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

被引:25
作者
Boxma, Brigitte [3 ,9 ]
Ricard, Guenola [1 ,2 ]
van Hoek, Angela Ham [3 ,8 ]
Severing, Edouard [3 ]
Moon-van der Staay, Seung-Yeo [3 ]
van der Staay, Georg W. M. [3 ]
van Alen, Theo A. [3 ]
de Graaf, Rob M. [3 ]
Cremers, Geert [3 ]
Kwantes, Michiel [3 ]
McEwan, Neil R. [4 ]
Newbold, C. Jamie [4 ]
Jouany, Jean-Pierre [5 ]
Michalowski, Tadeusz [6 ]
Pristas, Peter [7 ]
Huynen, Martijn A. [1 ,2 ]
Hackstein, Johannes H. P. [3 ]
机构
[1] Radboud Univ Nijmegen, Nijmegen Med Ctr, CMBI 260, Ctr Mol & Biomol Informat, NL-6500 HB Nijmegen, Netherlands
[2] Radboud Univ Nijmegen, Nijmegen Med Ctr, CMBI 260, NCMLS, NL-6500 HB Nijmegen, Netherlands
[3] Radboud Univ Nijmegen, Fac Sci, Dept Evolut Microbiol, NL-6525 ED Nijmegen, Netherlands
[4] Aberystwyth Univ, Inst Rural Sci, Aberystwyth SY23 3AL, Ceredigion, Wales
[5] INRA, UR1213 Herbivores, F-63122 St Genes Champanelle, France
[6] Polish Acad Sci, Kielanowski Inst Anim Physiol & Nutr, PL-05110 Jablonna, Poland
[7] Slovak Acad Sci, Inst Anim Physiol, SK-04001 Kosice, Slovakia
[8] RIKILT, Inst Food Safety, Wageningen UR, Netherlands
[9] Intervet Int, Boxmeer, Netherlands
关键词
D O I
10.1186/1471-2148-7-230
中图分类号
Q [生物科学];
学科分类号
07 [理学]; 0710 [生物学]; 09 [农学];
摘要
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.
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页数:12
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