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The final step of 40S ribosomal subunit maturation is controlled by a dual key lock
Open accessPreprint — published as 10.7554/elife.61254 · Paper page
Abstract
Preventing premature interaction of preribosomes with the translation apparatus is essential to translation accuracy. Hence, the final maturation step releasing functional 40S ribosomal subunits, namely processing of the 18S ribosomal RNA 3’ end, is safeguarded by protein DIM2, which both interacts with the endoribonuclease NOB1 and masks the rRNA cleavage site. To elucidate the control mechanism that unlocks NOB1 activity, we performed cryo-EM analysis of late human pre-40S particles purified using a catalytically-inactive form of ATPase RIO1. These structures, together with in vivo and in vitro functional analyses, support a model in which ATP-loaded RIO1 cooperates with ribosomal protein RPS26/eS26 to displace DIM2 from the 18S rRNA 3’ end, thereby triggering final cleavage by NOB1; release of ADP then leads to RIO1 dissociation from the 40S subunit. This dual key lock mechanism requiring RIO1 and RPS26 guarantees the precise timing of pre-40S particle conversion into translation-competent ribosomal subunits.
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Metadata
- Authors
- Plassart, L., Shayan, R., Montellese, C., Rinaldi, D., Larburu, N., Pichereaux, C., Lebaron, S., O’Donohue, M.-F., Kutay, U., Marcoux, J., Gleizes, P.-E., & Plisson-Chastang, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- ETH Zurich (CH)
- Corresponding author
- Gleizes, Pierre-Emmanuel
- ORCID
- Venue
- eLife
- Publisher
- openRxiv
- Published
- 2020-07-31
- Volume
- 10
- Pages
- e61254
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC8112863
- OpenAlex
- W3046742242
- Cited by
- 55
- References
- 1
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 12 · 2023: 6 · 2022: 11 · 2021: 5
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
- HAL (submittedVersion, other-oa)
- HAL (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- ETH Zürich Research Collection (cc-by)
- Funders
- National Science Foundation
- European Commission
- Agence Nationale de la Recherche (ANR-16-CE11-0029)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (166565)
- Ministry of Economy, Trade and Industry
- Centre National de la Recherche Scientifique
- Région Occitanie Pyrénées-Méditerranée
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- cryo-EM structure
- MeSH terms
- Humans, Nuclear Proteins, Ribosomal Proteins, RNA-Binding Proteins, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Ribosome Subunits, Small, Eukaryotic
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