The C-H Peripheral Stalk Base: A Novel Component in V1-ATPase Assembly
@article{Hildenbrand2010TheCP, title={The C-H Peripheral Stalk Base: A Novel Component in V1-ATPase Assembly}, author={Zacariah L. Hildenbrand and Sudheer Kumar Molugu and Daniela Stock and Ricardo A Bernal}, journal={PLoS ONE}, year={2010}, volume={5} }
Vacuolar ATPases (V-ATPases) are molecular machines responsible for creating electrochemical gradients and preserving pH-dependent cellular compartments by way of proton translocation across the membrane. V-ATPases employ a dynamic rotary mechanism that is driven by ATP hydrolysis and the central rotor stalk. Regulation of this rotational catalysis is the result of a reversible V1Vo-domain dissociation that is required to preserve ATP during instances of cellular starvation. Recently the method…
28 Citations
Crystal structure of yeast V1‐ATPase in the autoinhibited state
- Chemistry, BiologyThe EMBO journal
- 2016
The crystal structure of yeast V1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C‐terminal domain rotating ~150° from a position near the membrane in holo V‐ATPase to a position at the bottom of V1 near an open catalytic site.
Probing Subunit-Subunit Interactions in the Yeast Vacuolar ATPase by Peptide Arrays
- Biology, ChemistryPloS one
- 2012
Background Vacuolar (H+)-ATPase (V-ATPase; V1Vo-ATPase) is a large multisubunit enzyme complex found in the endomembrane system of all eukaryotic cells where its proton pumping action serves to…
Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation
- Chemistry, Biology
- 2021
CryoEM of yeast V-ATPase was used to determine structures of the intact enzyme, the dissociated but complete V1 complex, and the V1complex lacking sub unit C, suggesting how RAVE could reassemble V1 and VO by recruiting subunit C.
Subunit Positioning and Stator Filament Stiffness in Regulation and Power Transmission in the V1 Motor of the Manduca sexta V-ATPase
- BiologyJournal of molecular biology
- 2014
Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation.
- Chemistry, BiologyNature structural & molecular biology
- 2022
Cryogenic-electron microscopy of yeast V-ATPase was used to determine structures of the intact enzyme, the dissociated but complete V1complex and the V1 complex lacking subunit C, suggesting how RAVE could reassemble V1 and VO by recruiting sub unit C.
Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution
- Biology, ChemistryNature Structural &Molecular Biology
- 2012
This work presents the structure of the Saccharomyces cerevisiae V-type ATPase at 11-Å resolution by cryo-EM of protein particles in ice and provides support for this model by demonstrating that mutation of subunit H to increase the rigidity of the linker between its two domains decreases its ability to inhibit ATPase activity.
Function and Regulation of Mammalian V-ATPase Isoforms
- Biology
- 2016
The binding interaction phenomena specifically at the stalk region, which mediates the reversible assembly and disassembly of V-ATPase in eukaryotic/mammalian cell systems is discussed.
The Plant V-ATPase
- BiologyFrontiers in Plant Science
- 2022
Addressing the regulation of V-ATPase is a promising approach to adjust its activity for improved stress resistance or higher crop yield.
Biochemical and Biophysical Properties of Interactions between Subunits of the Peripheral Stalk Region of Human V-ATPase
- BiologyPloS one
- 2013
The in vitro binding interactions of the subunits at the stalk region of Homo sapiens (human) V-ATPase were investigated and it was likely that, in vivo, the E1G1 heterodimer has a significant role in the initiation of subunit assembly.
Structural Studies of Saccharomyces cerevisiae V1-ATPase in the Stationary Phase of Yeast Cell Culture
- Biology, Chemistry
- 2012
It was shown that by introducing a 3xFLAG tag at the C terminus of different V1-ATPase subunits, highly purified V 1- ATPase complex could be isolated and differed in the peripheral stalk subunit composition.
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