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    In eukaryotes and in archaea late steps of translation initiation involve the two initiation factors e/aIF5B and e/aIF1A. These two factors are also orthologous to the bacterial IF2 and IF1 proteins, respectively. Recent cryo-EM studies showed how e/aIF5B and e/aIF1A cooperate on the small ribosomal subunit to favor the binding of the large ribosomal subunit and the formation of a ribosome competent for elongation. In this review, pioneering studies and recent biochemical and structural results providing new insights into the role of a/eIF5B in archaea and eukaryotes will be presented. Recent structures will also be compared to orthologous bacterial initiation complexes to highlight domain-specific features and the evolution of initiation mechanisms. Copyright © 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

    Citation

    Ramy Kazan, Gabrielle Bourgeois, Christine Lazennec-Schurdevin, Pierre-Damien Coureux, Yves Mechulam, Emmanuelle Schmitt. Structural insights into the evolution of late steps of translation initiation in the three domains of life. Biochimie. 2024 Feb;217:31-41

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    PMID: 36773835

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