Evidence map›Paper›PMID 31379073›Full record

ArticleEMBO reports2019

Partially inserted nascent chain unzips the lateral gate of the Sec translocon.

Lukas Kater, Benedikt Frieg, Otto Berninghausen, Holger Gohlke, Roland Beckmann, Alexej Kedrov

Abstract read
In one paragraph

Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  9. Article
  10. Article
  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. Article
  15. Article
  16. Article
  17. Article
  18. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Lukas KaterGene Center Munich, Ludwig-Maximilian-University, Munich, Germany.
Benedikt FriegJohn von Neumann Institute for Computing, Jülich Supercomputing Centre, Institute for Complex Systems - Structural Biochemistry (ICS-6), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0002-7877-0262
Otto BerninghausenGene Center Munich, Ludwig-Maximilian-University, Munich, Germany.
Holger GohlkeJohn von Neumann Institute for Computing, Jülich Supercomputing Centre, Institute for Complex Systems - Structural Biochemistry (ICS-6), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0001-8613-1447
Roland BeckmannGene Center Munich, Ludwig-Maximilian-University, Munich, Germany.ORCID 0000-0003-4291-3898
Alexej KedrovGene Center Munich, Ludwig-Maximilian-University, Munich, Germany.ORCID 0000-0001-9117-752X

Funding

Deutsche Forschungsgemeinschaft 267205415 (A03, A10)Deutsche Forschungsgemeinschaft INST 208/704-1 FUGGDeutsche Forschungsgemeinschaft KE1879/3-1EC|H2020|H2020 Priority Excellent Science|H2020 European Research Council (ERC) Cryotranslation
6 · The paper itself

Abstract

The Sec translocon provides the lipid bilayer entry for ribosome-bound nascent chains and thus facilitates membrane protein biogenesis. Despite the appreciated role of the native environment in the translocon:ribosome assembly, structural information on the complex in the lipid membrane is scarce. Here, we present a cryo-electron microscopy-based structure of bacterial translocon SecYEG in lipid nanodiscs and elucidate an early intermediate state upon insertion of the FtsQ anchor domain. Insertion of the short nascent chain causes initial displacements within the lateral gate of the translocon, where α-helices 2b, 7, and 8 tilt within the membrane core to "unzip" the gate at the cytoplasmic side. Molecular dynamics simulations demonstrate that the conformational change is reversed in the absence of the ribosome, and suggest that the accessory α-helices of SecE subunit modulate the lateral gate conformation. Site-specific cross-linking validates that the FtsQ nascent chain passes the lateral gate upon insertion. The structure and the biochemical data suggest that the partially inserted nascent chain remains highly flexible until it acquires the transmembrane topology.

Indexed as

Cryoelectron MicroscopyEscherichia coliFluorescent DyesLipid BilayersMolecular Dynamics SimulationPeptidesProtein ConformationRibosomesSEC Translocation ChannelsFluorescent DyesLipid BilayersPeptidesSEC Translocation Channelsmembrane protein insertionnanodiscnative environmentreconstitutionribosome

Identifiers

PMID31379073
PMCPMC6776908

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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.