Evidence map›Paper›PMID 32311161›Full record

ArticleThe EMBO journal2020

Co-translational insertion and topogenesis of bacterial membrane proteins monitored in real time.

Evan Mercier, Wolfgang Wintermeyer, Marina V Rodnina

Abstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024
    Review
  11. Article
  12. Review
  13. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  14. Article
  15. 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
  16. Article
  17. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  18. Article
  19. 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

3 authors.

Evan MercierDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Wolfgang WintermeyerDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-0105-3879

Funding

Deutsche Forschungsgemeinschaft (DFG) SFB1190
6 · The paper itself

Abstract

Integral membrane proteins insert into the bacterial inner membrane co-translationally via the translocon. Transmembrane (TM) segments of nascent proteins adopt their native topological arrangement with the N-terminus of the first TM (TM1) oriented to the outside (type I) or the inside (type II) of the cell. Here, we study TM1 topogenesis during ongoing translation in a bacterial in vitro system, applying real-time FRET and protease protection assays. We find that TM1 of the type I protein LepB reaches the translocon immediately upon emerging from the ribosome. In contrast, the type II protein EmrD requires a longer nascent chain before TM1 reaches the translocon and adopts its topology by looping inside the ribosomal peptide exit tunnel. Looping presumably is mediated by interactions between positive charges at the N-terminus of TM1 and negative charges in the tunnel wall. Early TM1 inversion is abrogated by charge reversal at the N-terminus. Kinetic analysis also shows that co-translational membrane insertion of TM1 is intrinsically rapid and rate-limited by translation. Thus, the ribosome has an important role in membrane protein topogenesis.

Indexed as

Fluorescence Resonance Energy TransferProtein BiosynthesisEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsEmrD protein, E coliEscherichia coli ProteinsMembrane Transport ProteinsIn vitro translationpositive-inside rulereal-time translation kineticsribosometransmembrane segment inversion

Identifiers

PMID32311161
PMCPMC7396858

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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.