Conformational proofreading of distant 40S ribosomal subunit maturation events by a long-range communication mechanism
- Mitterer, Valentin Institute for Molecular Biosciences, University of Graz, Austria - Biochemistry Centre, University of Heidelberg, Germany -
- Shayan, Ramtin Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, France -
- Ferreira-Cerca, Sébastien Biochemistry III – Institute for Biochemistry, Genetics and Microbiology, University of Regensburg, Germany
- Murat, Guillaume Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
- Enne, Tanja Institute for Molecular Biosciences, University of Graz, Austria
- Rinaldi, Dana Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, France
- Weigl, Sarah Institute for Molecular Biosciences, University of Graz, Austria
- Omanic, Hajrija Institute for Molecular Biosciences, University of Graz, Austria
- Gleizes, Pierre-Emmanuel Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, France
- Kressler, Dieter Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
- Plisson-Chastang, Celia Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, France
- Pertschy, Brigitte Institute for Molecular Biosciences, University of Graz, Austria
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2019
Published in:
- Nature Communications. - 2019, vol. 10, no. 1, p. 2754
English
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.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
-
- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 326945
- DOI 10.1038/s41467-019-10678-z
- Persistent URL
- https://folia.unifr.ch/unifr/documents/307989
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