Efficient translation of the coat protein cistron of tobacco mosaic virus in a cell-free system from Escherichia coli.
Translation of tobacco mosaic virus (TMV) RNA in a cell-free system derived from Escherichia coli (MRE 600) reveals several discrete polypeptides in the Mr range of 10,000-50,000. The major product is a polypeptide of Mr 17,500 which comigrates with authentic TMV coat protein on sodium dodecyl sulphate/polyacrylamide gel electrophoresis. Structural investigations by peptide-mapping techniques and differential radiolabelling confirm that the major product is TMV coat protein with an N-terminal methionine. The major polypeptide product can be assembled in vitro into virus-like ribonucleoprotein particles. The structural and evolutionary implications of this observation, and the values of TMV in elucidating eukaryotic mRNA interactions with the prokaryotic protein-synthesizing machinery, are discussed.
D002474:Cell-Free System; D004926:Escherichia coli; D005796:Genes; D014176:Protein Biosynthesis; D014027:Tobacco Mosaic Virus; D014764:Viral Proteins / Q000235:genetics*
D014764:Viral Proteins