Chapter 11 Supercomplex organization of the yeast respiratory chain complexes and the ADP/ATP carrier proteins.

Abstract:

: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.

journal_name

Methods Enzymol

journal_title

Methods in enzymology

authors

Stuart RA

doi

10.1016/S0076-6879(08)04411-X

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

191-208

eissn

0076-6879

issn

1557-7988

pii

S0076-6879(08)04411-X

journal_volume

456

pub_type

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