Messenger RNA for the coat protein of tobacco mosaic virus

@article{Hunter1976MessengerRF,
  title={Messenger RNA for the coat protein of tobacco mosaic virus},
  author={Tony Hunter and Tim Hunt and John Knowland and David Zimmern},
  journal={Nature},
  year={1976},
  volume={260},
  pages={759-764}
}
TMV RNA is not an efficient template for translation of the viral coat protein, in spite of containing nucleo-tide sequences coding for the protein. Efficient translation requires the prior synthesis within infected cells of a smaller RNA carrying only a portion of the information encoded in the whole genome. 
Regulation of Translation of Viral mRNAs
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Viral genomes, and in particular viral RNA genomes, have served as model systems to investigate the steps involved in protein synthesis and have successfully helped to unravel the various strategies of translation known to occur on mRNA templates.
The Translation of Large Plant Viral RNAs
TLDR
The following overview of plant viral translation will center on the viruses with large, presumably multigenic RNAs (molecular weight over 106) and the large components of the multicomponent viruses like the bromoviridae.
Effects of the 5′-Leader Sequence of Tobacco Mosaic Virus RNA, or Derivatives Thereof, on Foreign mRNA and Native Viral Gene Expression
TLDR
One such pleiotropic sequence, the 5′-untranslated leader of tobacco mosaic virus (TMV) RNA, is the main subject of this article.
Virus reconstitution and the proof of the existence of genomic RNA.
This paper is a historical overview of the work done on the tobacco mosaic virus. The primary finding was that a virus is capable of reassembling itself from its component protein and RNA, and that
Virus reconstitution and the proof of the existence of genomic RNA.
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This paper is a historical overview of the work done on the tobacco mosaic virus. The primary finding was that a virus is capable of reassembling itself from its component protein and RNA, and that
Efficient translation of the coat protein cistron of tobacco mosaic virus in a cell-free system from Escherichia coli.
TLDR
Translation of tobacco mosaic virus RNA in a cell-free system derived from Escherichia coli reveals several discrete polypeptides in the Mr range of 10,000-50,000 which comigrates with authentic TMV coat protein on sodium dodecyl sulphate/polyacrylamide gel electrophoresis.
Leaky UAG termination codon in tobacco mosaic virus RNA
TLDR
It is shown 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 160Kprotein is increased whereas the yield of the 110K protein is diminished.
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References

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TLDR
The reconstitution of TMV does not proceed by the stepwise addition of single protein subunits, but by the addition of preformed disks to the growing rod, which is the basis of the selectivity for viral over other RNAs.
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RNA from tobacco mosaic virus can be translated inside oocytes of the frog Xenopus laevis. The main product is a polypeptide with a molecular weight of 140,000. There is no evidence for coat protein
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The nucleotide sequence has been determined for the first 53 bases of brome mosaic virus RNA4, the monocistronic messenger for brome mosaic virus coat protein. The sequence includes the binding site
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TLDR
TMV RNA, like many animal cellular and viral mRNAs recently examined, has a 5' terminus blocked by a methylated nucleotide inverted with respect to the rest of the chain, yielding products which imply the structure m7G5'ppp5'Gp.
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