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

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dc.contributor.author van Hoek, A. H.
dc.contributor.author Jouany, Jean-Pierre
dc.contributor.author al, et
dc.contributor.author Boxma, B.
dc.contributor.author Pristas, P.
dc.contributor.author Newbold, C. James
dc.contributor.author Severing, E.
dc.contributor.author McEwan, Neil R.
dc.contributor.author Huynen, M. A.
dc.contributor.author Ricard, G.
dc.contributor.author Michalowski, T.
dc.date.accessioned 2009-07-08T14:44:59Z
dc.date.available 2009-07-08T14:44:59Z
dc.date.issued 2009-07-08
dc.identifier.citation van Hoek , A H , Jouany , J-P , al , Boxma , B , Pristas , P , Newbold , C J , Severing , E , McEwan , N R , Huynen , M A , Ricard , G & Michalowski , T 2009 , ' The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin ' Unknown Journal . en
dc.identifier.other PURE: 116651
dc.identifier.other dspace: 2160/2572
dc.identifier.uri http://hdl.handle.net/2160/2572
dc.description 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, paper no. 230. en
dc.description.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. en
dc.language.iso eng
dc.relation.ispartof Unknown Journal en
dc.title The [FeFe] hydrogenase of Nyctotherus ovalis has a chimeric origin en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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