The general structure of F- and V-ATPases is quite similar and they may sha
re a common mechanism of action that involves mechanochemical energy transd
uction. Both holoenzymes are composed of catalytic sectors, F-1 and V-1 res
pectively, and membrane sectors, F-0 and V-0 respectively. Although we assu
me that a similar mechanism underlies ATP-dependent proton pumping by F- an
d V-ATPases in eukaryotic cells, the latter cannot catalyze pmf-driven ATP
synthesis. The loss of this ability is probably due to a proton slip that i
s a consequence of alterations in its membrane sector. The major events inc
lude gene duplication of the proteolipids and the presence of three distinc
t proteolipids in each complex. (C) 2001 Federation of European Biochemical
Societies. Published by Elsevier Science B.V. All rights reserved.