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

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

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.

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O4-(5'-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus. [Proc Natl Acad Sci U S A. 1978]
O4-(5'-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus.
Rothberg PG, Harris TJ, Nomoto A, Wimmer E. Proc Natl Acad Sci U S A. 1978 Oct; 75(10):4868-72.
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Crawford NM, Baltimore D. Proc Natl Acad Sci U S A. 1983 Dec; 80(24):7452-5.
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Cited by 73 PubMed Central articles

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