Eukaryotic translation initiation factor eIF5 promotes the accuracy of start codon recognition by regulating Pi release and conformational transitions of the preinitiation complex

@inproceedings{Saini2014EukaryoticTI,
  title={Eukaryotic translation initiation factor eIF5 promotes the accuracy of start codon recognition by regulating Pi release and conformational transitions of the preinitiation complex},
  author={Adesh K Saini and Jagpreet Singh Nanda and Pilar Martin-Marcos and Jinsheng Dong and F. R. Zhang and Meenakshi Bhardwaj and Jon R. Lorsch and Alan G Hinnebusch},
  booktitle={Nucleic acids research},
  year={2014}
}
eIF5 is the GTPase activating protein (GAP) for the eIF2 · GTP · Met-tRNAi (Met) ternary complex with a critical role in initiation codon selection. Previous work suggested that the eIF5 mutation G31R/SUI5 elevates initiation at UUG codons by increasing GAP function. Subsequent work implicated eIF5 in rearrangement of the preinitiation complex (PIC) from an open, scanning conformation to a closed state at AUG codons, from which Pi is released from eIF2 · GDP · Pi. To identify eIF5 functions… CONTINUE READING

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