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.

  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},
  volume={268 1},
  • M. Ho, K. Hill, T. Stevens
  • Published 5 January 1993
  • Biology, Chemistry
  • The Journal of biological chemistry

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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.
Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H+-ATPase Complex (*)
Results indicate that Vma22p, along with Vma21p and Vma12p, form a set of ER proteins required for V-ATPase assembly, which is associated with ER membranes.
VMA8 Encodes a 32-kDa V1 Subunit of the Saccharomyces cerevisiae Vacuolar H+-ATPase Required for Function and Assembly of the Enzyme Complex (*)
VMA8, the gene encoding the 32-kDa subunit of the V-ATPase is identified by 100% match between the sequences of tryptic peptides and the predicted protein sequence of ORF11, which resulted in a mutant exhibiting pH-sensitive growth, slowed growth under all conditions, and an inability to grow on nonfermentable carbon sources.
Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex.
It is suggested that Vma21p is required for assembly of the integral membrane sector of the V-ATPase in the endoplasmic reticulum and that the unassembled 100-kDa integral membrane subunit present in delta vma21 cells is rapidly degraded by nonvacuolar proteases.
VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly*
Data indicate that Vma12p functions in the ER after the insertion of V0subunits into the ER membrane, and that assembly is required for the stability of the V0 subunits and their transport as a complex out of this compartment.
Wild-type and Mutant Vacuolar Membranes Support pH-dependent Reassembly of the Yeast Vacuolar H+-ATPase in Vitro*
The results indicate that previously assembled Vo complexes are capable of inducing assembly of the peripheral sub units, both with each other and with the membrane subunits, and of activating the ATPase activity that resides in the peripheralSubunits in a pH-dependent manner.
Assembly of the Yeast Vacuolar H+-ATPase Occurs in the Endoplasmic Reticulum and Requires a Vma12p/Vma22p Assembly Complex
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.
VMA11 and VMA16 Encode Second and Third Proteolipid Subunits of the Saccharomyces cerevisiae Vacuolar Membrane H+-ATPase*
Results suggest that the three proteolipid subunits of the V-ATPase have similar but not redundant functions, each of which is most likely involved in proton transport activity of the enzyme complex.
Vacuolar H+-ATPase: From mammals to yeast and back
The isolation of yeast genes encoding subunits of V-ATPase opened an avenue for molecular biology studies of the enzyme and revealed the relation between V- and F- ATPases that evolved from a common ancestor.
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.


Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase
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
  • 1990
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
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.
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.