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Related Experiment Videos

Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation

S Z Tarun1, S E Wells, J A Deardorff

  • 1Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, Berkeley, CA 94720, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 19, 1997
PubMed
Summary

Yeast translation factor eIF4G

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Area of Science:

  • Molecular Biology
  • Yeast Genetics
  • Protein Interactions

Background:

  • The eukaryotic translation initiation factor 4G (eIF4G) is crucial for protein synthesis, bridging mRNA's 5' cap and 3' poly(A) tail.
  • eIF4G interacts with both the cap-binding protein eIF4E and the poly(A)-binding protein (Pab1p).

Purpose of the Study:

  • To investigate the functional significance of the Pab1p-binding site on yeast eIF4G homologs (Tif4631p and Tif4632p).
  • To determine the role of this interaction in cap and poly(A) tail synergy during translation.
  • To explore the in vivo relevance of the Pab1p-binding site in relation to eIF4E function.

Main Methods:

  • Site-directed mutagenesis to identify conserved Pab1p-binding sites on Tif4631p and Tif4632p.
  • In vitro translation assays using uncapped, polyadenylylated mRNA.

Related Experiment Videos

  • Analysis of synergistic translation stimulation by the cap and poly(A) tail.
  • In vivo studies involving mutations in eIF4G and Pab1p, and their effects on cell growth and synthetic lethality with eIF4E mutations.

    • Main Results:

    • A conserved Pab1p-binding site was identified on yeast eIF4G homologs.
    • This site is essential for Pab1p and poly(A) tails to stimulate in vitro translation of uncapped mRNA.
    • The region containing the Pab1p-binding site is required for synergistic translation stimulation by the cap and poly(A) tail.
    • Mutations in this eIF4G region are essential for cell growth when the eIF4E binding site is compromised.
    • Pab1p mutations exhibit synthetic lethal interactions with eIF4E mutations.

    Conclusions:

    • Yeast eIF4G mediates poly(A) tail-stimulated translation in vitro.
    • Pab1p and the eIF4G Pab1p-binding domain can functionally compensate for partial loss of eIF4E function in vivo.
    • This highlights a critical interplay between the cap-binding complex and the poly(A) tail machinery mediated by eIF4G.