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Gene Review

PMA1  -  H(+)-exporting P2-type ATPase PMA1

Saccharomyces cerevisiae S288c

Synonyms: Plasma membrane ATPase 1, Proton pump 1, YGL008C
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Disease relevance of PMA1


High impact information on PMA1

  • The strong homology between the amino-acid sequence encoded by PMA1 and those of (Na+ + K+), Na+-, K+- and Ca2+- ATPases is consistent with the notion that the family of cation pumps which form a phosphorylated intermediate evolved from a common ancestral ATPase [5].
  • The function of the PMA1 gene is essential because a null mutation is lethal in haploid cells [5].
  • We have cloned, mapped and sequenced the gene encoding the yeast plasma membrane ATPase (PMA1) and report here that it maps to chromosome VII adjacent to LEU1 [5].
  • Bsd2 also controls the vacuolar targeting of a manganese transporter and a mutant plasma membrane ATPase, and together with the ER retrieval receptor Rer1, it protects cells from stress [6].
  • Although Eps1 interaction with wild-type Pma1 was not detected, Eps1 co-immunoprecipitates with Pma1-D378N [7].

Biological context of PMA1


Anatomical context of PMA1

  • Finally, we show that yeast expressing a constitutively active allele of calcineurin display pma1-like phenotypes, and that membranes from these yeast have decreased levels of Pma1p activity [10].
  • We took advantage of a temperature-sensitive mutant in PMA1, encoding the plasma membrane ATPase, in which newly synthesized Pma1 is mislocalized to the vacuole via the endosome [12].
  • We found that cytosol from an lst1-null strain supported the packaging of alpha-factor precursor into COPII vesicles but was deficient in the packaging of Pma1p, the essential plasma membrane ATPase [13].
  • Interestingly, in an elo3delta mutant at 37 degrees C, newly synthesized Pma1p failed to enter raft domains early in the biosynthetic pathway, and upon arrival at the plasma membrane was rerouted to the vacuole for degradation [14].
  • Although considerably more oxidation-resistant than other P-type ATPases, the yeast PMA1 H+-ATPase of Saccharomyces cerevisiae SY4 secretory vesicles was inactivated by H2O2, Fe2+, Fe- and Cu-Fenton reagents [15].

Associations of PMA1 with chemical compounds

  • Deletion of APA1 causes a defective regulation of the PMA1 expression by glucose but has not noticeable effect on the expression of other TUF-regulated genes [16].
  • PDR5 was solubilized with n-dodecyl-beta-D-malto-side and separated from the PMA1 plasma membrane H(+)-ATPase by glycerol gradient centrifugation [17].
  • By contrast with wild-type Pma1, mutant Pma1-10 is hypophosphorylated and fails to associate with a Triton-insoluble fraction at 37 degrees C, suggesting failure to enter lipid rafts [18].
  • We also show that calcineurin mutants are sensitive to aminoglycoside antibiotics such as hygromycin B while pma1 mutants are more resistant than wild type [10].
  • Sorbic acid appeared to stimulate plasma membrane H+-ATPase activity in both PMA1 and pma1-205 [19].

Physical interactions of PMA1

  • Furthermore, Pma1p coimmunoprecipitated with Lst1p and Sec24p from vesicles [13].
  • The RPG sequences from PMA1 interact with the promoter binding factor TUF [20].

Enzymatic interactions of PMA1


Regulatory relationships of PMA1

  • The screening is based on the ability to abrogate the growth defect of cells suffering from the galactose induced Pdr3p driven over-expression of a dominant-lethal allele of the PMA1 gene placed under the control of the PDR5 promoter [23].
  • On the other hand, ethanol activated the plasma membrane H(+)-ATPase activity from a strain expressing only the PMA1 ATPase but did not activate that from a strain expressing only the PMA2 ATPase [24].
  • Cells carrying the wild-type PMA1 gene on the chromosome and a dominant lethal mutation under the control of a GAL1 promoter on a centromere-containing plasmid exhibit a galactose-dependent lethality [25].
  • (Capieaux, E., Vignais, M.-L., Sentenac, A. and Goffeau, A. (1989). J. Biol. Chem. 264, 7437-7446), who show that the transcriptional factor TUF/RAP1 binds to upstream activating sequences in the PMA1 gene [26].
  • Surprisingly, monomeric Pma1p present in ceramide-deficient membranes can be exported from the ER in COPII vesicles in a reaction that is stimulated by Lst1p [27].
  • ATG19 was also able to suppress other dominant lethal PMA1 mutations [28].

Other interactions of PMA1

  • A novel gene, AST1, identified by this selection, suppresses several pma1 alleles defective for targeting [29].
  • As this pump is electrogenic, the activity of the Trk1 and -2 K+ uptake system is crucial for sustained Pma1p operation [30].
  • The gene called PMA2 encodes a polypeptide of Mr = 102,157, which, with the exception of the 144 amino-terminal residues, is highly homologous to the structural gene PMA1 for the H+-ATPase [31].
  • Examination of STE6 localization by indirect immunofluorescence indicates that STE6 is found in a punctate, possibly vesicular, intracellular pattern, distinct from the rim-staining pattern characteristic of PMA1 [32].
  • Within a 31 kb region from PMA1 towards TRP5, a total of 12 transcription products ranging from 0.6 to 3.6 kb were identified in cells grown exponentially on rich medium [11].

Analytical, diagnostic and therapeutic context of PMA1


  1. Cloning and expression of the yeast plasma membrane ATPase in Escherichia coli. Holzer, K.P., Hammes, G.G. J. Biol. Chem. (1989) [Pubmed]
  2. Molecular cloning of a P-type ATPase gene from the cyanobacterium Synechocystis sp. PCC 6803. Homology to eukaryotic Ca(2+)-ATPases. Geisler, M., Richter, J., Schumann, J. J. Mol. Biol. (1993) [Pubmed]
  3. Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold. Piper, P.W., Talreja, K., Panaretou, B., Moradas-Ferreira, P., Byrne, K., Praekelt, U.M., Meacock, P., Récnacq, M., Boucherie, H. Microbiology (Reading, Engl.) (1994) [Pubmed]
  4. Influence of anti-Helicobacter triple-therapy with metronidazole, omeprazole and clarithromycin on intestinal microflora. Bühling, A., Radun, D., Müller, W.A., Malfertheiner, P. Aliment. Pharmacol. Ther. (2001) [Pubmed]
  5. Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases. Serrano, R., Kielland-Brandt, M.C., Fink, G.R. Nature (1986) [Pubmed]
  6. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. Hettema, E.H., Valdez-Taubas, J., Pelham, H.R. EMBO J. (2004) [Pubmed]
  7. Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family. Wang, Q., Chang, A. EMBO J. (2003) [Pubmed]
  8. Eps1, a novel PDI-related protein involved in ER quality control in yeast. Wang, Q., Chang, A. EMBO J. (1999) [Pubmed]
  9. A library of yeast genomic MCM1 binding sites contains genes involved in cell cycle control, cell wall and membrane structure, and metabolism. Kuo, M.H., Grayhack, E. Mol. Cell. Biol. (1994) [Pubmed]
  10. Ion tolerance of Saccharomyces cerevisiae lacking the Ca2+/CaM-dependent phosphatase (calcineurin) is improved by mutations in URE2 or PMA1. Withee, J.L., Sen, R., Cyert, M.S. Genetics (1998) [Pubmed]
  11. Physical, transcriptional and genetical mapping of a 24 kb DNA fragment located between the PMA1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae. Capieaux, E., Ulaszewski, S., Balzi, E., Goffeau, A. Yeast (1991) [Pubmed]
  12. Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. Luo, W., Chang, A. J. Cell Biol. (1997) [Pubmed]
  13. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. Shimoni, Y., Kurihara, T., Ravazzola, M., Amherdt, M., Orci, L., Schekman, R. J. Cell Biol. (2000) [Pubmed]
  14. A specific structural requirement for ergosterol in long-chain fatty acid synthesis mutants important for maintaining raft domains in yeast. Eisenkolb, M., Zenzmaier, C., Leitner, E., Schneiter, R. Mol. Biol. Cell (2002) [Pubmed]
  15. Mechanisms of Saccharomyces cerevisiae PMA1 H+-ATPase inactivation by Fe2+, H2O2 and Fenton reagents. Stadler, N., Höfer, M., Sigler, K. Free Radic. Res. (2001) [Pubmed]
  16. Transcriptional control of yeast plasma membrane H(+)-ATPase by glucose. Cloning and characterization of a new gene involved in this regulation. García-Arranz, M., Maldonado, A.M., Mazón, M.J., Portillo, F. J. Biol. Chem. (1994) [Pubmed]
  17. Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast. Decottignies, A., Kolaczkowski, M., Balzi, E., Goffeau, A. J. Biol. Chem. (1994) [Pubmed]
  18. A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface. Gong, X., Chang, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  19. Activity of the plasma membrane H(+)-ATPase and optimal glycolytic flux are required for rapid adaptation and growth of Saccharomyces cerevisiae in the presence of the weak-acid preservative sorbic acid. Holyoak, C.D., Stratford, M., McMullin, Z., Cole, M.B., Crimmins, K., Brown, A.J., Coote, P.J. Appl. Environ. Microbiol. (1996) [Pubmed]
  20. The yeast H+-ATPase gene is controlled by the promoter binding factor TUF. Capieaux, E., Vignais, M.L., Sentenac, A., Goffeau, A. J. Biol. Chem. (1989) [Pubmed]
  21. Calcium signaling and sugar-induced activation of plasma membrane H(+)-ATPase in Saccharomyces cerevisiae cells. Trópia, M.J., Cardoso, A.S., Tisi, R., Fietto, L.G., Fietto, J.L., Martegani, E., Castro, I.M., Brandão, R.L. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  22. Yeast protein kinase Ptk2 localizes at the plasma membrane and phosphorylates in vitro the C-terminal peptide of the H+-ATPase. Eraso, P., Mazón, M.J., Portillo, F. Biochim. Biophys. Acta (2006) [Pubmed]
  23. Screening for effectors that modify multidrug resistance in yeast. Kozovská, Z., Subik, J. Int. J. Antimicrob. Agents (2003) [Pubmed]
  24. The in vivo activation of Saccharomyces cerevisiae plasma membrane H(+)-ATPase by ethanol depends on the expression of the PMA1 gene, but not of the PMA2 gene. Monteiro, G.A., Supply, P., Goffeau, A., Sá-Correia, I. Yeast (1994) [Pubmed]
  25. Dominant lethal mutations in the plasma membrane H(+)-ATPase gene of Saccharomyces cerevisiae. Harris, S.L., Na, S., Zhu, X., Seto-Young, D., Perlin, D.S., Teem, J.H., Haber, J.E. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  26. Transcriptional regulation by glucose of the yeast PMA1 gene encoding the plasma membrane H(+)-ATPase. Rao, R., Drummond-Barbosa, D., Slayman, C.W. Yeast (1993) [Pubmed]
  27. Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. Lee, M.C., Hamamoto, S., Schekman, R. J. Biol. Chem. (2002) [Pubmed]
  28. Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway. Mazón, M.J., Eraso, P., Portillo, F. Mol. Microbiol. (2007) [Pubmed]
  29. Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. Chang, A., Fink, G.R. J. Cell Biol. (1995) [Pubmed]
  30. pH-Responsive, posttranslational regulation of the Trk1 potassium transporter by the type 1-related Ppz1 phosphatase. Yenush, L., Merchan, S., Holmes, J., Serrano, R. Mol. Cell. Biol. (2005) [Pubmed]
  31. A second transport ATPase gene in Saccharomyces cerevisiae. Schlesser, A., Ulaszewski, S., Ghislain, M., Goffeau, A. J. Biol. Chem. (1988) [Pubmed]
  32. Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae. Berkower, C., Loayza, D., Michaelis, S. Mol. Biol. Cell (1994) [Pubmed]
  33. Enzymatic properties of the PMA2 plasma membrane-bound H(+)-ATPase of Saccharomyces cerevisiae. Supply, P., Wach, A., Goffeau, A. J. Biol. Chem. (1993) [Pubmed]
  34. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. Roberg, K.J., Crotwell, M., Espenshade, P., Gimeno, R., Kaiser, C.A. J. Cell Biol. (1999) [Pubmed]
  35. Genetic and molecular mapping of the pma1 mutation conferring vanadate resistance to the plasma membrane ATPase from Saccharomyces cerevisiae. Ulaszewski, S., Balzi, E., Goffeau, A. Mol. Gen. Genet. (1987) [Pubmed]
  36. Site-directed mutagenesis of the yeast PMA1 H(+)-ATPase. Structural and functional role of cysteine residues. Petrov, V.V., Slayman, C.W. J. Biol. Chem. (1995) [Pubmed]
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