Article Dans Une Revue Nature Communications Année : 2019

Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism

Résumé

Eukaryotic ribosomes are synthesized in a hierarchical process driven by a plethora of assembly factors, but how maturation events at physically distant sites on pre-ribosomes are coordinated is poorly understood. Using functional analyses and cryo-EM, we show that ribosomal protein Rps20 orchestrates communication between two multi-step maturation events across the pre-40S subunit. Our study reveals that during pre-40S maturation, formation of essential contacts between Rps20 and Rps3 permits assembly factor Ltv1 to recruit the Hrr25 kinase, thereby promoting Ltv1 phosphorylation. In parallel, a deeply buried Rps20 loop reaches to the opposite pre-40S side, where it stimulates Rio2 ATPase activity. Both cascades converge to the final maturation steps releasing Rio2 and phosphorylated Ltv1. We propose that conformational proofreading exerted via Rps20 constitutes a checkpoint permitting assembly factor release and progression of pre-40S maturation only after completion of all earlier maturation steps.

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hal-02399643 , version 1 (01-02-2024)

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Valentin Mitterer, Ramtin Shayan, Sébastien Ferreira-Cerca, Guillaume Murat, Tanja Enne, et al.. Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism. Nature Communications, 2019, 10 (1), pp.2754. ⟨10.1038/s41467-019-10678-z⟩. ⟨hal-02399643⟩
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