Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism
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 orchestrat...
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| Hauptverfasser: | , , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
21 June 2019
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| In: |
Nature Communications
Year: 2019, Jahrgang: 10 |
| ISSN: | 2041-1723 |
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| Verfasserangaben: | Valentin Mitterer, Ramtin Shayan, Sebastien Ferreira-Cerca, Guillaume Murat, Tanja Enne, Dana Rinaldi, Sarah Weigl, Hajrija Omanic, Pierre-Emmanuel Gleizes, Dieter Kressler, Celia Plisson-Chastang & Brigitte Pertschy |
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| 520 | |a 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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