence
Electrophoresis, Polyacrylamide Gel
Plant Viruses/enzymology,genetics
Plants/microbiology
RNA Helicases
RNA Nucleotidyltransferases/genetics,metabolism
RNA Viruses/enzymology,genetics
Chemicals
Adenosine Triphosphate
RNA Nucleotidyltransferases
RNA Helicases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Laín S
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Riechmann J L
García J A
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