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Published August 10, 1978 | public
Journal Article Open

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.

Additional Information

Copyright © 1978 by the American Society for Biochemistry and Molecular Biology. (Received for publication, April 27, 1978) We are grateful to Dr. John Rose and Matthew Scott whose suggestions induced us to test for a linkage to tyrosine. We also thank Dr. Eckard Wimmer for suggesting the use of micrococcal nuclease. This work was supported by Grants CA14051 and CA12174 from the National Institutes of Health and Grant AI08388 from the National Institute of Allergy and Infectious Diseases. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. [D.B. was an] American Cancer Society Research Professor.

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Created:
August 22, 2023
Modified:
October 16, 2023