The 5'-terminal structures of poliovirion RNA and poliovirus mRNA differ only in the genome-linked protein VPg.
- 2 December 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (12) , 5345-5349
- https://doi.org/10.1073/pnas.74.12.5345
Abstract
The 5''-terminal, RNase T1-resistant oligonucleotide of poliovirus mRNA was isolated. Its sequence is pU-U-A-A-A-A-C-A-Gp, which is identical to that of virion RNA except that the genome-linked protein VPg is absent. Because all newly synthesized viral RNA are VPg-linked, VPg is apparently cleaved from progeny RNA at the linkage between protein and nucleic acid prior to polyribosome formation. This may represent a new mode of processing of viral macromolecules. Virion RNA from which VPg was cleaved proteolytically retains its specific infectivity, suggesting that VPg is not involved in early steps (penetration and translation) of the infectious cycle initiated by RNA.This publication has 20 references indexed in Scilit:
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