Proteolytic maturation of the turnip-yellow-mosaic-virus polyprotein coded in vitro occurs by internal catalysis.

Abstract

The genomic RNA of turnip yellow mosaic virus is translated in vitro into two major high-molecular-weight proteins, the larger of which (Mr 195 000) undergoes post-translational cleavage. The mechanism of formation of the primary cleavage products (Mr 120 000 and Mr 78 000) of the 195 000-Mr protein has been examined. The fact that cleavage partly occurs at a rate insensitive to dilution of the 195 000-Mr protein is suggestive of an intramolecular mechanism of proteolytic maturation.