Cruciat C M, Brunner S, Baumann F, Neupert W, Stuart R A
Institut für Physiologische Chemie der Universität München, Goethestrasse 33, 80336 München, Germany.
J Biol Chem. 2000 Jun 16;275(24):18093-8. doi: 10.1074/jbc.M001901200.
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 bc(1) and cytochrome c oxidase complexes co-exist as a larger complex of approximately 1000 kDa in the mitochondrial membrane. Following solubilization with a mild detergent, the cytochrome bc(1)-cytochrome c oxidase complex remains stable. It was analyzed using the techniques of gel filtration and blue native-polyacrylamide gel electrophoresis. Direct physical association of subunits of the cytochrome bc(1) complex with those of the cytochrome c oxidase complex was verified by co-immunoprecipitation analysis. Our data indicate that the cytochrome bc(1) complex is exclusively in association with the cytochrome c oxidase complex in yeast mitochondria. We term this complex the cytochrome bc(1)-cytochrome c oxidase supracomplex.
线粒体电子传递链复合物是嵌入内膜的大型多亚基复合物。我们在此报告，在酿酒酵母中，细胞色素bc(1)复合物和细胞色素c氧化酶复合物在线粒体膜中以大约1000 kDa的更大复合物形式共存。用温和的去污剂溶解后，细胞色素bc(1)-细胞色素c氧化酶复合物保持稳定。使用凝胶过滤和蓝色天然聚丙烯酰胺凝胶电泳技术对其进行了分析。通过共免疫沉淀分析证实了细胞色素bc(1)复合物的亚基与细胞色素c氧化酶复合物的亚基直接物理缔合。我们的数据表明，在酵母线粒体中，细胞色素bc(1)复合物仅与细胞色素c氧化酶复合物缔合。我们将这种复合物称为细胞色素bc(1)-细胞色素c氧化酶超复合物。
