Journal of Biological Chemistry
Volume 278, Issue 36, 5 September 2003, Pages 34051-34060
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Protein Synthesis, Post-Translation Modification, and Degradation
Translation of the Minor Capsid Protein of a Calicivirus Is Initiated by a Novel Termination-dependent Reinitiation Mechanism*

https://doi.org/10.1074/jbc.M304874200Get rights and content
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Caliciviruses represent a family of positive strand RNA viruses responsible for a variety of syndromes in man and animals. VP10, a minor structural protein of the calicivirus rabbit hemorrhagic disease virus, is encoded in the small 3′-terminal open reading frame (ORF) 2 and is translated with an efficiency of ∼20% of the preceding ORF1. The presence of the ORF1 termination codon is crucial for VP10 expression. Translation of VP10 starts at an AUG codon located at positions –5 to –3 of the ORF1 termination codon. However, VP10 was also expressed in the absence of an AUG initiation codon. The majority of ORF1 could be deleted or replaced by different sequences without significant influence on VP10 expression as long as translation terminated at the given position. The RNA sequence of the 3′-terminal 84 nucleotides of ORF1 but not the encoded peptide was found to be crucial for VP10 expression. In contrast, nearly the entire ORF2 could be replaced by a foreign sequence without abrogation of its translation. Accordingly, VP10 is expressed in a translation termination/reinitiation process that is particular because it is independent of an AUG translational start codon and requires the presence of a sequence element upstream of the initiation site.

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*

This work was supported by Grants Me1367/1-3 and Me1367/1-5 from the Deutsche Forschungsgemeinschaft. 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.

The on-line version of this article (available at http://www.jbc.org) contains primer sequences.