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

Brigitte Boxma, Guenola Ricard, Angela Ham 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, Charles James Newbold, Jean-Pierre Jouany, Tadeusz Michalowski, Peter Pristas, Martijn A. Huynen, Johannes H. P. Hackstein

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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
Article number230
Number of pages12
JournalBMC Evolutionary Biology
Publication statusPublished - 16 Nov 2007


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