Evidence map›Paper›PMID 27436903›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Outer membrane protein functions as integrator of protein import and DNA inheritance in mitochondria.

Sandro Käser, Silke Oeljeklaus, Jiří Týč, Sue Vaughan, Bettina Warscheid, André Schneider

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Single p197 molecules of the mitochondrial genome segregation system ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  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

6 authors at 3 institutions in 3 countries.

Sandro KäserDepartment of Chemistry and Biochemistry, University of Bern, Bern CH-3012, Switzerland;
Silke OeljeklausDepartment of Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg 79104, Germany;
Jiří TýčDepartment of Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom;
Sue VaughanDepartment of Biological and Medical Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom;
Bettina WarscheidDepartment of Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg 79104, Germany; Centre for Biological Signalling Studies (BIOSS), University of Freiburg, Freiburg 79104, Germany andre.schneider@dcb.unibe.ch Bettina.warscheid@biologie.uni-freiburg.de.
André SchneiderDepartment of Chemistry and Biochemistry, University of Bern, Bern CH-3012, Switzerland; andre.schneider@dcb.unibe.ch Bettina.warscheid@biologie.uni-freiburg.de.
Oxford Brookes University · GBUniversity of Bern · CHUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trypanosomatids are one of the earliest diverging eukaryotes that have fully functional mitochondria. pATOM36 is a trypanosomatid-specific essential mitochondrial outer membrane protein that has been implicated in protein import. Changes in the mitochondrial proteome induced by ablation of pATOM36 and in vitro assays show that pATOM36 is required for the assembly of the archaic translocase of the outer membrane (ATOM), the functional analog of the TOM complex in other organisms. Reciprocal pull-down experiments and immunofluorescence analyses demonstrate that a fraction of pATOM36 interacts and colocalizes with TAC65, a previously uncharacterized essential component of the tripartite attachment complex (TAC). The TAC links the single-unit mitochondrial genome to the basal body of the flagellum and mediates the segregation of the replicated mitochondrial genomes. RNAi experiments show that pATOM36, in line with its dual localization, is not only essential for ATOM complex assembly but also for segregation of the replicated mitochondrial genomes. However, the two functions are distinct, as a truncated version of pATOM36 lacking the 75 C-terminal amino acids can rescue kinetoplast DNA missegregation but not the lack of ATOM complex assembly. Thus, pATOM36 has a dual function and integrates mitochondrial protein import with mitochondrial DNA inheritance.

Indexed as

Amino Acid SequenceCarrier ProteinsCell LineDNA, MitochondrialDNA, ProtozoanFlagellaGenome, MitochondrialMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtein TransportProtozoan ProteinsRNA InterferenceSequence Homology, Amino AcidTrypanosoma brucei bruceiCarrier ProteinsDNA, MitochondrialDNA, ProtozoanMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtozoan Proteinsevolutionmitochondriamitochondrial genomeprotein importtrypanosomes

Identifiers

PMID27436903
PMCPMC4978248
OpenAlexW2481126429

What OpenQuestion holds

Textmetadata
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.