Dataset Information

MgATP hydrolysis destabilizes the interaction between subunit H and yeast V₁-ATPase, highlighting H's role in V-ATPase regulation by reversible disassembly.

ABSTRACT: Vacuolar H⁺-ATPases (V-ATPases; V₁V_o-ATPases) are rotary-motor proton pumps that acidify intracellular compartments and, in some tissues, the extracellular space. V-ATPase is regulated by reversible disassembly into autoinhibited V₁-ATPase and V_o proton channel sectors. An important player in V-ATPase regulation is subunit H, which binds at the interface of V₁ and V_o H is required for MgATPase activity in holo-V-ATPase but also for stabilizing the MgADP-inhibited state in membrane-detached V₁ However, how H fulfills these two functions is poorly understood. To characterize the H-V₁ interaction and its role in reversible disassembly, we determined binding affinities of full-length H and its N-

SUBMITTER: Sharma S

PROVIDER: S-EPMC6036194 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Dataset Information

MgATP hydrolysis destabilizes the interaction between subunit H and yeast V₁-ATPase, highlighting H's role in V-ATPase regulation by reversible disassembly.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

MgATP hydrolysis destabilizes the interaction between subunit H and yeast V1-ATPase, highlighting H's role in V-ATPase regulation by reversible disassembly.

OmicsDI is part of the ELIXIR infrastructure

Tweets

MgATP hydrolysis destabilizes the interaction between subunit H and yeast V₁-ATPase, highlighting H's role in V-ATPase regulation by reversible disassembly.