Key result
The coat protein of the yeast double-stranded RNA virus L-A interacts with the eukaryotic mRNA 5' cap structure through a covalent bond, in contrast to cellular cap-binding proteins.
The coat protein of the yeast double-stranded RNA virus L-A acts as a novel cap-binding protein that attaches covalently to the eukaryotic mRNA cap structure.
Hypothesis-generating in yeast; leaves open whether analogous viral proteins modulate cap-dependent processes in mammalian cells.
The eukaryotic mRNA 5' cap structure m7GpppX (where X is any nucleotide) interacts with a number of cellular proteins. Several of these proteins were studied in mammalian, yeast, and drosophila cells and found to be involved in translation initiation. Here we describe a novel cap-binding protein, the coat protein of L-A, a double-stranded RNA virus that is persistently maintained in many Saccharomyces cerevisiae strains. The results also suggest that the coat protein of a related double-stranded RNA virus (L-BC) is likewise a cap-binding protein. Strikingly, in contrast to the cellular cap-binding proteins, the interaction between the L-A virus coat protein and the cap structure is through a covalent bond.
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Blanc et al. (1992) studied this question. Coat protein of L-A virus vs. Cellular cap-binding proteins was evaluated on Interaction with eukaryotic mRNA 5' cap structure. The coat protein of the yeast double-stranded RNA virus L-A interacts with the eukaryotic mRNA 5' cap structure through a covalent bond, in contrast to cellular cap-binding proteins.
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