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Pol of gag–pol fusion protein required for encapsidation of viral RNA of yeast L-A virus

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Abstract

DOUBLE-STRANDED RNA viruses have an RNA-dependent RNA polymerase activity associated with the viral particles which is indispensable for their replication cycle. Using the yeast L-A double-stranded RNA virus we have investigated the mechanism by which the virus encapsidates its genomic RNA and RNA polymerase. The L-A gag gene encodes the principal viral coat protein and the overlapping pol gene is expressed as a gag–pol fusion protein which is formed by a −1 ribosomal frameshift1–3. Here we show that Gag alone is sufficient for virus particle formation, but that it fails to package the viral single-stranded RNA genome. Encapsidation of the viral RNA requires only a part of the Pol region (the N-terminal quarter), which is presumably distinct from the RNA polymerase domain. Given that the Pol region has single-stranded RNA-binding activity, these results are consistent with our L-A virus encapsidation model1: the Pol region of the fusion protein binds specifically to the viral genome (+) strand, and the N-terminal gag-encoded region primes polymerization of Gag to form the capsid, thus ensuring the packaging of both the viral genome and the RNA polymerase.

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Fujimura, T., Ribas, J., Makhov, A. et al. Pol of gag–pol fusion protein required for encapsidation of viral RNA of yeast L-A virus. Nature 359, 746–749 (1992). https://doi.org/10.1038/359746a0

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  • DOI: https://doi.org/10.1038/359746a0

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