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Gene Review

VMA4  -  H(+)-transporting V1 sector ATPase subunit E

Saccharomyces cerevisiae S288c

Synonyms: O6241, V-ATPase 27 kDa subunit, V-ATPase subunit E, V-type proton ATPase subunit E, VAT5, ...
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Disease relevance of VMA4

  • A recombinant form of subunit E (Vma4p) from yeast vacuolar ATPases (V-ATPases) has been overexpressed in Escherichia coli, purified to homogeneity, and explored by mass spectrometry [1].

High impact information on VMA4

  • The ATP hydrolysis rate was 72% of the wild-type rate; but there was no proton translocation, and two V(1) subunits (Vma4p and Vma8p) were present at lower levels [2].
  • The Rim101p-dependent gene VMA4 is required for growth in alkaline conditions, illustrating how Rim101p may control adaptation [3].
  • Cells lacking a functional VMA4 gene are unable to grow at pH > 7 or in elevated concentrations of CaCl2 [4].
  • Plasmid-borne, mutagenized vma4 genes were screened for failure to complement these phenotypes [4].
  • Furthermore, we show that the in vivo stability of Vma4p is dependent upon interaction with Vma10p [5].

Biological context of VMA4


Anatomical context of VMA4

  • The VMA4 gene encodes a 26.6-kDa hydrophilic polypeptide which exhibits 34% sequence identity with the E subunit of the vacuolar ATPase from bovine kidney microsomes [6].

Associations of VMA4 with chemical compounds

  • Cells of the delta vma4 mutant strain, with no functional vacuolar H(+)-ATPase, had elevated levels of [Ca2+]i, reaching 1.8 microM when pre-incubated with glucose and exposed to 10 mM CaCl2 [7].

Physical interactions of VMA4

  • Yeast two-hybrid data indicate that Vma1p and Vma2p interact with each other and that Vma4p interacts with itself [8].

Other interactions of VMA4

  • We report here the characterization of two genes, VMA4 and VMA5, that encode peripheral subunits of the vacuolar H(+)-ATPase [9].
  • The chromosomal VMA4 gene was inactivated by a 171-base pair deletion followed by insertion of the URA3 gene within the coding sequence [6].
  • The tightly linked VMA4 and MIP1 (encoding the mitochondrial DNA polymerase) genes are divergently transcribed from face-to-face promoters [6].

Analytical, diagnostic and therapeutic context of VMA4

  • Analysis of the secondary structure of Vma4p by circular dichroism spectroscopy indicated 32% alpha-helix and 23% beta-sheet content [1].


  1. Expression, purification, and characterization of subunit E, an essential subunit of the vacuolar ATPase. Grüber, G., Godovac-Zimmermann, J., Link, T.A., Coskun, U., Rizzo, V.F., Betz, C., Bailer, S.M. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  2. Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p. Keenan Curtis, K., Kane, P.M. J. Biol. Chem. (2002) [Pubmed]
  3. Alkaline response genes of Saccharomyces cerevisiae and their relationship to the RIM101 pathway. Lamb, T.M., Xu, W., Diamond, A., Mitchell, A.P. J. Biol. Chem. (2001) [Pubmed]
  4. Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology. Zhang, J.W., Parra, K.J., Liu, J., Kane, P.M. J. Biol. Chem. (1998) [Pubmed]
  5. V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase. Tomashek, J.J., Graham, L.A., Hutchins, M.U., Stevens, T.H., Klionsky, D.J. J. Biol. Chem. (1997) [Pubmed]
  6. The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in Saccharomyces cerevisiae. Foury, F. J. Biol. Chem. (1990) [Pubmed]
  7. Calcium homeostasis in yeast cells exposed to high concentrations of calcium. Roles of vacuolar H(+)-ATPase and cellular ATP. Halachmi, D., Eilam, Y. FEBS Lett. (1993) [Pubmed]
  8. Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase. Tomashek, J.J., Sonnenburg, J.L., Artimovich, J.M., Klionsky, D.J. J. Biol. Chem. (1996) [Pubmed]
  9. 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. Ho, M.N., Hill, K.J., Lindorfer, M.A., Stevens, T.H. J. Biol. Chem. (1993) [Pubmed]
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