Evidence map›Paper›PMID 29284403›Full record

ArticleBMC genomics2017

The emerging picture of the mitochondrial protein import complexes of Amoebozoa supergroup.

Małgorzata Wojtkowska, Dorota Buczek, Yutaka Suzuki, Victoria Shabardina, Wojciech Makałowski, Hanna Kmita

Abstract read
In one paragraph

Article in BMC genomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Cell-Free DNA and Mitochondria in Parkinson's Disease.International journal of molecular sciences · 2025
    Review
  2. Lessons from the deep: mechanisms behind diversification of eukaryotic protein complexes.Biological reviews of the Cambridge Philosophical Society · 2023
    Article
  3. Article
  4. Review
  5. Article
  6. Unusual Occurrence of Two Bona-Fide CCA-Adding Enzymes inInternational journal of molecular sciences · 2020
    Article
4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Małgorzata WojtkowskaLaboratory of Bioenergetics, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, 61-614, Poznan, Poland. woytek@amu.edu.pl.ORCID 0000-0001-8526-1362
Dorota BuczekLaboratory of Bioenergetics, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, 61-614, Poznan, Poland.
Yutaka SuzukiDepartment of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Chiba, 277-8562, Japan.
Victoria ShabardinaInstitute of Bioinformatics, Faculty of Medicine, University of Muenster, Niels Stensen Strasse 14, 48149, Muenster, Germany.
Wojciech MakałowskiInstitute of Bioinformatics, Faculty of Medicine, University of Muenster, Niels Stensen Strasse 14, 48149, Muenster, Germany.
Hanna KmitaLaboratory of Bioenergetics, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, 61-614, Poznan, Poland.

Funding

Fundacja na rzecz Nauki Polskiej MPD/2010/3Polish Ministry of Science and Higher Education 01/KNOW2/2014
6 · The paper itself

Abstract

backgroundThe existence of mitochondria-related organelles (MROs) is proposed for eukaryotic organisms. The Amoebozoa includes some organisms that are known to have mitosomes but also organisms that have aerobic mitochondria. However, the mitochondrial protein apparatus of this supergroup remains largely unsampled, except for the mitochondrial outer membrane import complexes studied recently. Therefore, in this study we investigated the mitochondrial inner membrane and intermembrane space complexes, using the available genome and transcriptome sequences.

resultsWhen compared with the canonical cognate complexes described for the yeast Saccharomyces cerevisiae, amoebozoans with aerobic mitochondria, display lower differences in the number of subunits predicted for these complexes than the mitochondrial outer membrane complexes, although the predicted subunits appear to display different levels of diversity in regard to phylogenetic position and isoform numbers. For the putative mitosome-bearing amoebozoans, the number of predicted subunits suggests the complex elimination distinctly more pronounced than in the case of the outer membrane ones.

conclusionThe results concern the problem of mitochondrial and mitosome protein import machinery structural variability and the reduction of their complexity within the currently defined supergroup of Amoebozoa. This results are crucial for better understanding of the Amoebozoa taxa of both biomedical and evolutionary importance.

Indexed as

Acanthamoeba castellaniiAmoebozoaCells, CulturedDictyosteliumGene Expression ProfilingGenomicsMitochondrial Membrane Transport ProteinsPhylogenyProtein SubunitsMitochondrial Membrane Transport ProteinsProtein SubunitsAmoebozoaMIA complexMitochondriaMitosomesOXA complexPAM complexProtein importsmall TimsTIM22 complexTIM23 complex

Identifiers

PMID29284403
PMCPMC5747110

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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.