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

B. Boxma, G. Ricard, A.H.A.M. van Hoek, E. Severing, S.Y. Moon-van der Staay, G.W.M. van der Staay, T.A. Alen, R.M. de Graaf, G. Cremers, M. Kwantes, N.R. McEwan, C.J. Newbold, J.P. Jouany, T. Michalowski, P. Pristas, M.A. Huynen, J.H.P. Hackstein

    Research output: Contribution to journalArticleAcademicpeer-review

    23 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
    Article number230
    Number of pages12
    JournalBMC Evolutionary Biology
    Volume7
    DOIs
    Publication statusPublished - 2007

    Keywords

    • multiple sequence alignment
    • complex-i
    • phylogenetic analysis
    • eukaryotic evolution
    • iron hydrogenases
    • life-style
    • hydrogenosomes
    • mitochondria
    • protein
    • models

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