Genome-linked protein VPg of poliovirus is present as free VPg and VPg-pUpU in poliovirus-infected cells
- Creators
- Crawford, Nigel M.
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Baltimore, David
Abstract
VPg is a virus-encoded protein covalently attached to the 5' end of poliovirus virion RNA. We have used antibody prepared against chemically synthesized VPg to detect two forms of VPg in infected cells. Both forms were specifically immunoprecipitated from lysates of infected cells labeled with [3H]leucine. One appears to be unmodified VPg because it had the same electrophoretic mobility as synthetic VPg. The other had a larger apparent molecular weight than VPg and could be labeled in vivo with 32Pi. Its structure is VPg-pUpU, the UMP dinucleotide being attached to VPg via a phosphodiester bond to tyrosine, the third amino acid from the NH2 terminus of VPg. This structure is identical to that found at the 5' end of virion and minus-strand RNA.
Additional Information
© 1983 by the National Academy of Sciences. Contributed by David Baltimore, September 15, 1983. We thank Marie Chow, Peter Sarnow, Karla Kirkegaard, Gordon Foulkes, and Vincent Racaniello for their help and suggestions. N.M.C. was a predoctoral fellow of the National Science Foundation. D.B. is an American Cancer Society Research Professor. This investigation was supported by grants from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - CRApnas83.pdf
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Additional details
- PMCID
- PMC389969
- Eprint ID
- 7423
- Resolver ID
- CaltechAUTHORS:CRApnas83
- NSF Graduate Research Fellowship
- American Cancer Society
- NIH
- Created
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2007-02-13Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field