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Complete translation of poliovirus RNA in a eukaryotic cell-free system

Villa-Komaroff, Lydia and Guttman, Naomi and Baltimore, David and Lodish, Harvey F. (1975) Complete translation of poliovirus RNA in a eukaryotic cell-free system. Proceedings of the National Academy of Sciences of the United States of America, 72 (10). pp. 4157-4161. ISSN 0027-8424. PMCID PMC433159.

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Poliovirus RNA stimulates incorporation of 35S from both [35S]methionine and formyl-[35S]methionyl-tRNAf{}Met in cell-free systems derived from HeLa cells or from poliovirus-infected HeLa cells. The largest product formed under the direction of the viral RNA is the same size as the polyprotein thought to represent translation of the entire RNA. Synthesis of this polyprotein and other large products was stimulated greatly by increasing the salt concentration during the reaction from the optimum for initiation (90 mM) to the optimum for elongation (155 mM). Only one initiation peptide could be identified, and a tryptic digest of the product contained mainly peptides that cochromatographed with peptides from authentic viral proteins. The RNA from a deletion mutant of poliovirus initiated protein synthesis at the same site used by standard RNA and programmed synthesis of an appropriately deleted set of polypeptides. The results strongly support the model of translation of poliovirus RNA from a single initiation site into a continuous polyprotein that is cleaved to form the functional proteins. It is suggested that uninfected HeLa cell extracts can carry out the cleavages of nascent polyprotein.

Item Type:Article
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URLURL TypeDescription CentralArticle
Baltimore, David0000-0001-8723-8190
Additional Information:© 1975 by the National Academy of Sciences. Contributed by David Baltimore, July 7, 1975. This work was supported by the following grants from the National Institutes of Health: AI-08814, AI-08388, AM-15929, and CA-12174. D.B. is an American Cancer Research Professor. H.F.L. is the recipient of Research Career Development Award no. GM-50175 from the National Institutes of Health.
Funding AgencyGrant Number
American Cancer SocietyUNSPECIFIED
Subject Keywords:protein synthesis; picornaviruses; polyproteins; proteolysis
Issue or Number:10
PubMed Central ID:PMC433159
Record Number:CaltechAUTHORS:VILpnas75
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7519
Deposited By: Tony Diaz
Deposited On:01 Mar 2007
Last Modified:29 Jan 2021 00:18

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