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.
| Original language | English |
|---|---|
| Pages (from-to) | 31-41 |
| Number of pages | 11 |
| Journal | Biochimie |
| Volume | 217 |
| DOIs | |
| Publication status | Published - 1 Feb 2024 |
Keywords
- Initiator tRNA
- Late steps of initiation
- Ribosome
- eIF1A
- eIF5B
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