Evidence map›Paper›PMID 35231030›Full record

ArticlePLoS biology2022

The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.

Büsra Güngör, Tamara Flohr, Sriram G Garg, Johannes M Herrmann

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
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  7. Review
  8. Article
  9. Article
  10. EMC rectifies the topology of multipass membrane proteins.Nature structural & molecular biology · 2024
    Article
  11. Article
  12. The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023
    Review
  13. Article
  14. Article
  15. Article
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  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Büsra GüngörCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-9179-973X
Tamara FlohrCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-8775-7959
Sriram G GargInstitute for Molecular Evolution, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0003-2081-4506
University of Kaiserslautern · DEHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two multisubunit protein complexes for membrane protein insertion were recently identified in the endoplasmic reticulum (ER): the guided entry of tail anchor proteins (GET) complex and ER membrane complex (EMC). The structures of both of their hydrophobic core subunits, which are required for the insertion reaction, revealed an overall similarity to the YidC/Oxa1/Alb3 family members found in bacteria, mitochondria, and chloroplasts. This suggests that these membrane insertion machineries all share a common ancestry. To test whether these ER proteins can functionally replace Oxa1 in yeast mitochondria, we generated strains that express mitochondria-targeted Get2-Get1 and Emc6-Emc3 fusion proteins in Oxa1 deletion mutants. Interestingly, the Emc6-Emc3 fusion was able to complement an Δoxa1 mutant and restored its respiratory competence. The Emc6-Emc3 fusion promoted the insertion of the mitochondrially encoded protein Cox2, as well as of nuclear encoded inner membrane proteins, although was not able to facilitate the assembly of the Atp9 ring. Our observations indicate that protein insertion into the ER is functionally conserved to the insertion mechanism in bacteria and mitochondria and adheres to similar topological principles.

Indexed as

Amino Acid SequenceCell RespirationElectron Transport Complex IVEndoplasmic ReticulumMembrane ProteinsMitochondriaMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesMutationNuclear ProteinsPhylogenyProtein BiosynthesisProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidElectron Transport Complex IVMembrane ProteinsMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesNuclear ProteinsOXA1 proteinSaccharomyces cerevisiae Proteins

Identifiers

PMID35231030
PMCPMC8887752
OpenAlexW4214736319

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.