Evidence map›Paper›PMID 25314960›Full record

ArticleNature communications2014

Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion.

Yan Ge, Albena Draycheva, Thomas Bornemann, Marina V Rodnina, Wolfgang Wintermeyer

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023
    Review
  6. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  7. Article
  8. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  9. Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021
    Review
  10. 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
  11. Article
  12. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  13. Article
  14. Article
  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

5 authors.

Yan GeDepartment of Physical Biochemistry, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Albena DraychevaDepartment of Physical Biochemistry, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Thomas BornemannDepartment of Physical Biochemistry, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Wolfgang WintermeyerDepartment of Physical Biochemistry, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are co-translationally inserted into the bacterial plasma membrane via the SecYEG translocon by lateral release of hydrophobic transmembrane segments into the phospholipid bilayer. The trigger for lateral opening of the translocon is not known. Here we monitor lateral opening by photo-induced electron transfer (PET) between two fluorophores attached to the two SecY helices at the rim of the gate. In the resting translocon, the fluorescence is quenched, consistent with a closed conformation. Ribosome binding to the translocon diminishes PET quenching, indicating opening of the gate. The effect is larger with ribosomes exposing hydrophobic transmembrane segments and vanishes at low temperature. We propose a temperature-dependent dynamic equilibrium between closed and open conformations of the translocon that is shifted towards partially and fully open by ribosome binding and insertion of a hydrophobic peptide, respectively. The combined effects of ribosome and peptide binding allow for co-translational membrane insertion of successive transmembrane segments.

Indexed as

Bacterial ProteinsElectron TransportFluorescent DyesMethanocaldococcusProtein Sorting SignalsRibosomesBacterial ProteinsFluorescent DyesProtein Sorting Signals

Identifiers

PMID25314960
PMCPMC4218953

What OpenQuestion holds

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Registered trials

None linked

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.