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, Neil R McEwan, C Jamie Newbold, Jean-Pierre Jouany, Tadeusz Michalowski, Peter Pristas, Martijn A Huynen, Johannes H P Hackstein

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

BACKGROUND: The 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.

RESULTS: The [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.

CONCLUSION: The 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.

Original languageEnglish
Pages (from-to)230
JournalBMC Evolutionary Biology
Volume7
DOIs
Publication statusPrint publication - 16 Nov 2007
Externally publishedYes

Keywords

  • Animals
  • Chimera/genetics
  • Ciliophora/enzymology
  • Electron Transport Complex I/genetics
  • Evolution, Molecular
  • Gene Transfer, Horizontal
  • Genome, Mitochondrial
  • Genome, Protozoan
  • Hydrogenase/genetics
  • Iron-Sulfur Proteins/genetics
  • Phylogeny
  • Sequence Alignment
  • Sequence Homology, Amino Acid

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  • Cite this

    Boxma, B., Ricard, G., van Hoek, A. H. A. M., Severing, E., Moon-van der Staay, S-Y., van der Staay, G. W. M., van Alen, T. A., de Graaf, R. M., Cremers, G., Kwantes, M., McEwan, N. R., Newbold, C. J., Jouany, J-P., Michalowski, T., Pristas, P., Huynen, M. A., & Hackstein, J. H. P. (2007). The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin. BMC Evolutionary Biology, 7, 230. https://doi.org/10.1186/1471-2148-7-230