Open AccessEfficient Translation of the Coat Protein Cistron of Tobacco Mosaic Virus in a Cell‐Free System from Escherichia coli
Author(s) -
GLOVER James F.,
WILSON T. Michael A.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06463.x
Subject(s) - tobacco mosaic virus , cistron , escherichia coli , biology , ribonucleoprotein , rna , translation (biology) , coat protein , biochemistry , microbiology and biotechnology , virus , chemistry , virology , messenger rna , gene
Translation of tobacco mosaic virus (TMV) RNA in a cell‐free system derived from Escherichia coli (MRE 600) reveals several discrete polypeptides in the M r range of 10000–50000. The major product is a polypeptide of M r 17500 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.