Evidence map›Paper›PMID 27974208›Full record

ArticleCell reports2016

Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis.

Alexej Kedrov, Stephan Wickles, Alvaro H Crevenna, Eli O van der Sluis, Robert Buschauer, Otto Berninghausen, Don C Lamb, Roland Beckmann

Abstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  5. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

8 authors.

Alexej KedrovGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany. Electronic address: kedrov@genzentrum.lmu.de.
Stephan WicklesGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany.
Alvaro H CrevennaPhysical Chemistry, Department of Chemistry, Center for Nanoscience (CeNS), the NanoSystems Initiative Munich (NIM), Ludwig-Maximilians-University Munich, Butenandtstrasse 11, Munich 81377, Germany.
Eli O van der SluisGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany.
Robert BuschauerGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany.
Otto BerninghausenGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany.
Don C LambPhysical Chemistry, Department of Chemistry, Center for Nanoscience (CeNS), the NanoSystems Initiative Munich (NIM), Ludwig-Maximilians-University Munich, Butenandtstrasse 11, Munich 81377, Germany; Center for Integrated Protein Science Munich (CiPSM), Ludwig-Maximilians-University, Butenandtstrasse 5-13, Munich 81377, Germany.
Roland BeckmannGene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, Munich 81377, Germany; Center for Integrated Protein Science Munich (CiPSM), Ludwig-Maximilians-University, Butenandtstrasse 5-13, Munich 81377, Germany. Electronic address: beckmann@genzentrum.lmu.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the YidC/Oxa1/Alb3 family universally facilitate membrane protein biogenesis, via mechanisms that have thus far remained unclear. Here, we investigated two crucial functional aspects: the interaction of YidC with ribosome:nascent chain complexes (RNCs) and the structural dynamics of RNC-bound YidC in nanodiscs. We observed that a fully exposed nascent transmembrane domain (TMD) is required for high-affinity YidC:RNC interactions, while weaker binding may already occur at earlier stages of translation. YidC efficiently catalyzed the membrane insertion of nascent TMDs in both fluid and gel phase membranes. Cryo-electron microscopy and fluorescence analysis revealed a conformational change in YidC upon nascent chain insertion: the essential TMDs 2 and 3 of YidC were tilted, while the amphipathic helix EH1 relocated into the hydrophobic core of the membrane. We suggest that EH1 serves as a mechanical lever, facilitating a coordinated movement of YidC TMDs to trigger the release of nascent chains into the membrane.

Indexed as

Protein BiosynthesisCryoelectron MicroscopyElectron Transport Complex IVEscherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsMembrane Transport ProteinsMitochondrial ProteinsNuclear ProteinsProtein BindingRibosomesElectron Transport Complex IVEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinsMitochondrial ProteinsNuclear ProteinsOXA1 proteinYIDC protein, E colicryo-electron microscopyfluorescence correlation spectroscopyinsertasemacromolecular assemblymembrane proteinnanodisctranslocon

Identifiers

PMID27974208
PMCPMC5186731

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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.