Diab H, et al. (2009) Subunit Interactions and Requirements for Inhibition of the Yeast V1-ATPase. J Biol Chem 284(20):13316-25
Abstract: Disassembly of the yeast V-ATPase into cytosolic V1 and membrane V0 sectors inactivates MgATPase activity of the V1-ATPase. This inactivation requires the V1 H subunit (Parra et al (2000) J. Biol. Chem. 275:21761-7), but its mechanism is not fully understood. The H subunit has two domains. Interactions of each domain with V1 and Vo subunits were identified by two-hybrid assay. The B subunit of the V1 catalytic headgroup interacted with the H subunit N-terminal domain (H-NT), but the C-terminal domain (H-CT) interacted with V1 subunits B, E (peripheral stalk), and D (central stalk), and the cytosolic N-terminal domain of V0 subunit Vph1p. V1-ATPase complexes from yeast expressing H-NT are partially inhibited, exhibiting 26% the MgATPase activity of complexes with no H subunit. The H-CT domain does not copurify with V1 when expressed in yeast, but the bacterially expressed and purified H-CT domain inhibits MgATPase activity in V1 lacking H almost as well as the full-length H subunit. Binding of full-length H subunit to V1 was more stable than binding of either H-NT or H-CT, suggesting that both domains contribute to binding and inhibition. Intact H and H-CT can bind to the expressed N-terminal domain of Vph1p, but this fragment of Vph1p does not bind to V1 complexes containing subunit H. We propose that upon disassembly, the H subunit undergoes a conformational change that inhibits V1 and precludes V0 interactions.
|Status: Published||Type: Journal Article||PubMed ID: 19299516|
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