Evidence map›Paper›PMID 21680715›Full record

ArticleMolecular biology of the cell2011

Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex.

David A Stroud, Thomas Becker, Jian Qiu, Diana Stojanovski, Sylvia Pfannschmidt, Christophe Wirth, Carola Hunte, Bernard Guiard, Chris Meisinger, Nikolaus Pfanner and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. 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
2.3field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  16. The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Review
  18. Article
  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

11 authors at 2 institutions in 3 countries.

David A StroudInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany.
Thomas Becker
Jian Qiu
Diana Stojanovski
Sylvia Pfannschmidt
Christophe Wirth
Carola Hunte
Bernard Guiard
Chris Meisinger
Nikolaus Pfanner
Nils Wiedemann
University of Freiburg · DECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of β-barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belongs to the BamA/Sam50/Toc75 family of proteins that have been conserved from Gram-negative bacteria to mitochondria and chloroplasts. These proteins contain one or more N-terminal polypeptide transport-associated (POTRA) domains. POTRA domains can bind precursor proteins, however, different views exist on the role of POTRA domains in the biogenesis of β-barrel proteins. It has been suggested that the single POTRA domain of mitochondrial Sam50 plays a receptor-like function at the SAM complex. We established a system to monitor the interaction of chemical amounts of β-barrel precursor proteins with the SAM complex of wild-type and mutant yeast in organello. We report that the SAM complex lacking the POTRA domain of Sam50 efficiently binds β-barrel precursors, but is impaired in the release of the precursors. These results indicate the POTRA domain of Sam50 is not essential for recognition of β-barrel precursors but functions in a subsequent step to promote the release of precursor proteins from the SAM complex.

Indexed as

Protein Sorting SignalsCell-Free SystemGene Knockout TechniquesMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsMultiprotein ComplexesMutant ProteinsPorinsProtein PrecursorsProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsMultiprotein ComplexesMutant ProteinsPorinsProtein PrecursorsProtein Sorting SignalsSaccharomyces cerevisiae ProteinsSam50 protein, S cerevisiae

Identifiers

PMID21680715
PMCPMC3154879
OpenAlexW2158747963

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.