HIS-154 IS INVOLVED IN THE LINKAGE OF THE SACCHAROMYCES-CEREVISIAE L-A DOUBLE-STRANDED-RNA VIRUS GAG PROTEIN TO THE CAP STRUCTURE OF MESSENGER-RNAS AND IS ESSENTIAL FOR M(1) SATELLITE VIRUS EXPRESSION

The coat protein (Gag) of the double-stranded RNA virus L-A was previously shown to form a covalent bond with the cap structure of eukaryotic mRNAs. Here, we identify the linkage as a phosphoroimidazole bond between the alpha phosphate of the cap structure and a nitrogen in the Gag protein His-154 imidazole side chain. Mutations of His-154 abrogate the ability of Gag to bind to the cap structure, without affecting cap recognition, in vivo virus particle formation from an L-A cDNA clone, or in vitro specific binding and replication of plus-stranded single-stranded RNA. However, genetic analyses demonstrate that His-154 is essential for M1 satellite virus expression.