NDLI: Efficient Translation of the Coat Protein Cistron of Tobacco Mosaic Virus in a Cell-Free System from Escherichia coli

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Efficient Translation of the Coat Protein Cistron of Tobacco Mosaic Virus in a Cell-Free System from Escherichia coli

Content Provider	Scilit
Author	Glover, James F. Wilson, T. Michael A.
Copyright Year	2005
Description	Journal: Journal of Biological Inorganic Chemistry 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.
Ending Page	492
Starting Page	485
ISSN	2573508X
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1982.tb06463.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	3
Volume Number	122
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2005-03-03
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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