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Abstract
THE RNA of tobacco mosaic virus (TMV) can be translated in various cell-free systems1–3 and in amphibian oocytes4, to yield two large polypeptides of molecular weights (MW) approximately 110,000 (110K) and 160,000 (160K). Products of the same sizes are found in infected plants2,5 and protoplasts6 and they are probably components of the viral replicase7,8. I show here that synthesis of these two proteins is initiated at the same site; the larger product is generated by partial readthrough of an amber (UAG) termination codon, and in the presence of yeast amber suppressor tRNA, the in vitro synthesis of the 160K protein is increased whereas the yield of the 110K protein is diminished.
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