Evidence map›Paper›PMID 39041433›Full record

ArticleNucleic acids research2024

Ribosomal protein RPL39L is an efficiency factor in the cotranslational folding of a subset of proteins with alpha helical domains.

Arka Banerjee, Meric Ataman, Maciej Jerzy Smialek, Debdatto Mookherjee, Julius Rabl, Aleksei Mironov, Lea Mues, Ludovic Enkler, Mairene Coto-Llerena, Alexander Schmidt and 5 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Functional Characterization and Heterogeneity Analysis of Ribosomal Proteins in Mouse Preimplantation Embryos.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  11. Article
  12. Ribosomal protein paralogues in ribosome specialization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  13. Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  14. Article
  15. Article
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

15 authors.

Arka BanerjeeBiozentrum, University of Basel, Basel, Switzerland.
Meric AtamanBiozentrum, University of Basel, Basel, Switzerland.
Maciej Jerzy SmialekBiozentrum, University of Basel, Basel, Switzerland.
Debdatto MookherjeeBiozentrum, University of Basel, Basel, Switzerland.
Julius RablCryo-EM Knowledge Hub (CEMK), ETH Zürich, Switzerland.
Aleksei MironovBiozentrum, University of Basel, Basel, Switzerland.
Lea MuesBiozentrum, University of Basel, Basel, Switzerland.
Ludovic EnklerBiozentrum, University of Basel, Basel, Switzerland.
Mairene Coto-LlerenaInstitute of Medical Genetics and Pathology, University Hospital Basel, University of Basel, Switzerland.
Alexander SchmidtBiozentrum, University of Basel, Basel, Switzerland.
Daniel BoehringerCryo-EM Knowledge Hub (CEMK), ETH Zürich, Switzerland.
Salvatore PiscuoglioInstitute of Medical Genetics and Pathology, University Hospital Basel, University of Basel, Switzerland.
Anne SpangBiozentrum, University of Basel, Basel, Switzerland.
Nitish MittalBiozentrum, University of Basel, Basel, Switzerland.
Mihaela ZavolanBiozentrum, University of Basel, Basel, Switzerland.ORCID 0000-0002-8832-2041

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 51NF40_141735
6 · The paper itself

Abstract

Increasingly many studies reveal how ribosome composition can be tuned to optimally translate the transcriptome of individual cell types. In this study, we investigated the expression pattern, structure within the ribosome and effect on protein synthesis of the ribosomal protein paralog 39L (RPL39L). With a novel mass spectrometric approach we revealed the expression of RPL39L protein beyond mouse germ cells, in human pluripotent cells, cancer cell lines and tissue samples. We generated RPL39L knock-out mouse embryonic stem cell (mESC) lines and demonstrated that RPL39L impacts the dynamics of translation, to support the pluripotency and differentiation, spontaneous and along the germ cell lineage. Most differences in protein abundance between WT and RPL39L KO lines were explained by widespread autophagy. By CryoEM analysis of purified RPL39 and RPL39L-containing ribosomes we found that, unlike RPL39, RPL39L has two distinct conformations in the exposed segment of the nascent peptide exit tunnel, creating a distinct hydrophobic patch that has been predicted to support the efficient co-translational folding of alpha helices. Our study shows that ribosomal protein paralogs provide switchable modular components that can tune translation to the protein production needs of individual cell types.

Indexed as

Protein BiosynthesisProtein FoldingRibosomal ProteinsRibosomesAnimalsCell DifferentiationHumansMiceMice, KnockoutMouse Embryonic Stem CellsProtein Conformation, alpha-HelicalRibosomal Proteins

Identifiers

PMID39041433
PMCPMC11347166

What Socratic holds

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Registered trials

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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 Socratic graph.