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Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon

Strauss, Ellen G. and Rice, Charles M. and Strauss, James H. (1983) Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon. Proceedings of the National Academy of Sciences of the United States of America, 80 (17). pp. 5271-5275. ISSN 0027-8424. PMCID PMC384235.

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We have obtained the nucleotide sequence of the genomic RNAs of two alphaviruses, Sindbis virus and Middelburg virus, over an extensive region encoding the nonstructural (replicase) proteins. In both viruses in an equivalent position an opal (UGA) termination codon punctuates a long otherwise open reading frame. The nonstructural proteins are translated as polyprotein precursors that are processed by posttranslational cleavage into four polypeptide chains; the sequence data presented here indicate that the COOH-terminal polypeptide, ns72, may be produced by read-through of this opal codon. The high degree of amino acid homology between the ns72 polypeptides of the two viruses, in contrast to the lack of conserved sequence upstream from the read-through site, suggests that ns72 plays an important role in viral replication, possibly modulating the action of other replicase components.

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Additional Information:© 1983 National Academy of Sciences. Communicated by Ray D. Owen, May 31, 1983. The computer programs used in this work, including production of figures, were written by Tim Hunkapiller and we are grateful to him for access to these programs and instructions in their use. The computer work was performed on the computer facility of Lee Hood and we are grateful for the time on these facilities. Edith Lenches gave expert technical assistance in the maintenance and preparation of virus stocks and cell lines. This work was supported by Grants AI 10793 and GM 06965 from the National Institutes of Health and by Grant PCM 8022830 from the National Science Foundation. 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.
Funding AgencyGrant Number
NIHAI 10793
NIHGM 06965
Issue or Number:17
PubMed Central ID:PMC384235
Record Number:CaltechAUTHORS:20120709-105424972
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:32310
Deposited By: Jason Perez
Deposited On:09 Jul 2012 18:10
Last Modified:15 Jun 2020 23:28

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