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Cryo-EM study of start codon selection during archaeal translation initiation

Author

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  • Pierre-Damien Coureux

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay)

  • Christine Lazennec-Schurdevin

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay)

  • Auriane Monestier

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay)

  • Eric Larquet

    (Laboratoire de Physique de la Matière Condensée, Ecole polytechnique, CNRS, Université Paris-Saclay)

  • Lionel Cladière

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay
    Present address: Station Biologique de Roscoff, Place Georges Teissier, 29680 Roscoff, France)

  • Bruno P. Klaholz

    (Institute of Genetics and Molecular and Cellular Biology, Centre National de la Recherche Scientifique (CNRS)/Institut National de la Santé et de la Recherche Médicale (INSERM)/Université Louis Pasteur, BP 10142)

  • Emmanuelle Schmitt

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay)

  • Yves Mechulam

    (Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay)

Abstract

Eukaryotic and archaeal translation initiation complexes have a common structural core comprising e/aIF1, e/aIF1A, the ternary complex (TC, e/aIF2-GTP-Met-tRNAiMet) and mRNA bound to the small ribosomal subunit. e/aIF2 plays a crucial role in this process but how this factor controls start codon selection remains unclear. Here, we present cryo-EM structures of the full archaeal 30S initiation complex showing two conformational states of the TC. In the first state, the TC is bound to the ribosome in a relaxed conformation with the tRNA oriented out of the P site. In the second state, the tRNA is accommodated within the peptidyl (P) site and the TC becomes constrained. This constraint is compensated by codon/anticodon base pairing, whereas in the absence of a start codon, aIF2 contributes to swing out the tRNA. This spring force concept highlights a mechanism of codon/anticodon probing by the initiator tRNA directly assisted by aIF2.

Suggested Citation

  • Pierre-Damien Coureux & Christine Lazennec-Schurdevin & Auriane Monestier & Eric Larquet & Lionel Cladière & Bruno P. Klaholz & Emmanuelle Schmitt & Yves Mechulam, 2016. "Cryo-EM study of start codon selection during archaeal translation initiation," Nature Communications, Nature, vol. 7(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13366
    DOI: 10.1038/ncomms13366
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    Cited by:

    1. Gabrielle Bourgeois & Pierre-Damien Coureux & Christine Lazennec-Schurdevin & Clément Madru & Thomas Gaillard & Magalie Duchateau & Julia Chamot-Rooke & Sophie Bourcier & Yves Mechulam & Emmanuelle Sc, 2025. "Structures of Saccharolobus solfataricus initiation complexes with leaderless mRNAs highlight archaeal features and eukaryotic proximity," Nature Communications, Nature, vol. 16(1), pages 1-18, December.

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