Evidence map›Paper›PMID 33289941›Full record

ArticleThe EMBO journal2021

A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes.

Hanna Kratzat, Timur Mackens-Kiani, Michael Ameismeier, Mia Potocnjak, Jingdong Cheng, Estelle Dacheux, Abdelkader Namane, Otto Berninghausen, Franz Herzog, Micheline Fromont-Racine and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.7field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
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  5. A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026
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  11. eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

Hanna KratzatGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Timur Mackens-KianiGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Michael AmeismeierGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0002-1194-3448
Mia PotocnjakGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Jingdong ChengGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0003-4442-377X
Estelle DacheuxGénétique des Interactions Macromoléculaires, UMR3525 CNRS, Institut Pasteur, Paris, France.
Abdelkader NamaneGénétique des Interactions Macromoléculaires, UMR3525 CNRS, Institut Pasteur, Paris, France.ORCID 0000-0001-7180-7619
Otto BerninghausenGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Franz HerzogGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Micheline Fromont-RacineGénétique des Interactions Macromoléculaires, UMR3525 CNRS, Institut Pasteur, Paris, France.ORCID 0000-0001-9906-0334
Thomas BeckerGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0001-8458-2738
Roland BeckmannGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID 0000-0003-4291-3898
Center for Integrated Protein Science Munich · DECentre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (ANR) ANR-17-CE11-0049-01Agence Nationale de la Recherche (ANR) ANR-17-CE12-0024-02Deutsche Forschungsgemeinschaft (DFG) BE1814/15-1Deutsche Forschungsgemeinschaft (DFG) TRR174
6 · The paper itself

Abstract

In eukaryotic translation, termination and ribosome recycling phases are linked to subsequent initiation of a new round of translation by persistence of several factors at ribosomal sub-complexes. These comprise/include the large eIF3 complex, eIF3j (Hcr1 in yeast) and the ATP-binding cassette protein ABCE1 (Rli1 in yeast). The ATPase is mainly active as a recycling factor, but it can remain bound to the dissociated 40S subunit until formation of the next 43S pre-initiation complexes. However, its functional role and native architectural context remains largely enigmatic. Here, we present an architectural inventory of native yeast and human ABCE1-containing pre-initiation complexes by cryo-EM. We found that ABCE1 was mostly associated with early 43S, but also with later 48S phases of initiation. It adopted a novel hybrid conformation of its nucleotide-binding domains, while interacting with the N-terminus of eIF3j. Further, eIF3j occupied the mRNA entry channel via its ultimate C-terminus providing a structural explanation for its antagonistic role with respect to mRNA binding. Overall, the native human samples provide a near-complete molecular picture of the architecture and sophisticated interaction network of the 43S-bound eIF3 complex and the eIF2 ternary complex containing the initiator tRNA.

Indexed as

ATP-Binding Cassette TransportersCell LineDNA-Binding ProteinsEukaryotic Initiation Factor-2HEK293 CellsHumansProtein BindingProtein BiosynthesisRibosome Subunits, Small, EukaryoticRNA, MessengerRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsABCE1 protein, humanATP-Binding Cassette TransportersDNA-Binding ProteinsEukaryotic Initiation Factor-2RNA, MessengerRNA, TransferSaccharomyces cerevisiae ProteinsABCE1cryo-EMeIF3ribosome recyclingtranslation initiation

Identifiers

PMID33289941
PMCPMC7780240
OpenAlexW3112131467

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.