Abstract
The basal proton conductance of mitochondria causes mild uncoupling and may be an important contributor to metabolic rate. The molecular nature of the proton-conductance pathway is unknown. We show that the proton conductance of muscle mitochondria from mice in which isoform 1 of the adenine nucleotide translocase has been ablated is half that of wild-type controls. Overexpression of the adenine nucleotide translocase encoded by the stress-sensitive B gene in Drosophila mitochondria increases proton conductance, and underexpression decreases it, even when the carrier is fully inhibited using carboxyatractylate. We conclude that half to two-thirds of the basal proton conductance of mitochondria is catalysed by the adenine nucleotide carrier, independently of its ATP/ADP exchange or fatty-acid-dependent proton-leak functions.
Original language | English |
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Pages (from-to) | 353-362 |
Number of pages | 10 |
Journal | Biochemical Journal |
Volume | 392 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1 Dec 2005 |
Externally published | Yes |
Keywords
- Adenine nucleotide translocase (ANT) knock-out mouse
- Carboxyatractylate
- Drosophila
- Proton leak