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Gene Review

VMA7  -  H(+)-transporting V1 sector ATPase subunit F

Saccharomyces cerevisiae S288c

Synonyms: V-ATPase 14 kDa subunit, V-ATPase subunit F, V-type proton ATPase subunit F, Vacuolar proton pump subunit F, YGR020C
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Disease relevance of VMA7


High impact information on VMA7

  • Although Vma7p and Vma10p have been observed to interact with the V0 sector, our results indicate that these subunits behave primarily as canonical V1 sector subunits [3].
  • Epitope-tagged Vma7p was constructed and the proton uptake activity of isolated vacuoles from this yeast strain was markedly inhibited by a monoclonal antibody against the epitope-tag [4].
  • Vacuolar membranes isolated from a vma7 delta null mutant contained no V-ATPase activity [5].
  • Western analysis of vma7 delta cells revealed greatly reduced levels of the remaining V0 complex V-ATPase subunits, but normal levels of the V1 subunits [5].
  • The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence [2].

Biological context of VMA7


Physical interactions of VMA7


Other interactions of VMA7

  • The anti-HA epitope antibody inhibited both the ATP-dependent proton uptake and the ATPase activities of the Vma16p-HA and Vma7p-HA containing complexes, in intact vacuoles and in the detergent-solubilized enzyme [7].
  • In order to characterize the functional link between these two activities we searched for proteins interacting with C. albicans Vps34p and demonstrate physical interaction of Vps34p with the subunit of the vacuolar H+ -ATPase Vma7p [6].

Analytical, diagnostic and therapeutic context of VMA7


  1. Expression, purification and secondary structure analysis of Saccharomyces cerevisiae vacuolar membrane H+-ATPase subunit F (Vma7p). Jones, R.P., Hunt, I.E., Jaeger, J., Ward, A., O'Reilly, J., Barratt, E.A., Findlay, J.B., Harrison, M.A. Mol. Membr. Biol. (2001) [Pubmed]
  2. The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence. Poltermann, S., Nguyen, M., Günther, J., Wendland, J., Härtl, A., Künkel, W., Zipfel, P.F., Eck, R. Microbiology (Reading, Engl.) (2005) [Pubmed]
  3. 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]
  4. The Saccharomyces cerevisiae VMA7 gene encodes a 14-kDa subunit of the vacuolar H(+)-ATPase catalytic sector. Nelson, H., Mandiyan, S., Nelson, N. J. Biol. Chem. (1994) [Pubmed]
  5. VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase complex. Graham, L.A., Hill, K.J., Stevens, T.H. J. Biol. Chem. (1994) [Pubmed]
  6. The phosphatidylinositol 3-kinase Vps34p of the human pathogenic yeast Candida albicans is a multifunctional protein that interacts with the putative vacuolar H+ -ATPase subunit Vma7p. Eck, R., Nguyen, M., Günther, J., Künkel, W., Zipfel, P.F. Int. J. Med. Microbiol. (2005) [Pubmed]
  7. Biochemical support for the V-ATPase rotary mechanism: antibody against HA-tagged Vma7p or Vma16p but not Vma10p inhibits activity. Aviezer-Hagai, K., Padler-Karavani, V., Nelson, N. J. Exp. Biol. (2003) [Pubmed]
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