Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase.

@article{Ho1993IsolationOV,
  title={Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase.},
  author={M N Ho and Kathryn J. Hill and Margaret A Lindorfer and Tom H. Stevens},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 1},
  pages={
          221-7
        }
}
  • M. Ho, K. Hill, T. Stevens
  • Published 5 January 1993
  • Biology, Chemistry
  • The Journal of biological chemistry

Figures and Tables from this paper

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VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly*
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Wild-type and Mutant Vacuolar Membranes Support pH-dependent Reassembly of the Yeast Vacuolar H+-ATPase in Vitro*
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Assembly of the Yeast Vacuolar H+-ATPase Occurs in the Endoplasmic Reticulum and Requires a Vma12p/Vma22p Assembly Complex
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Subcellular fractionation and chemical cross-linking studies have revealed that Vma12p and Vma22p form a stable membrane associated complex, the first evidence for a dedicated assembly complex in the ER required for the assembly of an integral membrane protein complex (V-ATPase) as it is transported through the secretory pathway.
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Vacuolar H+-ATPase: From mammals to yeast and back
TLDR
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Assembly and Regulation of the Yeast Vacuolar H+-ATPase
TLDR
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.
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References

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Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase
TLDR
Initial results suggest that the peripheral and integral membrane subunits may be independently assembled in the vacuolar H+-ATPase complex and may be part of the final enzyme complex.
Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality.
  • H. Nelson, N. Nelson
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
Failure to lower the pH in the vacuolar system of yeast, and probably other eukaryotic cells, is lethal and the mutants may survive only if a low external pH allows for this acidification by fluid-phase endocytosis.
Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase
TLDR
The results indicate that the vacuolar proton-translocating ATPase complex is essential for vacUolar acidification and that the low-pH state of the vacUole is crucial for normal growth.
Biochemical characterization of the yeast vacuolar H(+)-ATPase.
TLDR
The structure and function of the yeast vacuolar H+-ATPase were characterized by examining the inhibition of ATPase activity by KNO3, and it was suggested that this is a conformation-specific disassembly of the enzyme.
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