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

Natalie Perzov; Vered Padler-Karavani; Hannah Nelson; Nathan Nelson

doi:10.1016/S0014-5793(01)02709-0

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 journal › Article › peer-review

Abstract

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, F_o and V_o 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 language	English
Pages (from-to)	223-228
Number of pages	6
Journal	FEBS Letters
Volume	504
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(01)02709-0
State	Published - 31 Aug 2001

Keywords

F-ATPase
Proteolipid
Slip mechanism
V-ATPase

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10.1016/S0014-5793(01)02709-0

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abstract = "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.",

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AU - Perzov, Natalie

AU - Padler-Karavani, Vered

AU - Nelson, Hannah

AU - Nelson, Nathan

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AB - 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.

KW - F-ATPase

KW - Proteolipid

KW - Slip mechanism

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

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Keywords

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