TY - JOUR
T1 - The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin
AU - Boxma, Brigitte
AU - Ricard, Guenola
AU - van Hoek, Angela H A M
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, C Jamie
AU - Jouany, Jean-Pierre
AU - Michalowski, Tadeusz
AU - Pristas, Peter
AU - Huynen, Martijn A
AU - Hackstein, Johannes H P
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.
KW - Animals
KW - Chimera/genetics
KW - Ciliophora/enzymology
KW - Electron Transport Complex I/genetics
KW - Evolution, Molecular
KW - Gene Transfer, Horizontal
KW - Genome, Mitochondrial
KW - Genome, Protozoan
KW - Hydrogenase/genetics
KW - Iron-Sulfur Proteins/genetics
KW - Phylogeny
KW - Sequence Alignment
KW - Sequence Homology, Amino Acid
U2 - 10.1186/1471-2148-7-230
DO - 10.1186/1471-2148-7-230
M3 - Article
C2 - 18021395
SN - 1471-2148
VL - 7
SP - 230
JO - BMC Evolutionary Biology
JF - BMC Evolutionary Biology
ER -