Reference : The atypical subunit composition of respiratory complexes I and IV is associated with...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/226521
The atypical subunit composition of respiratory complexes I and IV is associated with original extra structural domains in Euglena gracilis.
English
Miranda Astudillo, Héctor Vicente mailto [Université de Liège - ULiège > Département des sciences de la vie > Génétique et physiologie des microalgues >]
Yadav, Sathish [University of Groningen > Groningen Biological Sciences and Biotechnology Institute > Department ofElectron Microscopy > >]
Colina-Tenorio, Lilia [Universidad Nacional Autónoma de México > Instituto de Fisiología Celular > Departamento de Genética Molecular > >]
Bouillenne, Fabrice [University of Liège > InBioS/Centre for Protein Engineering > > >]
Degand, Hervé [Université Catholique de Louvain, Louvain-la-Neuve > Institut des Sciences de la Vie > > >]
Morsomme, Pierre [Université Catholique de Louvain, Louvain-la-Neuve > Institut des Sciences de la Vie > > >]
Boekema, Egbert [University of Groningen > Groningen Biological Sciences and Biotechnology Institute > Department ofElectron Microscopy > >]
Cardol, Pierre mailto [Université de Liège - ULiège > Département des sciences de la vie > Génétique et physiologie des microalgues > >]
26-Jun-2018
Scientific Reports
Nature
8
1
9698
Yes (verified by ORBi)
International
2045-2322
[en] In mitochondrial oxidative phosphorylation, electron transfer from NADH or succinate to oxygen by a series of large protein complexes in the inner mitochondrial membrane (complexes I-IV) is coupled to the generation of an electrochemical proton gradient, the energy of which is utilized by complex V to generate ATP. In Euglena gracilis, a non-parasitic secondary green alga related to trypanosomes, these respiratory complexes totalize more than 40 Euglenozoa-specific subunits along with about 50 classical subunits described in other eukaryotes. In the present study the Euglena proton-pumping complexes I, III, and IV were purified from isolated mitochondria by a two-steps liquid chromatography approach. Their atypical subunit composition was further resolved and confirmed using a three-steps PAGE analysis coupled to mass spectrometry identification of peptides. The purified complexes were also observed by electron microscopy followed by single-particle analysis. Even if the overall structures of the three oxidases are similar to the structure of canonical enzymes (e.g. from mammals), additional atypical domains were observed in complexes I and IV: an extra domain located at the tip of the peripheral arm of complex I and a "helmet-like" domain on the top of the cytochrome c binding region in complex IV.
http://hdl.handle.net/2268/226521
10.1038/s41598-018-28039-z

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