The Gag domain of the Gag-Pol fusion protein directs incorporation into the L-A double-stranded RNA viral particles in Saccharomyces cerevisiae.

The Journal of Biological Chemistry
J C Ribas, R B Wickner

Abstract

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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Citations

Nov 5, 2008·Proceedings of the National Academy of Sciences of the United States of America·Jinghua TangMax L Nibert
Feb 24, 2006·Molecular Biology of the Cell·Scott NolanEric Grote
Oct 7, 2016·PLoS Pathogens·Paul A RowleySara L Sawyer
Mar 21, 2019·Journal of the Royal Society, Interface·Sean Sheppard, Duygu Dikicioglu
Aug 24, 2000·The Journal of Biological Chemistry·T Fujimura, R Esteban
Sep 13, 2018·Viruses·Daniel LuqueJosé R Castón
Jan 28, 2021·Microorganisms·Lina AitmanaitėSaulius Serva
Nov 20, 2020·Journal of Virology·Michaela ProcházkováPavel Plevka

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