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Journal Articles Biochimie Year : 2023

Structural insights into the evolution of late steps of translation initiation in the three domains of life

Abstract

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.
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hal-04058214 , version 1 (04-04-2023)

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Ramy Kazan, Gabrielle Bourgeois, Christine Lazennec-Schurdevin, Pierre-Damien Coureux, Yves Mechulam, et al.. Structural insights into the evolution of late steps of translation initiation in the three domains of life. Biochimie, 2023, pp.S0300-9084(23)00030-5. ⟨10.1016/j.biochi.2023.02.002⟩. ⟨hal-04058214⟩
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