Analysis of the protein composition of alfalfa mosaic virus RNA-dependent RNA polymerase

Virology. 1991 May;182(1):309-15. doi: 10.1016/0042-6822(91)90674-z.

Abstract

RNA-dependent RNA polymerase (RdRp) was solubilized and purified from cellular membranes isolated from alfalfa mosaic virus (AIMV)-infected tobacco by employing a procedure recently described for brome mosaic virus RdRp [R. Quadt and E.M.J. Jaspars, 1990, Virology 178, 189-194]. The purified AIMV RdRp is completely dependent on added template RNAs and exhibits a high degree of template specificity. Analysis of the protein composition of AIMV RdRp showed that AIMV-encoded proteins P1 and P2 and the coat protein (CP) are present in the active enzyme complex. Minus-strand synthesis by the AIMV RdRp is inhibited by AIMV CP. Native double-stranded AIMV RNAs are utilized as template for viral RNA synthesis by AIMV RdRp indicating that a helicase activity is present in the purified AIMV RdRp preparation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Capsid / metabolism
  • Macromolecular Substances
  • Medicago sativa
  • Molecular Weight
  • Mosaic Viruses / enzymology*
  • Mosaic Viruses / growth & development
  • RNA, Viral / biosynthesis
  • RNA-Dependent RNA Polymerase / chemistry*
  • RNA-Dependent RNA Polymerase / immunology
  • RNA-Dependent RNA Polymerase / metabolism
  • Substrate Specificity
  • Templates, Genetic
  • Viral Proteins / metabolism

Substances

  • Macromolecular Substances
  • RNA, Viral
  • Viral Proteins
  • RNA-Dependent RNA Polymerase