Evidence map›Paper›PMID 18021395›Full record

ArticleBMC evolutionary biology2007

The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin.

Brigitte Boxma, Guenola Ricard, Angela H A M van Hoek, Edouard Severing, Seung-Yeo Moon-van der Staay, Georg W M van der Staay, Theo A van Alen, Rob M de Graaf, Geert Cremers, Michiel Kwantes and 7 more

Open access · goldAbstract read
In one paragraph

Article in BMC evolutionary biology, 2007. 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
2.3field-weighted citation impact, top 13% 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, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Diversity and origins of anaerobic metabolism in mitochondria and related organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  9. The Role of Ciliate Protozoa in the Rumen.Frontiers in microbiology · 2015
    Review
  10. Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  11. Article
  12. Review
  13. Rewiring and regulation of cross-compartmentalized metabolism in protists.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Review
  14. The hydrogenosomes of Psalteriomonas lanterna.BMC evolutionary biology · 2009
    Article
  15. 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

17 authors at 7 institutions in 5 countries.

Brigitte BoxmaDepartment of Evolutionary Microbiology, Faculty of Science, Radboud University Nijmegen, Toernooiveld 1, NL-6525 ED Nijmegen, The Netherlands. Brigitte.Boxma@intervet.com
Guenola Ricard
Angela H A M van Hoek
Edouard Severing
Seung-Yeo Moon-van der Staay
Georg W M van der Staay
Theo A van Alen
Rob M de Graaf
Geert Cremers
Michiel Kwantes
Neil R McEwan
C Jamie Newbold
Jean-Pierre Jouany
Tadeusz Michalowski
Peter Pristas
Martijn A Huynen
Johannes H P Hackstein
Radboud University Nijmegen · NLAberystwyth University · GBRadboud University Medical Center · NLInstitute of Animal Physiology of the Slovak Academy of Sciences · SKKielanowski Institute of Animal Physiology and Nutrition · PLTiFN · NLUnité Mixte de Recherche sur les Herbivores · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe hydrogenosomes of the anaerobic ciliate Nyctotherus ovalis show how mitochondria can evolve into hydrogenosomes because they possess a mitochondrial genome and parts of an electron-transport chain on the one hand, and a hydrogenase on the other hand. The hydrogenase permits direct reoxidation of NADH because it consists of a [FeFe] hydrogenase module that is fused to two modules, which are homologous to the 24 kDa and the 51 kDa subunits of a mitochondrial complex I.

resultsThe [FeFe] hydrogenase belongs to a clade of hydrogenases that are different from well-known eukaryotic hydrogenases. The 24 kDa and the 51 kDa modules are most closely related to homologous modules that function in bacterial [NiFe] hydrogenases. Paralogous, mitochondrial 24 kDa and 51 kDa modules function in the mitochondrial complex I in N. ovalis. The different hydrogenase modules have been fused to form a polyprotein that is targeted into the hydrogenosome.

conclusionThe hydrogenase and their associated modules have most likely been acquired by independent lateral gene transfer from different sources. This scenario for a concerted lateral gene transfer is in agreement with the evolution of the hydrogenosome from a genuine ciliate mitochondrion by evolutionary tinkering.

Indexed as

AnimalsChimeraCiliophoraElectron Transport Complex IEvolution, MolecularGene Transfer, HorizontalGenome, MitochondrialGenome, ProtozoanHydrogenaseIron-Sulfur ProteinsPhylogenySequence AlignmentSequence Homology, Amino AcidElectron Transport Complex IHydrogenaseiron hydrogenaseIron-Sulfur Proteins

Identifiers

PMID18021395
PMCPMC2216082
OpenAlexW2050794004

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Registered trials

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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.