The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA.
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.
Blanc
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Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Goyer
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Sonenberg
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D000595:Amino Acid Sequence; D001665:Binding Sites; D002213:Capsid / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003488:Cyanogen Bromide; D005838:Genotype; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012315:RNA Caps / Q000378:metabolism*; D012328:RNA Viruses / Q000235:genetics / Q000378:metabolism*; D012330:RNA, Double-Stranded / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism*; D012260:Ribonucleases; D012270:Ribosomes / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013816:Thermodynamics; D014158:Transcription, Genetic; D014357:Trypsin
D010446:Peptide Fragments; D012315:RNA Caps; D012330:RNA, Double-Stranded; D012333:RNA, Messenger; D012260:Ribonucleases; D014357:Trypsin; D003488:Cyanogen Bromide