Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly.

@article{Asano1997StructureOC,
  title={Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly.},
  author={Katsura Asano and Hans Peter Vornlocher and Nancy J. Richter-Cook and William C. Merrick and Alan G Hinnebusch and John W. B. Hershey},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 43},
  pages={
          27042-52
        }
}
The mammalian translation initiation factor 3 (eIF3), is a multiprotein complex of approximately 600 kDa that binds to the 40 S ribosome and promotes the binding of methionyl-tRNAi and mRNA. cDNAs encoding 5 of the 10 subunits, namely eIF3-p170, -p116, -p110, -p48, and -p36, have been isolated previously. Here we report the cloning and characterization of human cDNAs encoding the major RNA binding subunit, eIF3-p66, and two additional subunits, eIF3-p47 and eIF3-p40. Each of these proteins is… CONTINUE READING
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Summary of dbEST by Human Library, National Center for Biotechnology Information

H.-P. Vornlocher, P. Hanachi, J.W.B. Hershey
National Center for Biotechnology Information • 1996