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Cited by 55RNA and protein synthesis mechanismsNuclear Structure and FunctionRNA Research and Splicing

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The final step of 40S ribosomal subunit maturation is controlled by a dual key lock

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Plassart, Laura, Shayan, Ramtin, Montellese, Christian, Rinaldi, Dana, Larburu, Natacha, Pichereaux, Carole, Froment, Carine, Lebaron, Simon, O'Donohue, Marie-Françoise, Kutay, Ulrike, Marcoux, Julien, Gleizes, Pierre-Emmanuel, Plisson-Chastang, Celia·2021·eLife
DOI 10.7554/elife.61254PMC PMC8112863

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Abstract

Preventing premature interaction of pre-ribosomes with the translation apparatus is essential for translational accuracy. Hence, the final maturation step releasing functional 40S ribosomal subunits, namely processing of the 18S ribosomal RNA 3′ end, is safeguarded by the 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-electron microscopy analysis of late human pre-40S particles purified using a catalytically inactive form of the 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., Froment, 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)
  • Molecular, Cellular and Developmental Biology department (MCD), Centre de Biologie Integrative (CBI), University of Toulouse, CNRS, UPS, Toulouse, France
Corresponding author
Gleizes, Pierre-Emmanuel
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2021-04-28
Volume
10
Pages
e61254
ISSN
2050-084X (ISSN-L)
DOI
10.7554/elife.61254
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
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
  • Agence Nationale de la Recherche (16-CE11-0029, ANR RIBOMAN)
  • Swiss National Science Foundation (31003A_166565)
  • CALMIP (2018-[P1406]))
  • iNEXT (PID3684 - VID 5784)
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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