Assembly of the yeast vacuolar H+‐ATPase and ATP hydrolysis occurs in the absence of subunit c″

  title={Assembly of the yeast vacuolar H+‐ATPase and ATP hydrolysis occurs in the absence of subunit c″},
  author={Graham Whyteside and Lucien C. D. Gibson and Moira Scott and Malcolm E. Finbow},
  journal={FEBS Letters},
Structure and Regulation of Plant Vacuolar H+-ATPase
The vacuolar proton translocating ATPase (V-ATPase) is an essential protein complex present in all eukaryotes which functions as ATP-driven rotary motor. In higher eukaryotes, the V-ATPase consists
Analysis of Strains with Mutations in Six Genes Encoding Subunits of the V-ATPase
To address questions about the structure of the vacuolar ATPase, we have generated mutant strains of Neurospora crassa defective in six subunits, C, H, a, c, c′, and c″. Except for strains lacking
Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1
Stability and function of the metabolon composed of H+ATPase and glycolytic components can be compromised by either loss of required PFK-1 binding (G820R) or loss of pump protein (R807Q) in the context of dRTA.
Effects of Human a3 and a4 Mutations That Result in Osteopetrosis and Distal Renal Tubular Acidosis on Yeast V-ATPase Expression and Activity*
Immunoblots confirmed wild type levels for V-ATPase a, A, and B subunits on vacuolar membranes and confirmed that a4 W520L affects both Vo and V1 subunits is a unique phenotype for any V- ATPase subunit mutation and supports the concerted pathway for V’s assembly in vivo.
Identification of New Pathogenicity Genes in Magnaporthe Oryzae through the Construction of an Agrobacterium Tumefacines-Mediated Insertion Mutant Library
The overall aim of this dissertation project was to identify genes involved in pathogenicity through the construction and characterization of a random insertional mutagenesis library of Magnaporthe oryzae strain 70-15 via two transformation methods.
Author Index


Composition and assembly of the yeast vacuolar H(+)-ATPase complex.
The proton-translocating ATPase (H(+)-ATPase) found on the membrane of the yeast vacuole is the best characterized member of the V-type ATPase family and 14 genes, the majority designated VMA (for vacuolar membrane ATPase) encoding subunits of the enzyme complex are identified.
Assembly and Regulation of the Yeast Vacuolar H+-ATPase
This review focuses on characterization of the yeast V-ATPase stalk subunits, which form the interface between V1 and V0, potential mechanisms of silencing ATP hydrolytic activity in disassembled V1 sectors, and the structure and function of RAVE, a recently discovered complex that regulates V- ATPase assembly.
Assembly of the Yeast Vacuolar Proton-Translocating ATPase
Three genes in yeast are identified that codefor proteins that are not part of the final V-ATPase complex yet required for its assembly, and these nonsubunit Vma proteins are referred to as assembly factors, since their function is dedicated to assembling the V- ATPase.
Evidence that there are two copies of subunit c" in V0 complexes in the vacuolar H+-ATPase.
The proton-translocating core of eukaryotic vacuolar H(+)-ATPase (V-ATPase), V(0) consists of a hexameric arrangement of transmembrane alpha-helices formed from the related polypeptides, subunit c
Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine.
Structural information has provided important hints as to how these enzymes couple H+ transport to the chemical work of ATP synthesis, and the torque of such movement is proposed to cause the rotation of gamma within the alpha 3 beta 3 complex.
H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function
  • R. H. Fillingame
  • Chemistry, Biology
    Journal of bioenergetics and biomembranes
  • 1992
A unique class of suppressor mutations identify a transmembrane helix of subunita that is proposed to interact with the bihelical unit of subunitc during proton transport and the role of multiple units of sub unitc in coupling proton translocation to ATP synthesis is considered.
Composition of the central stalk of the Na+‐pumping V‐ATPase from Caloramator fervidus
The Na+‐pumping V‐ATPase complex of the thermophilic bacterium Caloramator fervidus was purified and dissociated under controlled conditions and difference mapping of subcomplex projections revealed the presence and position of two subunits in the central stalk.
Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo.
  • P. Kane
  • Biology
    The Journal of biological chemistry
  • 1995
Membrane sectors of F- and V-type H+-transporting ATPases.
Direct observation of the rotation of F1-ATPase
It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.