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The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin |
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| Authors: | Brigitte Boxma Guenola Ricard Angela HAM van Hoek Edouard Severing Seung-Yeo Moon-van der Staay Georg WM 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 HP Hackstein |
| Affiliation: | 1. Department of Evolutionary Microbiology, Faculty of Science, Radboud University Nijmegen, Toernooiveld 1, NL-6525, Nijmegen, ED, The Netherlands 8. Intervet International, Boxmeer, The Netherlands 2. Nijmegen Centre for Molecular Life Sciences (NCMLS) and Center for Molecular and Biomolecular Informatics, CMBI 260, Radboud University Nijmegen Medical Centre, PO Box 9101, NL- 6500, Nijmegen, HB, The Netherlands 7. RIKILT – Institute of Food Safety, Wageningen, UR, The Netherlands 3. The Institute of Rural Science, University of Wales Aberystwyth, Llanbadarn Fawr, SY23 3AL, Aberystwyth, Ceredigion, Wales, UK 4. INRA, UR1213 Herbivores, St Genès Champanelle, F-63122, Theix, France 5. Kielanowski Institute of Animal Physiology and Nutrition, Polish Acedemy of Sciences, Instytucka 3, P-05-110, Jablonna, Warsaw, Poland 6. Institute of Animal Physiology, Slovak Academy of Sciences, Soltesovej 4, SK-040 01, Kosice, Slovakia |
| 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. |
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