Abstract
Turnip yellow mosaic virus genomic RNA codes in vitro for two overlapping proteins, 150-kilodalton (150K protein) and 206-kilodalton (206K protein) proteins. The proteolytic maturation known to affect the 206K protein has been further characterized by in vitro translation assays in a reticulocyte lysate or wheat germ extract. Cleavage is inhibited at 37 degrees C and restored when the temperature is shifted to 30 or 25 degrees C. Temperature shift experiments are used here to demonstrate that the 150K protein and the previously characterized 78K protein are the two fragments resulting from a primary cleavage phenomenon that affects the 206K protein in a cotranslational manner under usual translation conditions. This processing is prevented by several cysteine and serine proteinase inhibitors.
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