Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit.

@article{LeFebvre2006TranslationIF,
  title={Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit.},
  author={Aaron K LeFebvre and Nadejda L Korneeva and Marjan Trutschl and Urska Cvek and Roy D Duzan and Christopher A Bradley and John W. B. Hershey and R. E. Rhoads},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 32},
  pages={22917-32}
}
eIF3 in mammals is the largest translation initiation factor ( approximately 800 kDa) and is composed of 13 nonidentical subunits designated eIF3a-m. The role of mammalian eIF3 in assembly of the 48 S complex occurs through high affinity binding to eIF4G. Interactions of eIF4G with eIF4E, eIF4A, eIF3, poly(A)-binding protein, and Mnk1/2 have been mapped to discrete domains on eIF4G, and conversely, the eIF4G-binding sites on all but one of these ligands have been determined. The only eIF4G… CONTINUE READING

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