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Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine
Journal of Biological Chemistry (1978)
  • Victor R. Ambros, Massachusetts Institute of Technology
  • David Baltimore, Massachusetts Institute of Technology
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.
Disciplines
Publication Date
August 10, 1978
Citation Information
Victor R. Ambros and David Baltimore. "Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine" Journal of Biological Chemistry Vol. 253 Iss. 15 (1978)
Available at: http://works.bepress.com/victor_ambros/88/