Evidence map›Paper›PMID 21460184›Full record

ArticleMolecular biology of the cell2011

Mitochondria can recognize and assemble fragments of a beta-barrel structure.

Jonas E N Müller, Drazen Papic, Thomas Ulrich, Iwan Grin, Monika Schütz, Philipp Oberhettinger, Jan Tommassen, Dirk Linke, Kai S Dimmer, Ingo B Autenrieth and 1 more

Abstract 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 25% 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, 28 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Article
  7. Review
  8. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  9. Article
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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

11 authors at 3 institutions in 2 countries.

Jonas E N MüllerInterfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.
Drazen Papic
Thomas Ulrich
Iwan Grin
Monika Schütz
Philipp Oberhettinger
Jan Tommassen
Dirk Linke
Kai S Dimmer
Ingo B Autenrieth
Doron Rapaport
University of Tübingen · DEMax Planck Institute for Developmental Biology · DEUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-barrel proteins are found in the outer membranes of eukaryotic organelles of endosymbiotic origin as well as in the outer membrane of Gram-negative bacteria. Precursors of mitochondrial β-barrel proteins are synthesized in the cytosol and have to be targeted to the organelle. Currently, the signal that assures their specific targeting to mitochondria is poorly defined. To characterize the structural features needed for specific mitochondrial targeting and to test whether a full β-barrel structure is required, we expressed in yeast cells the β-barrel domain of the trimeric autotransporter Yersinia adhesin A (YadA). Trimeric autotransporters are found only in prokaryotes, where they are anchored to the outer membrane by a single 12-stranded β-barrel structure to which each monomer is contributing four β-strands. Importantly, we found that YadA is solely localized to the mitochondrial outer membrane, where it exists in a native trimeric conformation. These findings demonstrate that, rather than a linear sequence or a complete β-barrel structure, four β-strands are sufficient for the mitochondria to recognize and assemble a β-barrel protein. Remarkably, the evolutionary origin of mitochondria from bacteria enables them to import and assemble even proteins belonging to a class that is absent in eukaryotes.

Indexed as

Adhesins, BacterialMitochondriaMitochondrial MembranesModels, MolecularMolecular ChaperonesPeptide FragmentsProtein FoldingProtein MultimerizationProtein Sorting SignalsProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeAdhesins, BacterialMolecular ChaperonesPeptide FragmentsProtein Sorting SignalsRecombinant ProteinsYadA protein, Yersinia

Identifiers

PMID21460184
PMCPMC3093317
OpenAlexW1984491422

What OpenQuestion holds

Textmetadata
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.