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Gene Review

VMA2  -  H(+)-transporting V1 sector ATPase subunit B

Saccharomyces cerevisiae S288c

Synonyms: V-ATPase 57 kDa subunit, V-ATPase subunit B, V-type proton ATPase subunit B, VAT2, Vacuolar proton pump subunit B, ...
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High impact information on VMA2

  • Vacuoles isolated from cells bearing the vat2 null allele were completely devoid of vacuolar ATPase activity [1].
  • The vacuolar acidification-defective vat2 mutant exhibited normal zymogen activation but displayed a minor defect in vacuolar protein sorting [1].
  • For photochemical cross-linking, unique cysteine residues were introduced into the yeast V-ATPase B subunit at sites that were localized based on molecular modeling using the crystal structure of the mitochondrial F(1) domain [2].
  • To investigate residues involved in the formation of the noncatalytic nucleotide binding sites of the vacuolar proton-translocating adenosine triphosphatase (V-ATPase), cysteine scanning mutagenesis of the VMA2 gene that encodes the B subunit in yeast was performed [3].
  • Replacement of the single endogenous cysteine residue at position 188 gave rise to a Cys-less form of the B subunit (Vma2p) which had near wild-type levels of activity and which was used in the construction of 16 single cysteine-containing mutants [3].

Biological context of VMA2

  • Cloning of structural genes for the three subunits of the H+-ATPase (VMA1, VMA2, and VMA3) and their nucleotide sequence determination have been accomplished, which provide greater advantages for molecular biological studies on the structure-function relationship and biogenesis of the enzyme complex [4].
  • However, its deletion in cells lacking the vacuolar ATPase subunit Vma2p leads to loss of viability, suggesting that Tlg2p is involved in endocytosis [5].
  • Mutations at two residues postulated to be contributed by Vma2p to the catalytic site (R381S and Y352S) resulted in a complete loss of ATPase activity and proton transport, with the former having a partial effect on V-ATPase assembly [6].
  • Both genes are interrupted by introns, two in vma1 and four in vma2 [7].

Associations of VMA2 with chemical compounds

  • None of the mutations in either the putative adenine binding pocket nor the P-loop region had any effect on the ability of Vma2p to correctly fold nor on the V-ATPase to correctly assemble [6].

Physical interactions of VMA2

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

Other interactions of VMA2

  • No alleles of the VAT2 or TFP1 genes (known to encode subunits of the vacuolar H(+)-ATPase) were identified in the Vph- screen [9].
  • In order to investigate the influence of vacuolar pH on processing in vivo, the autoactivation of proteinase A and its processing of procarboxypeptidase Y were studied in a vma2 prb1 mutant, which is deficient in vacuolar acidification and proteinase B activity [10].

Analytical, diagnostic and therapeutic context of VMA2

  • Based upon the recent x-ray structure of the mitochondrial F1 ATPase (Abrahams, J.P., Leslie, A.G., Lutter, R., and Walker, J.E. (1994) Nature 370,621-628), site-directed mutagenesis of the yeast VMA2 gene has been carried out in a strain containing a deletion of this gene [6].


  1. Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase. Yamashiro, C.T., Kane, P.M., Wolczyk, D.F., Preston, R.A., Stevens, T.H. Mol. Cell. Biol. (1990) [Pubmed]
  2. Three-dimensional structure of the vacuolar ATPase. Localization of subunit H by difference imaging and chemical cross-linking. Wilkens, S., Inoue, T., Forgac, M. J. Biol. Chem. (2004) [Pubmed]
  3. Cysteine scanning mutagenesis of the noncatalytic nucleotide binding site of the yeast V-ATPase. Vasilyeva, E., Liu, Q., MacLeod, K.J., Baleja, J.D., Forgac, M. J. Biol. Chem. (2000) [Pubmed]
  4. Structure and function of the yeast vacuolar membrane proton ATPase. Anraku, Y., Umemoto, N., Hirata, R., Wada, Y. J. Bioenerg. Biomembr. (1989) [Pubmed]
  5. A yeast t-SNARE involved in endocytosis. Séron, K., Tieaho, V., Prescianotto-Baschong, C., Aust, T., Blondel, M.O., Guillaud, P., Devilliers, G., Rossanese, O.W., Glick, B.S., Riezman, H., Keränen, S., Haguenauer-Tsapis, R. Mol. Biol. Cell (1998) [Pubmed]
  6. Site-directed mutagenesis of the yeast V-ATPase B subunit (Vma2p). Liu, Q., Kane, P.M., Newman, P.R., Forgac, M. J. Biol. Chem. (1996) [Pubmed]
  7. Sequence of the genes encoding subunits A and B of the vacuolar H(+)-ATPase of Schizosaccharomyces pombe. Ghislain, M., Bowman, E.J. Yeast (1992) [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. Genes required for vacuolar acidity in Saccharomyces cerevisiae. Preston, R.A., Reinagel, P.S., Jones, E.W. Genetics (1992) [Pubmed]
  10. pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro. Sørensen, S.O., van den Hazel, H.B., Kielland-Brandt, M.C., Winther, J.R. Eur. J. Biochem. (1994) [Pubmed]
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