Reference : The atypical subunit composition of respiratory complexes I and IV is associated with...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Phytobiology (plant sciences, forestry, mycology...)
The atypical subunit composition of respiratory complexes I and IV is associated with original extra structural domains in Euglena gracilis.
Miranda-Astudillo, H. V. [> >]
Yadav, K. N. S. [> >]
Colina-Tenorio, L. [> >]
Bouillenne, Fabrice [Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines >]
Degand, H. [> >]
Morsomme, P. [> >]
Boekema, E. J. [> >]
Cardol, Pierre mailto [Université de Liège - ULiège > Département des sciences de la vie > Génétique et physiologie des microalgues >]
Scientific Reports
Yes (verified by ORBi)
United Kingdom
[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.
H2020 ; 682580 - BEAL - Bioenergetics in microalgae : regulation modes of mitochondrial respiration, photosynthesis, and fermentative pathways, and their interactions in secondary algae

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