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

Pierre-Damien Coureux (), Christine Lazennec-Schurdevin, Auriane Monestier, Eric Larquet, Lionel Cladière, Bruno P. Klaholz, Emmanuelle Schmitt () and Yves Mechulam
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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
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

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13366

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