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J Biol Chem, Vol. 273, Issue 36, 22983-22989, September 4, 1998
°
Cells
From the Centre de Génétique Moléculaire et
Cellulaire, UMR 5534, CNRS, Université Claude Bernard de Lyon I,
69622 Villeurbanne cedex, France
F1-ATPase assembly has been studied in human
° cells devoid of mitochondrial DNA (mtDNA). Since, in these
cells, oxidative phosphorylation cannot provide ATP, their growth
relies on glycolysis. Despite the absence of the mtDNA-coded F0
subunits 6 and 8, ° cells possessed normal levels of F1-ATPase 
and 
subunits. This F1-ATPase was functional and azide- or
aurovertin-sensitive but oligomycin-insensitive. In addition,
aurovertin decreased cell growth in ° cells and also reduced their
mitochondrial membrane potential, as measured by rhodamine 123 fluorescence. Therefore, a functional F1-ATPase was important to
maintain the mitochondrial membrane potential and the growth of these
° cells. Bongkrekic acid, a specific adenine nucleotide
translocator (ANT) inhibitor, also reduced ° cell growth and
mitochondrial membrane potential. In conclusion, ° cells need both
a functional F1-ATPase and a functional ANT to maintain their
mitochondrial membrane potential, which is necessary for their growth.
ATP hydrolysis catalyzed by F1 must provide ADP3
at a
sufficient rate to maintain a rapid exchange with the glycolytic ATP4 by ANT, this electrogenic exchange inducing a
mitochondrial membrane potential efficient enough to sustain cell
growth. However, since the effects of bongkrekic acid and of aurovertin
were additive, other electrogenic pumps should cooperate with this
pathway.
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