Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).

  title={Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).},
  author={Chaomin Sun and Aleksandar Todorovic and Jordi Querol-Aud{\'i} and Yun Bai and Nancy Villa and M Patricia Snyder and John Ashchyan and Christopher S Lewis and Abbey Hartland and Scott D Gradia and Christopher S. Fraser and Jennifer A. Doudna and Eva Nogales and Jamie H D Cate},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={108 51},
Protein fate in higher eukaryotes is controlled by three complexes that share conserved architectural elements: the proteasome, COP9 signalosome, and eukaryotic translation initiation factor 3 (eIF3). Here we reconstitute the 13-subunit human eIF3 in Escherichia coli, revealing its structural core to be the eight subunits with conserved orthologues in the proteasome lid complex and COP9 signalosome. This structural core in eIF3 binds to the small (40S) ribosomal subunit, to translation… CONTINUE READING
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Crystal structure of the eukaryotic 40 S ribosomal subunit in complex with initiation factor 1

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