Evidence map›Paper›PMID 27929371›Full record

ArticleeLife2016

Prefabrication of a ribosomal protein subcomplex essential for eukaryotic ribosome formation.

Cohue Peña, Sabina Schütz, Ute Fischer, Yiming Chang, Vikram G Panse

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Signal Transduction in Ribosome Biogenesis: A Recipe to Avoid Disaster.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Eukaryotic ribosome assembly, transport and quality control.Nature structural & molecular biology · 2017
    Review
  20. 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

5 authors.

Cohue PeñaInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Sabina SchützInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Ute FischerInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Yiming ChangInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Vikram G PanseInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.ORCID 0000-0001-7950-5746

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spatial clustering of ribosomal proteins (r-proteins) through tertiary interactions is a striking structural feature of the eukaryotic ribosome. However, the functional importance of these intricate inter-connections, and how they are established is currently unclear. Here, we reveal that a conserved ATPase, Fap7, organizes interactions between neighboring r-proteins uS11 and eS26 prior to their delivery to the earliest ribosome precursor, the 90S. In vitro, uS11 only when bound to Fap7 becomes competent to recruit eS26 through tertiary contacts found between these r-proteins on the mature ribosome. Subsequently, Fap7 ATPase activity unloads the uS11:eS26 subcomplex onto its rRNA binding site, and therefore ensures stoichiometric integration of these r-proteins into the 90S. Fap7-depletion in vivo renders uS11 susceptible to proteolysis, and precludes eS26 incorporation into the 90S. Thus, prefabrication of a native-like r-protein subcomplex drives efficient and accurate construction of the eukaryotic ribosome.

Indexed as

Protein MultimerizationAdenylate KinaseMacromolecular SubstancesNuclear ProteinsNucleoside-TriphosphataseRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenylate KinaseFAP7 protein, S cerevisiaeMacromolecular SubstancesNuclear ProteinsNucleoside-TriphosphataseRibosomal Proteinsribosomal protein S11RPS26A protein, S cerevisiaeSaccharomyces cerevisiae ProteinsATPasesbiochemistryeukaryotic ribosomal proteinsFap7protein complexesribosome assemblyS. cerevisiaeTsr2

Identifiers

PMID27929371
PMCPMC5148605

What OpenQuestion 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 OpenQuestion graph.