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

Natalie Perzov, Vered Padler-Karavani, Hannah Nelson, Nathan Nelson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The general structure of F- and V-ATPases is quite similar and they may share a common mechanism of action that involves mechanochemical energy transduction. Both holoenzymes are composed of catalytic sectors, F1 and V1 respectively, and membrane sectors, Fo and Vo respectively. Although we assume that a similar mechanism underlies ATP-dependent proton pumping by F- and 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 is a consequence of alterations in its membrane sector. The major events include gene duplication of the proteolipids and the presence of three distinct proteolipids in each complex.

Original languageEnglish
Pages (from-to)223-228
Number of pages6
JournalFEBS Letters
Issue number3
StatePublished - 31 Aug 2001


  • F-ATPase
  • Proteolipid
  • Slip mechanism
  • V-ATPase


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