Evidence map›Paper›PMID 25558985›Full record

ArticleNature structural & molecular biology2015

Charge-driven dynamics of nascent-chain movement through the SecYEG translocon.

Nurzian Ismail, Rickard Hedman, Martin Lindén, Gunnar von Heijne

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Spatially regulated mRNA translation enables functional membrane protein integration in synthetic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  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. Review
  10. Article
  11. Cotranslational folding and assembly of the dimericProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    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

4 authors.

Nurzian Ismail *Center for Biomembrane Research, Department of Biochemistry and Biophysics Stockholm University, Stockholm, Sweden.
Rickard Hedman *Center for Biomembrane Research, Department of Biochemistry and Biophysics Stockholm University, Stockholm, Sweden.
Martin LindénCenter for Biomembrane Research, Department of Biochemistry and Biophysics Stockholm University, Stockholm, Sweden.
Gunnar von HeijneCenter for Biomembrane Research, Department of Biochemistry and Biophysics Stockholm University, Stockholm, Sweden.

Funding

European Research Council 232648
6 · The paper itself

Abstract

On average, every fifth residue in secretory proteins carries either a positive or a negative charge. In a bacterium such as Escherichia coli, charged residues are exposed to an electric field as they transit through the inner membrane, and this should generate a fluctuating electric force on a translocating nascent chain. Here, we have used translational arrest peptides as in vivo force sensors to measure this electric force during cotranslational chain translocation through the SecYEG translocon. We find that charged residues experience a biphasic electric force as they move across the membrane, including an early component with a maximum when they are 47-49 residues away from the ribosomal P site, followed by a more slowly varying component. The early component is generated by the transmembrane electric potential, whereas the second may reflect interactions between charged residues and the periplasmic membrane surface.

Indexed as

Cell MembraneEscherichia coliEscherichia coli ProteinsMembrane PotentialsMembrane ProteinsProtein TransportSEC Translocation ChannelsEscherichia coli ProteinsMembrane ProteinsSecE protein, E coliSecG protein, E coliSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID25558985
PMCPMC4338579

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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.