The basal proton conductance of mitochondria depends on adenine nucleotide translocase content.

TitleThe basal proton conductance of mitochondria depends on adenine nucleotide translocase content.
Publication TypeJournal Article
Year of Publication2005
AuthorsBrand, MD, Pakay, JL, Ocloo, A, Kokoszka, J, Wallace, DC, Brookes, PS, Cornwall, EJ
JournalBiochem J
Volume392
IssuePt 2
Pagination353-62
Date Published2005 Dec 01
ISSN1470-8728
KeywordsAnimals, Cattle, Cell Respiration, Drosophila melanogaster, Drosophila Proteins, Female, Gene Expression Regulation, Enzymologic, Horses, Male, Membrane Potentials, Mice, Mice, Knockout, Mitochondria, Mitochondrial ADP, ATP Translocases, Phospholipids, Protein Binding, Protons, Rabbits, Rats, Swine
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.

DOI10.1042/BJ20050890
Alternate JournalBiochem. J.
Citation Key10.1042/BJ20050890
PubMed ID16076285
PubMed Central IDPMC1316271
Grant ListR01 NS041850 / NS / NINDS NIH HHS / United States
NS41850 / NS / NINDS NIH HHS / United States