Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition.

@article{Llcer2018TranslationalIF,
  title={Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition.},
  author={J. Ll{\'a}cer and T. Hussain and A. Saini and J. Nanda and Sukhvir Kaur and Yuliya Gordiyenko and Rakesh Kumar and A. Hinnebusch and J. Lorsch and V. Ramakrishnan},
  journal={eLife},
  year={2018},
  volume={7}
}
In eukaryotic translation initiation, AUG recognition of the mRNA requires accommodation of Met-tRNAi in a ‘PIN’ state, which is antagonized by the factor eIF1. eIF5 is a GTPase activating protein (GAP) of eIF2 that additionally promotes stringent AUG selection, but the molecular basis of its dual function was unknown. We present a cryo-electron microscopy (cryo-EM) reconstruction of a yeast 48S pre-initiation complex (PIC), at an overall resolution of 3.0 A, featuring the N-terminal domain… Expand
Structural inventory of native ribosomal ABCE1-43S pre-initiation complexes
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