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Gene Review

VMA13  -  H(+)-transporting V1 sector ATPase subunit H

Saccharomyces cerevisiae S288c

Synonyms: CLS11, V-ATPase 54 kDa subunit, V-ATPase subunit H, V-type proton ATPase subunit H, Vacuolar proton pump subunit H, ...
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High impact information on VMA13

  • High level overexpression of Vma5p and Vma13p was lethal even in wild-type cells [1].
  • Cells overexpressing Vma5p and Vma13p demonstrate a classic Vma(-) growth phenotype [1].
  • By using a two-hybrid screen, we found that an activator subunit (Vma13p) of yeast vacuolar H(+)-ATPase (V-ATPase) binds to the cytoplasmic domain of Ynd1p, a yeast ectoapyrase [2].
  • Vma13p bound to Nt-Vph1p in vitro demonstrating direct interaction [3].
  • Free V(1) complexes were isolated from the cytosol of wild-type yeast cells and mutant strains lacking V(o) subunit c (Vma3p) or V(1) subunit H (Vma13p) [4].

Biological context of VMA13

  • Ca(2+)-sensitive mutants of the yeast Saccharomyces cerevisiae showing a Pet- phenotype (cls7-cls11) have lesions in a system for maintaining intracellular Ca2+ homeostasis (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1986) J. Gen. Microbiol. 132, 979-988) [5].
  • The nucleotide sequence of the VMA13 gene predicted a hydrophilic polypeptide with a calculated molecular mass of 54,415 daltons [6].
  • A similar increase in the apyrase activity of Ynd1p was found in a vma1Delta mutant, in which the catalytic subunit A of V-ATPase is missing, and the membrane peripheral subunits including Vma13p are dissociated from the membranes [2].

Associations of VMA13 with chemical compounds

  • Evidence that the NH2 terminus of vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector [3].
  • The perchloric acid extracts were prepared from suspensions of cls11 mutant and wild-type cells incubated with [1,3-13C]glycerol or [2-13]acetate, and analyzed by 31P, 13C and 1H NMR [7].
  • 31P- and 1H-NMR spectra showed significant differences between cls11 and wild-type cells at the level of amino acids, the storage carbohydrate trehalose (higher in mutant cells), and sugar phosphates (higher in wild-type cells) [7].
  • For incubations with [2-13C]acetate, we calculated that the ratio of the relative flux through the glyoxylate shunt versus oxidative reactions is 58% in wild-type cells and 44% in the cls11 mutant cells [7].

Other interactions of VMA13


Analytical, diagnostic and therapeutic context of VMA13


  1. Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p. Keenan Curtis, K., Kane, P.M. J. Biol. Chem. (2002) [Pubmed]
  2. Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase. Zhong, X., Malhotra, R., Guidotti, G. J. Biol. Chem. (2000) [Pubmed]
  3. Evidence that the NH2 terminus of vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector. Landolt-Marticorena, C., Williams, K.M., Correa, J., Chen, W., Manolson, M.F. J. Biol. Chem. (2000) [Pubmed]
  4. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. Parra, K.J., Keenan, K.L., Kane, P.M. J. Biol. Chem. (2000) [Pubmed]
  5. Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity. Ohya, Y., Umemoto, N., Tanida, I., Ohta, A., Iida, H., Anraku, Y. J. Biol. Chem. (1991) [Pubmed]
  6. VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae. Ho, M.N., Hirata, R., Umemoto, N., Ohya, Y., Takatsuki, A., Stevens, T.H., Anraku, Y. J. Biol. Chem. (1993) [Pubmed]
  7. A multinuclear magnetic resonance study of a cls11 mutant showing the Pet- phenotype of Saccharomyces cerevisiae. Galons, J.P., Tanida, I., Ohya, Y., Anraku, Y., Arata, Y. Eur. J. Biochem. (1990) [Pubmed]
  8. Cloning, expression and crystallization of VMA13p, an essential subunit of the vacuolar H+-ATPase of Saccharomyces cerevisiae. Sagermann, M., Matthews, B.W. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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