Document Type
Article
Language
eng
Publication Date
9-2008
Publisher
American Society for Cell Biology
Source Publication
Molecular Biology of the Cell
Source ISSN
1059-1524
Original Item ID
DOI: 10.1091/mbc.E08-04-0402
Abstract
The ADP/ATP carrier (AAC) proteins play a central role in cellular metabolism as they facilitate the exchange of ADP and ATP across the mitochondrial inner membrane. We present evidence here that in yeast (Saccharomyces cerevisiae) mitochondria the abundant Aac2 isoform exists in physical association with the cytochrome c reductase (cytochrome bc1)-cytochrome c oxidase (COX) supercomplex and its associated TIM23 machinery. Using a His-tagged Aac2 derivative and affinity purification studies, we also demonstrate here that the Aac2 isoform can be affinity-purified with other AAC proteins. Copurification of the Aac2 protein with the TIM23 machinery can occur independently of its association with the fully assembled cytochrome bc1-COX supercomplex. In the absence of the Aac2 protein, the assembly of the cytochrome bc1-COX supercomplex is perturbed, whereby a decrease in the III2-IV2 assembly state relative to the III2-IV form is observed. We propose that the association of the Aac2 protein with the cytochrome bc1-COX supercomplex is important for the function of the OXPHOS complexes and for the assembly of the COX complex. The physiological implications of the association of AAC with the cytochrome bc1-COX-TIM23 supercomplex are also discussed.
Recommended Citation
Dienhart, Mary Kathryn and Stuart, Rosemary A., "The Yeast Aac2 Protein Exists in Physical Association with the Cytochrome bc1-COX Supercomplex and the TIM23 Machinery" (2008). Biological Sciences Faculty Research and Publications. 360.
https://epublications.marquette.edu/bio_fac/360
Comments
Published version. Molecular Biology of the Cell, Vol. 19, No. 9 (September 2008): 3934-3943. DOI. © 2009 American Society for Cell Biology. Used with permission.