Evidence map›Paper›PMID 27824037›Full record

ArticleNature communications2016

Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry.

Kristin Kiosze-Becker, Alessandro Ori, Milan Gerovac, André Heuer, Elina Nürenberg-Goloub, Umar Jan Rashid, Thomas Becker, Roland Beckmann, Martin Beck, Robert Tampé

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Mass Spectrometry- and Structural Biology-Based Investigation of Proteins.Advances in experimental medicine and biology · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Rebirth of the translational machinery: The importance of recycling ribosomes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Nonsense-Mediated mRNA Decay Begins Where Translation Ends.Cold Spring Harbor perspectives in biology · 2019
    Review
  19. Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    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

10 authors.

Kristin Kiosze-BeckerInstitute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt a.M., Germany.
Alessandro OriStructural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstr. 1, 69117 Heidelberg, Germany.
Milan GerovacInstitute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt a.M., Germany.
André HeuerGene Center and Center for Integrated Protein Science Munich (CiPSM), Department of Biochemistry, University of Munich, Feodor-Lynen-Str. 25, 81377 Munich, Germany.
Elina Nürenberg-GoloubInstitute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt a.M., Germany.
Umar Jan RashidInstitute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt a.M., Germany.
Thomas BeckerGene Center and Center for Integrated Protein Science Munich (CiPSM), Department of Biochemistry, University of Munich, Feodor-Lynen-Str. 25, 81377 Munich, Germany.
Roland BeckmannGene Center and Center for Integrated Protein Science Munich (CiPSM), Department of Biochemistry, University of Munich, Feodor-Lynen-Str. 25, 81377 Munich, Germany.
Martin BeckStructural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstr. 1, 69117 Heidelberg, Germany.ORCID 0000-0002-7397-1321
Robert TampéInstitute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt a.M., Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final-or the first-step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S·ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix-loop-helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling.

Indexed as

Archaeal ProteinsCross-Linking ReagentsIron-Sulfur ProteinsMass SpectrometryModels, MolecularRibosomal ProteinsRibosomesSulfolobus solfataricusArchaeal ProteinsCross-Linking ReagentsIron-Sulfur ProteinsRibosomal Proteins

Identifiers

PMID27824037
PMCPMC5105147

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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.