Chapter 11 Supercomplex organization of the yeast respiratory chain complexes and the ADP/ATP carrier proteins. Methods Enzymol 2009;456:191-208
Date
04/08/2009Pubmed ID
19348890DOI
10.1016/S0076-6879(08)04411-XScopus ID
2-s2.0-63449110220 (requires institutional sign-in at Scopus site) 11 CitationsAbstract
The enzymes involved in mitochondrial oxidative phosphorylation (OXPHOS) are coassembled into higher ordered supercomplexes within the mitochondrial inner membrane. The cytochrome bc(1)-cytochrome c oxidase (COX) supercomplex is formed by the coassociation of the two electron transport chain complexes, the cytochrome bc(1) (cytochrome c reductase) and the COX complex. Recent evidence indicates that a diversity in the populations of the cytochrome bc(1)-COX supercomplexes exists within the mitochondria, because different subpopulations of this supercomplex have been shown to further interact with distinct partner complexes (e.g., the TIM23 machinery and also the Shy1/Cox14 proteins). By use of native gel electrophoresis and affinity purification approaches, the abundant ADP/ATP carrier protein (AAC) isoform in the yeast Saccharomyces cerevisiae, the Aac2 isoform, has recently been found to also exist in physical association with the cytochrome bc(1)-COX supercomplex and its associated TIM23 machinery. The AAC proteins play a central role in cellular metabolism, because they facilitate the exchange of ADP and ATP across the mitochondrial inner membrane. The method used to analyze the cytochrome bc(1)-COX-AAC supercomplex and to affinity purify the Aac2 isoform and its associating proteins from S. cerevisiae mitochondria will be outlined in this chapter.
Author List
Stuart RAAuthor
Rosemary Stuart PhD Professor in the Biology department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
Chromatography, AffinityDetergents
Digitonin
Electrophoresis, Polyacrylamide Gel
Multienzyme Complexes
Receptors, Cytoplasmic and Nuclear
Saccharomyces cerevisiae
