Evidence map›Paper›PMID 34873152›Full record

ArticleNature communications2021

Monitoring the binding and insertion of a single transmembrane protein by an insertase.

Pawel R Laskowski, Kristyna Pluhackova, Maximilian Haase, Brian M Lang, Gisela Nagler, Andreas Kuhn, Daniel J Müller

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Factors modulating the assembly of human βNature structural & molecular biology · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  14. Article
  15. 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

7 authors at 2 institutions in 2 countries.

Pawel R LaskowskiDepartment of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-8118-9030
Kristyna PluhackovaDepartment of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-7498-6584
Maximilian HaaseMolecular Microbiology, Biology Institute, Universität Hohenheim, 70599, Stuttgart, Germany.
Brian M LangDepartment of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland.
Gisela NaglerMolecular Microbiology, Biology Institute, Universität Hohenheim, 70599, Stuttgart, Germany.
Andreas KuhnMolecular Microbiology, Biology Institute, Universität Hohenheim, 70599, Stuttgart, Germany.
Daniel J MüllerDepartment of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland. daniel.mueller@bsse.ethz.ch.ORCID http://orcid.org/0000-0003-3075-0665
ETH Zurich · CHUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells employ highly conserved families of insertases and translocases to insert and fold proteins into membranes. How insertases insert and fold membrane proteins is not fully known. To investigate how the bacterial insertase YidC facilitates this process, we here combine single-molecule force spectroscopy and fluorescence spectroscopy approaches, and molecular dynamics simulations. We observe that within 2 ms, the cytoplasmic α-helical hairpin of YidC binds the polypeptide of the membrane protein Pf3 at high conformational variability and kinetic stability. Within 52 ms, YidC strengthens its binding to the substrate and uses the cytoplasmic α-helical hairpin domain and hydrophilic groove to transfer Pf3 to the membrane-inserted, folded state. In this inserted state, Pf3 exposes low conformational variability such as typical for transmembrane α-helical proteins. The presence of YidC homologues in all domains of life gives our mechanistic insight into insertase-mediated membrane protein binding and insertion general relevance for membrane protein biogenesis.

Indexed as

AlgorithmsMolecular Dynamics SimulationCell MembraneEscherichia coliEscherichia coli ProteinsKineticsMembrane Transport ProteinsMicroscopy, Atomic ForceMicroscopy, ConfocalMutationProtein BindingProtein Conformation, alpha-HelicalSpectrometry, FluorescenceEscherichia coli ProteinsMembrane Transport ProteinsYIDC protein, E coli

Identifiers

PMID34873152
PMCPMC8648943
OpenAlexW4200174494

What OpenQuestion holds

Textmetadata
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.