Key result
The Gag domain instructs the incorporation of the Gag-Pol fusion protein into viral particles, and N-terminal acetylation of Gag is essential for viral assembly but dispensable for Gag-Pol function.
In the L-A double-stranded RNA virus of yeast, the Gag protein directs the incorporation of the Gag-Pol fusion protein into viral particles, and N-terminal acetylation of Gag is essential for assembly but not for Gag-Pol function.
Informs yeast viral assembly mechanisms; leaves open extension to human pathogens or therapeutic targets.
The L-A double-stranded RNA virus of yeast encodes its major coat protein, Gag, and a Gag-Pol fusion protein made by a -1 ribosomal frameshift, a coding strategy used by many retroviruses. We find that cells expressing only Gag from one plasmid and only Gag-Pol (in frame) from a separate plasmid can support the propagation of M1 double-stranded RNA, encoding the killer toxin. We use this system to separately investigate the functions of Gag and the Gag part of Gag-Pol. L-A contains two fusion protein molecules per particle, and although N-terminal acetylation of Gag is essential for viral assembly, it is completely dispensable for function of Gag-Pol. In general, the requirements on Gag for viral assembly and propagation are more stringent than on the Gag part of Gag-Pol. Finally, we directly show that it is Gag that instructs the incorporation of Gag-Pol into the viral particles.
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Ribas et al. (1998) studied L-A double-stranded RNA virus in Saccharomyces cerevisiae. Expression of Gag and Gag-Pol from separate plasmids was evaluated on Viral assembly and propagation of M1 double-stranded RNA. The Gag domain instructs the incorporation of the Gag-Pol fusion protein into viral particles, and N-terminal acetylation of Gag is essential for viral assembly but dispensable for Gag-Pol function.
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