The cytochrome bc(1) and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria

Citation
Cm. Cruciat et al., The cytochrome bc(1) and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria, J BIOL CHEM, 275(24), 2000, pp. 18093-18098
Citations number
31
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
275
Issue
24
Year of publication
2000
Pages
18093 - 18098
Database
ISI
SICI code
0021-9258(20000616)275:24<18093:TCBACC>2.0.ZU;2-G
Abstract
The mitochondrial electron transport chain complexes are large multisubunit complexes embedded in the inner membrane. We report here that in the yeast Saccharomyces cerevisiae, the cytochrome be, and cytochrome c oxidase comp lexes co-exist as a larger complex of similar to 1000 kDa in the mitochondr ial membrane. Following solubilization with a mild detergent, the cytochrom e bc(1)-cytochrome c oxidase complex remains stable. It was analyzed using the techniques of gel filtration and blue native-polyacrylamide gel electro phoresis. Direct physical. association of subunits of the cytochrome be, co mplex with those of the cytochrome c oxidase complex was verified by co-imm unoprecipitation analysis. Our data indicate that the cytochrome be, comple x is exclusively in association with the cytochrome c oxidase complex in ye ast mitochondria. We term this complex the cytochrome bc(1)-cytochrome c ox idase supracomplex.