RT Journal Article SR Electronic(1) A1 Maia, Ivan G. A1 Bernardi, FrançoiseYR 1996 T1 Nucleic acid-binding properties of a bacterially expressed potato virus Y helper component-proteinase JF Journal of General Virology, VO 77 IS 5 SP 869 OP 877 DO https://doi.org/10.1099/0022-1317-77-5-869 PB Microbiology Society, SN 1465-2099, AB The potyvirus helper component-proteinase (HC-Pro) is a multifunctional protein previously reported to have affinity for polyribonucleotides. To investigate further the ability of HC-Pro to bind nucleic acids, the potato virus Y (PVY) LYE84 isolate HC-Pro gene was amplified, cloned in an Escherichia coli expression vector and sequenced. HC-Pro was expressed as a fusion with the maltose-binding protein and purified by affinity chromatography. Electrophoretic mobility-shift assays demonstrated that HC-Pro acts as a sequence non-specific RNA-binding protein and suggest that more than one molecule of protein was bound per molecule of RNA. The HC-Pro RNA-binding activity was stable in 400 mM-NaCl and temperature sensitive. The recombinant protein preferentially bound ssRNA over DNA or dsRNA and showed little, if any, affinity for poly(A). The possible implications of the RNA-binding activity of HC-Pro in potyvirus replication and movement are discussed., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-77-5-869