Mitterer, Valentin and Shayan, Ramtin and Ferreira-Cerca, Sebastien and Murat, Guillaume and Enne, Tanja and Rinaldi, Dana and Weigl, Sarah and Omanic, Hajrija and Gleizes, Pierre-Emmanuel and Kressler, Dieter and Plisson-Chastang, Celia and Pertschy, Brigitte (2019) Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism. NATURE COMMUNICATIONS, 10: 2754. ISSN 2041-1723,
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TRANSLATION INITIATION; EUKARYOTIC RIBOSOME; CRYSTAL-STRUCTURE; RNA; BIOGENESIS; SYSTEM; 90S; REFINEMENT; TRANSPORT; PROTEINS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 08 Apr 2020 06:33 |
| Last Modified: | 08 Apr 2020 06:33 |
| URI: | https://pred.uni-regensburg.de/id/eprint/26815 |
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