Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine

J Biol Chem. 1978 Aug 10;253(15):5263-6.

Abstract

Purification and partial characterization of the poliovirus RNA-linked protein (VPg) are described. VPg has been freed from the RNA by ribonuclease digestion and phenol extraction. Gel filtration chromatography of VPg-pUp (labeled with 32P) in 0.5% sodium dodecyl sulfate or 6 M guanidine HCl indicates that it has a molecular weight of about 12,000. VPg is bound to the 5' end of poliovirion RNA by a phosphodiester bond between a tyrosine residue in the VPg molecule and the 5'-terminal uridine. After acid hydrolysis of [3H]tyrosine-labeled VPg-pU, free tyrosine can be released by venom phosphodiesterase. Acid hydrolysis of VPg-p labeled with either 32P or [3H] tyrosine yields tyrosine-phosphate. There appears to be only 1 tyrosine residue per VPg molecule.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Molecular Weight
  • Organophosphorus Compounds
  • Poliovirus / metabolism*
  • Protein Binding
  • RNA, Viral* / metabolism
  • Ribonucleases
  • Tyrosine*
  • Viral Proteins* / metabolism

Substances

  • Organophosphorus Compounds
  • RNA, Viral
  • Viral Proteins
  • Tyrosine
  • Ribonucleases