The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro.

@article{Fraser2004TheJO,
  title={The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro.},
  author={Christopher S. Fraser and Jennifer Lee and Greg L. Mayeur and Martin Bushell and Jennifer A. Doudna and John W. B. Hershey},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 10},
  pages={8946-56}
}
Eukaryotic initiation factor 3 (eIF3) is a 12-subunit protein complex that plays a central role in binding of initiator methionyl-tRNA and mRNA to the 40 S ribosomal subunit to form the 40 S initiation complex. The molecular mechanisms by which eIF3 exerts these functions are poorly understood. To learn more about the structure and function of eIF3 we have expressed and purified individual human eIF3 subunits or complexes of eIF3 subunits using baculovirus-infected Sf9 cells. The results… CONTINUE READING