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Related Experiment Videos

Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation.

I K Ali1, L McKendrick, S J Morley

  • 1Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.

The EMBO Journal
|August 3, 2001
PubMed
Summary

Picornavirus proteases cleave translation initiation factor eIF4G. The resulting p100 fragment can support capped mRNA translation, contrary to prior assumptions. Viral RNA competition explains host shut-off.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Picornavirus infection leads to host cell protein synthesis shut-off.
  • This shut-off is linked to the cleavage of translation initiation factor eIF4G by viral proteases.
  • A C-terminal fragment (p100) is generated, and its role in capped mRNA translation was presumed to be inhibitory.

Purpose of the Study:

  • To investigate the functional capacity of the p100 fragment of eIF4G in capped mRNA translation.
  • To determine the mechanism underlying picornavirus-induced host shut-off.

Main Methods:

  • Utilized an eIF4G-depleted reticulocyte lysate system.
  • Employed recombinant p100 for in vitro translation assays.
  • Assessed translation inhibition by cap analogues and 4E-BP1.

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Main Results:

  • Demonstrated that the p100 fragment can support capped mRNA translation.
  • Showed that recombinant p100 reverses inhibition caused by cap analogues, 4E-BP1, or endogenous eIF4G cleavage.
  • Determined that higher p100 concentrations are needed for maximal capped mRNA translation compared to endogenous eIF4G.

Conclusions:

  • The p100 fragment retains the ability to support capped mRNA translation.
  • Picornavirus-induced host shut-off is not due to p100's inability to translate capped mRNAs.
  • Host shut-off results from viral RNA outcompeting host mRNA for limiting p100 concentrations.