Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine.
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.
D001665:Binding Sites; D008970:Molecular Weight; D009943:Organophosphorus Compounds; D017955:Poliovirus / Q000378:metabolism*; D011485:Protein Binding; D012367:RNA, Viral / Q000378:metabolism; D012260:Ribonucleases; D014443:Tyrosine; D014764:Viral Proteins / Q000378:metabolism
D009943:Organophosphorus Compounds; D012367:RNA, Viral; D014764:Viral Proteins; D014443:Tyrosine; D012260:Ribonucleases