The RNA helicase CI from plum pox potyvirus has two regions involved in binding to RNA.
The plum pox virus (PPV) protein CI is an RNA helicase, whose function in the virus replication is still unknown. Recently, an RNA binding domain was mapped to a region of the CI protein that includes the arginine-rich motif VI typical of RNA helicases of the superfamily SF2. In the present study, a second region involved in RNA binding activity of the CI protein has been identified. Northwestern assays with a series of maltose-binding protein fusions that contain different CI fragments showed that the RNA binding domain is located between residues 75 and 143. This segment contains the two most amino-terminal conserved domains of RNA helicases: I, involved in NTP binding, and Ia, of unknown function. The results can be explained in the context of a close interdependence between the protein regions involved in the NTPase and RNA binding activities that is expected for an RNA helicase.
Fernández
A
A
Centro Nacional de Biotecnología (CSIC), Campus de la Universidad Autónoma de Madrid, Spain.
García
J A
JA
D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D007181:Inclusion Bodies, Viral / Q000378:metabolism; D017801:Plum Pox Virus / Q000201:enzymology*; D012313:RNA / Q000378:metabolism*; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D014764:Viral Proteins; D012313:RNA; D012316:RNA Nucleotidyltransferases; D020365:RNA Helicases