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Yeast Mitochondrial Dehydrogenases Are Associated in a Supramolecular Complex^†

Xavier Grandier-Vazeille,*^‡ Katell Bathany,^§ Stéphane Chaignepain,^‡ Nadine Camougrand,^‡ Stéphen Manon,^‡ and Jean-Marie Schmitter^§

UMR5095 C.N.R.S./Universit de Bordeaux 2, 1 rue Camille Saint-Sans, 33077 Bordeaux Cedex, France, and UMR5472 C.N.R.S./Universit de Bordeaux 1, Avenue Pey-Berland, 33405 Talence Cedex, France

Biochemistry, 2001, 40 (33), pp 9758–9769

DOI: 10.1021/bi010277r

Publication Date (Web): July 25, 2001

†

This work was supported by grants from the Centre National de la Recherche Scientifique, the Université de Bordeaux 2, the Université de Bordeaux 1, the Ecole Polytechnique and the Conseil Régional d'Aquitaine.

To whom correspondence should be addressed. Phone: 33-556-99-90-50. Fax: 33-556-99-90-51. E-mail: x.grandier-vazeilles@ ibgc.u-bordeaux2.fr.

‡

UMR5095 C.N.R.S.

UMR5472 C.N.R.S.

Abstract

Separation of yeast mitochondrial complexes by colorless native polyacrylamide gel electrophoresis led to the identification of a supramolecular structure exhibiting NADH−dehydrogenase activity. Components of this complex were identified by N-terminal Edman degradation and matrix-assisted laser desorption ionization mass spectrometry. The complex was found to contain the five known intermembrane space-facing dehydrogenases, namely two external NADH−dehydrogenases Nde1p and Nde2p, glycerol-3-phosphate dehydrogenase Gut2p, d- and l-lactate-dehydrogenases Dld1p and Cyb2p, the matrix-facing NADH−dehydrogenase Ndi1p, two probable flavoproteins YOR356Wp and YPR004Cp, four tricarboxylic acids cycle enzymes (malate dehydrogenase Mdh1p, citrate synthase Cit1p, succinate dehydrogenase Sdh1p, and fumarate hydratase Fum1p), and the acetaldehyde dehydrogenase Ald4p. The association of these proteins is discussed in terms of NADH-channeling.

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