VPg, coat protein and five non-structural proteins of potato A potyvirus bind RNA in a sequence-unspecific manner

J Gen Virol. 1998 Dec:79 ( Pt 12):3123-7. doi: 10.1099/0022-1317-79-12-3123.

Abstract

The potato A potyvirus (PVA)-encoded proteins P1, HC-Pro, P3, CI, VPg, NIaPro, NIb and coat protein (CP) were expressed as 6 x His-tagged recombinant proteins in Escherichia coli and purified to homogeneity. RNA binding was tested using purified proteins in Northwestern and liquid assays. PVA proteins except P3 bound to positive- and negative-sense transcripts prepared from the nontranslated 5'- and 3'-regions of PVA genomic RNA and to full-length transcripts of PVA RNA. RNA binding by these proteins showed no sequence specificity since they also bound to various non-PVA control RNAs. Binding properties of P1, HC-Pro, CI and NIaPro are consistent with previous studies carried out on a few other potyviruses, but the binding of VPg, NIb and CP to RNA reveal novel interactions between RNA and potyvirus proteins. Furthermore, the RNA-binding properties of all major proteins of a potyvirus have not been reported previously.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid / metabolism*
  • Potyvirus / genetics
  • Potyvirus / metabolism*
  • RNA, Viral / metabolism*
  • RNA-Binding Proteins / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Ribonucleoproteins*
  • Viral Nonstructural Proteins / metabolism*

Substances

  • RNA, Viral
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Ribonucleoproteins
  • Viral Nonstructural Proteins
  • genome-linked viral protein, potato virus Y