Reference : In Chlamydomonas, the Loss of Nd5 Subunit Prevents the Assembly of Whole Mitochondria...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/35187
In Chlamydomonas, the Loss of Nd5 Subunit Prevents the Assembly of Whole Mitochondrial Complex I and Leads to the Formation of a Low Abundant 700 Kda Subcomplex
English
Cardol, Pierre mailto [Université de Liège - ULiège > Département des sciences de la vie > Biochimie végétale >]
Boutaffala, Layla [Université de Liège - ULiège > > Virologie - Immunologie >]
Memmi, S. [> > > >]
Devreese, B. [> > > >]
Matagne, René-Fernand mailto [Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Remacle, Claire mailto [Université de Liège - ULiège > Département des sciences de la vie > Génétique >]
16-Jan-2008
Biochimica et Biophysica Acta. Bioenergetics
Elsevier Science
1777
388-396
Yes (verified by ORBi)
International
0005-2728
1879-2650
Amsterdam
Netherlands
[en] In the green alga Chlamydomonas reinhardtii, a mutant deprived of complex I enzyme activity presents a 1T deletion in the mitochondrial nd5 gene. The loss of the ND5 subunit prevents the assembly of the 950 kDa whole complex I. Instead, a low abundant 700 kDa subcomplex, loosely associated to the inner mitochondrial membrane, is assembled. The resolution of the subcomplex by SDS-PAGE gave rise to 19 individual spots, sixteen having been identified by mass spectrometry analysis. Eleven, mainly associated to the hydrophilic part of the complex, are homologs to subunits of the bovine enzyme whereas five (including gamma-type carbonic anhydrase subunits) are specific to green plants or to plants and fungi. None of the subunits typical of the beta membrane domain of complex I enzyme has been identified in the mutant. This allows us to propose that the truncated enzyme misses the membrane distal domain of complex I but retains the proximal domain associated to the matrix arm of the enzyme. A complex I topology model is presented in the light of our results. Finally, a supercomplex most probably corresponding to complex I-complex III association, was identified in mutant mitochondria, indicating that the missing part of the enzyme is not required for the formation of the supercomplex.
http://hdl.handle.net/2268/35187
10.1016/j.bbabio.2008.01.001

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