Features of V-ATPases that distinguish them from F-ATPases

Citation
N. Perzov et al., Features of V-ATPases that distinguish them from F-ATPases, FEBS LETTER, 504(3), 2001, pp. 223-228
Citations number
53
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
504
Issue
3
Year of publication
2001
Pages
223 - 228
Database
ISI
SICI code
0014-5793(20010831)504:3<223:FOVTDT>2.0.ZU;2-X
Abstract
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.