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Functional reconstitution of vacuolar H⁺-ATPase from V_o proton channel and mutant V₁-ATPase provides insight into the mechanism of reversible disassembly.

ABSTRACT: The vacuolar H⁺-ATPase (V-ATPase; V₁V_o-ATPase) is an ATP-dependent proton pump that acidifies subcellular compartments in all eukaryotic organisms. V-ATPase activity is regulated by reversible disassembly into autoinhibited V₁-ATPase and V_o proton channel subcomplexes, a process that is poorly understood on the molecular level. V-ATPase is a rotary motor, and recent structural analyses have revealed different rotary states for disassembled V₁ and V_o, a mismatch that is likely responsible for their inability to reconstitute into holo V-ATPase in vitro Here, using the model organism Saccharomyces cerevisiae, we show that a key impediment for binding of V₁ to V_o is the conformation

SUBMITTER: Sharma S

PROVIDER: S-EPMC6484122 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Functional reconstitution of vacuolar H⁺-ATPase from V_o proton channel and mutant V₁-ATPase provides insight into the mechanism of reversible disassembly.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Functional reconstitution of vacuolar H+-ATPase from Vo proton channel and mutant V1-ATPase provides insight into the mechanism of reversible disassembly.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Functional reconstitution of vacuolar H⁺-ATPase from V_o proton channel and mutant V₁-ATPase provides insight into the mechanism of reversible disassembly.