Evidence map›Paper›PMID 28273911›Full record

ArticleScientific reports2017

YidC and SecYEG form a heterotetrameric protein translocation channel.

Ilie Sachelaru, Lukas Winter, Denis G Knyazev, Mirjam Zimmermann, Andreas Vogt, Roland Kuttner, Nicole Ollinger, Christine Siligan, Peter Pohl, Hans-Georg Koch

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Review
  2. Review
  3. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. YidC fromBiomolecules · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  13. Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
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.

Ilie SachelaruInstitut für Biochemie und Molekularbiologie, ZBMZ, Faculty of Medicine, Albert-Ludwigs-Universität Freiburg, Stefan Meier Str. 17, Freiburg, 79104, Germany.
Lukas WinterInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Denis G KnyazevInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Mirjam ZimmermannInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Andreas VogtInstitut für Biochemie und Molekularbiologie, ZBMZ, Faculty of Medicine, Albert-Ludwigs-Universität Freiburg, Stefan Meier Str. 17, Freiburg, 79104, Germany.
Roland KuttnerInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Nicole OllingerInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Christine SiliganInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria.
Peter PohlInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, A-4020, Linz, Austria. Peter.Pohl@jku.at.ORCID 0000-0002-1792-2314
Hans-Georg KochInstitut für Biochemie und Molekularbiologie, ZBMZ, Faculty of Medicine, Albert-Ludwigs-Universität Freiburg, Stefan Meier Str. 17, Freiburg, 79104, Germany. Hans-Georg.Koch@biochemie.uni-freiburg.de.

Funding

Austrian Science Fund FWF P 28213Austrian Science Fund FWF W 1250
6 · The paper itself

Abstract

The heterotrimeric SecYEG complex cooperates with YidC to facilitate membrane protein insertion by an unknown mechanism. Here we show that YidC contacts the interior of the SecY channel resulting in a ligand-activated and voltage-dependent complex with distinct ion channel characteristics. The SecYEG pore diameter decreases from 8 Å to only 5 Å for the YidC-SecYEG pore, indicating a reduction in channel cross-section by YidC intercalation. In the presence of a substrate, YidC relocates to the rim of the pore as indicated by increased pore diameter and loss of YidC crosslinks to the channel interior. Changing the surface charge of the pore by incorporating YidC into the channel wall increases the anion selectivity, and the accompanying change in wall hydrophobicity is liable to alter the partition of helices from the pore into the membrane. This could explain how the exit of transmembrane domains from the SecY channel is facilitated by YidC.

Indexed as

Escherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationProtein Translocation SystemsSEC Translocation ChannelsEscherichia coli ProteinsMembrane Transport ProteinsProtein Translocation SystemsSEC Translocation ChannelsYIDC protein, E coli

Identifiers

PMID28273911
PMCPMC5427846

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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.