Nucleic Acids Research, Vol 25, Issue 22 4474-4480, Copyright © 1997 by Oxford University Press
A Fernandez, HS Guo, P Saenz, L Simon-Buela, M Gomez de Cedron and JA Garcia
The plum pox potyvirus (PPV) protein CI is an RNA helicase whose function
in the viral life cycle is still unknown. The CI protein contains seven
conserved sequence motifs typical of RNA helicases of the superfamily SF2.
We have introduced several individual point mutations into the region
coding for motif V of the PPV CI protein and expressed these proteins in
Escherichia coli as maltose binding protein fusions. Mutations that
abolished RNA helicase activity also disturbed NTP hydrolysis. No mutations
affected the RNA binding capacity of the CI protein. These mutations were
also introduced in the PPV genome making use of a full-length cDNA clone.
Mutant viruses carrying CI proteins with reduced RNA helicase activity
replicated very poorly in protoplasts and were unable to infect whole
plants without rapid pseudoreversion to wild-type. These results indicate
that motif V is involved in the NTP hydrolysis step required for potyvirus
RNA helicase activity, and that this activity plays an essential role in
virus RNA replication inside the infected cell.
ARTICLES
The motif V of plum pox potyvirus CI RNA helicase is involved in NTP hydrolysis and is essential for virus RNA replication
Centro Nacional de Biotecnologia (CSIC), Campus de la Universidad Autonoma de Madrid, 28049 Madrid, Spain.
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