ArticleThe Journal of biological chemistry2015
Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Control of Golgi- V-ATPase through Sac1-dependent co-regulation of PI(4)P and cholesterol.Nature communications · 2025Article
- Interaction of yeast V-ATPase with TLDc protein Rtc5p.bioRxiv : the preprint server for biology · 2025Article
- Monoclonal nanobodies alter the activity and assembly of the yeast vacuolar HbioRxiv : the preprint server for biology · 2025Article
- Molecular mechanism of Oxr1p mediated disassembly of yeast V-ATPase.EMBO reports · 2024Article
- The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa.International journal of molecular sciences · 2024Article
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo.Molecular biology of the cell · 2023Article
- The cytosolic N-terminal domain of V-ATPase a-subunits is a regulatory hub targeted by multiple signals.Frontiers in molecular biosciences · 2023Review
- The three-dimensional landscape of cortical chromatin accessibility in Alzheimer's disease.Nature neuroscience · 2022Article
- Article
- Review
- ATP synthesis in an ancient ATP synthase at low driving forces.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Coordinated conformational changes in the VNature structural & molecular biology · 2022Article
- Oxidative stress protein Oxr1 promotes V-ATPase holoenzyme disassembly in catalytic activity-independent manner.The EMBO journal · 2022Article
- The HAmerican journal of physiology. Cell physiology · 2021Review
- RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of Organelle Acidification.Frontiers in cell and developmental biology · 2021Review
- Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020Review
- Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of VScience advances · 2020Article
- Mechanical inhibition of isolated VeLife · 2020Article
- A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM.Nature structural & molecular biology · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The membrane sector (Vo) of the proton pumping vacuolar ATPase (V-ATPase, V1Vo-ATPase) from Saccharomyces cerevisiae was purified to homogeneity, and its structure was characterized by EM of single molecules and two-dimensional crystals. Projection images of negatively stained Vo two-dimensional crystals showed a ring-like structure with a large asymmetric mass at the periphery of the ring. A cryo-EM reconstruction of Vo from single-particle images showed subunits a and d in close contact on the cytoplasmic side of the proton channel. A comparison of three-dimensional reconstructions of free Vo and Vo as part of holo V1Vo revealed that the cytoplasmic N-terminal domain of subunit a (aNT) must undergo a large conformational change upon enzyme disassembly or (re)assembly from Vo, V1, and subunit C. Isothermal titration calorimetry using recombinant subunit d and aNT revealed that the two proteins bind each other with a Kd of ~5 μm. Treatment of the purified Vo sector with 1-palmitoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] resulted in selective release of subunit d, allowing purification of a VoΔd complex. Passive proton translocation assays revealed that both Vo and VoΔd are impermeable to protons. We speculate that the structural change in subunit a upon release of V1 from Vo during reversible enzyme dissociation plays a role in blocking passive proton translocation across free Vo and that the interaction between aNT and d seen in free Vo functions to stabilize the Vo sector for efficient reassembly of V1Vo.
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