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VMA11  -  H(+)-transporting V0 sector ATPase subunit c'

Saccharomyces cerevisiae S288c

Synonyms: CLS9, P1064, Proteolipid protein VMA11, TFP3, Trifluoperazine resistance protein 3, ...
 
 
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High impact information on TFP3

  • Mutations at the corresponding sites in the VMA11 and VMA16 genes of S. cerevisiae, which encode the c' and c" subunits, did not confer resistance to the drugs [1].
  • Analysis of vmaDelta strains showed that binding of V0 subunits to Vma21p was mediated by the proteolipid subunit Vma11p [2].
  • Limited proteolysis experiments with epitope-tagged copies of the proteolipids have revealed that the N and the C termini of c (Vma3p) and c' (Vma11p) were in the lumen of the vacuole [3].
  • The VMA11 gene was isolated from a yeast genomic DNA library by complementation of the vma11 mutation [4].
  • These cDNAs encoded a protein of unknown function, a component (VMA11) of the vacuolar H(+)-ATPase and a component (cytochrome c oxidase subunit VIa) of the mitochondrial electron transport chain, respectively [5].
 

Biological context of TFP3

  • Cells disrupted for the VMA16 gene displayed the same phenotypes as those lacking either Vma3p or Vma11p; the mutant cells lost V-ATPase activity and failed to assemble V-ATPase subunits onto the vacuolar membrane [6].
 

Anatomical context of TFP3

  • Biochemical detection of the VMA11 gene product was unsuccessful, but vacuoles in the VMA11-disrupted cells were not assembled with either subunit c or subunits a and b of the H(+)-ATPase, resulting in defects of the activity and in vivo vacuolar acidification [4].
 

Other interactions of TFP3

  • Surprisingly, loss-of-function mutations of either Vma11p Glu145 or Vma16p Glu108 resulted in a higher degree of assembly of the V1 subunits onto the V0 subcomplex in the vacuolar membrane [6].
 

Analytical, diagnostic and therapeutic context of TFP3

References

  1. The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae. Bowman, E.J., Graham, L.A., Stevens, T.H., Bowman, B.J. J. Biol. Chem. (2004) [Pubmed]
  2. Role of Vma21p in assembly and transport of the yeast vacuolar ATPase. Malkus, P., Graham, L.A., Stevens, T.H., Schekman, R. Mol. Biol. Cell (2004) [Pubmed]
  3. Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae. Flannery, A.R., Graham, L.A., Stevens, T.H. J. Biol. Chem. (2004) [Pubmed]
  4. VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity. Umemoto, N., Ohya, Y., Anraku, Y. J. Biol. Chem. (1991) [Pubmed]
  5. Altered fungal sensitivity to a plant antimicrobial peptide through over-expression of yeast cDNAs. Stephens, C., Harrison, S.J., Kazan, K., Smith, F.W., Goulter, K.C., Maclean, D.J., Manners, J.M. Curr. Genet. (2005) [Pubmed]
  6. VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase. Hirata, R., Graham, L.A., Takatsuki, A., Stevens, T.H., Anraku, Y. J. Biol. Chem. (1997) [Pubmed]
 
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