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Proceedings of the National Academy of Sciences, Vol 88, 174-178, Copyright © 1991 by National Academy of Sciences
JD Dinman, T Icho and RB Wickner
The L-A double-stranded RNA (dsRNA) virus of Saccharomyces cerevisiae has
two open reading frames (ORFs). ORF1 encodes the 80-kDa major coat protein
(gag). ORF2, which is expressed only as a 180-kDa fusion protein with ORF1,
encodes a single-stranded RNA-binding domain and has the consensus sequence
for RNA-dependent RNA polymerases of (+)-strand and double-stranded RNA
viruses (pol). We show that the 180-kDa protein is formed by -1 ribosomal
frame-shifting by a mechanism indistinguishable from that of retroviruses.
Analysis of the "slippery site" suggests that a low probability of
unpairing of the aminoacyl-tRNA from the 0-frame codon at the ribosomal A
site reduces the efficiency of frameshifting more than the reluctance of a
given tRNA to have its wobble base mispaired. Frameshifting of L-A requires
a pseudoknot structure just downstream of the shift site. The efficiency of
the L-A frameshift site is 1.8%, similar to the observed molar ratio in
viral particles of the 180-kDa fusion protein to the major coat protein.
ARTICLE
A -1 Ribosomal Frameshift in a Double-Stranded RNA Virus of Yeast Forms a Gag-Pol Fusion Protein
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