TY - JOUR
T1 - The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin
AU - Boxma, Brigitte
AU - Ricard, Guenola
AU - van Hoek, Angela Ham
AU - Severing, Edouard
AU - Moon-van der Staay, Seung-Yeo
AU - van der Staay, Georg W. M.
AU - van Alen, Theo A.
AU - de Graaf, Rob M.
AU - Cremers, Geert
AU - Kwantes, Michiel
AU - McEwan, Neil R.
AU - Newbold, Charles James
AU - Jouany, Jean-Pierre
AU - Michalowski, Tadeusz
AU - Pristas, Peter
AU - Huynen, Martijn A.
AU - Hackstein, Johannes H. P.
N1 - Boxma, B., Ricard, G., van Hoek, A. H., 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,article 230.
PY - 2007/11/16
Y1 - 2007/11/16
N2 - 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.
AB - 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.
UR - http://hdl.handle.net/2160/8877
U2 - 10.1186/1471-2148-7-230
DO - 10.1186/1471-2148-7-230
M3 - Article
SN - 1471-2148
VL - 7
JO - BMC Evolutionary Biology
JF - BMC Evolutionary Biology
M1 - 230
ER -