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The RNA helicase CI from plum pox potyvirus has two regions involved in binding to RNA
Author(s) -
Fernández Andrés,
García Juan Antonio
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00571-6
Subject(s) - rna helicase a , rna , helicase , degradosome , rna binding protein , biology , binding site , microbiology and biotechnology , rna dependent rna polymerase , genetics , gene
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 maltosebinding 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.