The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA

Author:

Blanc A1,Goyer C1,Sonenberg N1

Affiliation:

1. Department of Biochemistry, McGill University, Montreal, Quebec, Canada.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

Reference58 articles.

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4. Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine;Ambros V.;J. Biol. Chem.,1978

5. Expression of a functional influenza viral cap-recognizing protein by using a bovine papilloma virus vector;Braam-Markson J.;Proc. Natl. Acad. Sci. USA,1985

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