Evidence map›Paper›PMID 29330366›Full record

ArticleScientific reports2018

Each protomer of a dimeric YidC functions as a single membrane insertase.

Dirk Spann, Eva Pross, Yuanyuan Chen, Ross E Dalbey, Andreas Kuhn

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. YidC fromBiomolecules · 2023
    Article
  4. Article
  5. Article
  6. 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
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
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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 at 2 institutions in 2 countries.

Dirk SpannInstitute of Microbiology and Molecular Biology, University of Hohenheim, 70599, Stuttgart, Germany.
Eva ProssInstitute of Microbiology and Molecular Biology, University of Hohenheim, 70599, Stuttgart, Germany.
Yuanyuan ChenDepartment of Chemistry and Biochemistry, Ohio State University, Columbus OH, 43210, USA.
Ross E DalbeyDepartment of Chemistry and Biochemistry, Ohio State University, Columbus OH, 43210, USA.
Andreas KuhnInstitute of Microbiology and Molecular Biology, University of Hohenheim, 70599, Stuttgart, Germany. Andreas.Kuhn@uni-hohenheim.de.
University of Hohenheim · DEThe Ohio State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane insertase YidC catalyzes the entrance of newly synthesized proteins into the lipid bilayer. As an integral membrane protein itself, YidC can be found as a monomer, a dimer or also as a member of the holotranslocase SecYEGDF-YajC-YidC. To investigate whether the dimeric YidC is functional and whether two copies cooperate to insert a single substrate, we constructed a fusion protein where two copies of YidC are connected by a short linker peptide. The 120 kDa protein is stable and functional as it supports the membrane insertion of the M13 procoat protein, the C-tailed protein SciP and the fusion protein Pf3-Lep. Mutations that inhibit either protomer do not inactivate the insertase and rather keep it functional. When both protomers are defective, the substrate proteins accumulate in the cytoplasm. This suggests that the dimeric YidC operates as two insertases. Consistent with this, we show that the dimeric YidC can bind two substrate proteins simultaneously, suggesting that YidC indeed functions as a monomer.

Indexed as

MutationEnzyme StabilityEscherichia coliEscherichia coli ProteinsLipid BilayersMembrane Transport ProteinsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationRecombinant Fusion ProteinsEscherichia coli ProteinsLipid BilayersMembrane Transport ProteinsRecombinant Fusion ProteinsYIDC protein, E coli

Identifiers

PMID29330366
PMCPMC5766580
OpenAlexW2783287538

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.