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Gene Review

PMA2  -  H(+)-exporting P2-type ATPase PMA2

Saccharomyces cerevisiae S288c

Synonyms: Plasma membrane ATPase 2, Proton pump 2, YPL036W
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High impact information on PMA2

  • The PMA2 (plasma membrane H(+)-ATPase) isoform from Nicotiana plumbaginifolia was previously shown to be capable of functionally replacing the yeast H(+)-ATPase, provided that the external pH was kept above pH 5 [1].
  • 5. In this study, we used a positive selection to isolate 19 single point mutations of PMA2 which permit the growth of yeast cells at pH 4 [1].
  • Finally, by complementing yeast that lacks its endogenous H(+)-ATPase with wild-type and mutant forms of the Nicotiana plumbaginifolia H(+)-ATPase isoform PMA2, we provide physiological evidence for the importance of the phosphothreonine motif in 14-3-3 binding and, hence, in the activation of the H(+)-ATPase in vivo [2].
  • Moreover, the introduction of seven closely spaced mismatches near the end of a PMA1 segment with an otherwise-high level of identity with PMA2 led to a significantly increased concentration of the junctions near this end [3].
  • Chimeric PMA1::PMA2 sequences, placed under the control of the PMA1 promoter, were constructed by in vivo recombination between a gapped linearized plasmid containing the PMA2 gene and four different fragments of the PMA1 gene [3].

Biological context of PMA2

  • The extensive amino acid sequence homology with the fungal H+-ATPases described so far indicates that the PMA2-encoded protein is also able to function as a H+ pump [4].
  • Slower development of diploids is also observed on normal minimal medium after bilateral disruption of PMA2 in the two parents [4].
  • Correct in-frame assembly of the PMA sequences was screened by the expression of the lacZ reporter gene fused to the PMA2 coding region [3].
  • This partially active gene differs from a wild-type revertant only by the presence of two PMA2-encoded amino acid substitutions [5].
  • Revertants that can grow at pH 3.0 and on ammonium-containing plates frequently arise by ectopic recombination between pma1-105 and PMA2, a diverged gene that shares 85% DNA sequence identity with PMA1 [5].

Anatomical context of PMA2


Associations of PMA2 with chemical compounds

  • More striking, the glucose-activated PMA2 enzyme displays a three to four times higher apparent affinity for MgATP, and maximal activity is reached with a 10-fold lower free Mg2+ concentration [9].
  • Most of the suppressors either replaced the primary site mutation with alanine or restored the wild type residue by ectopic recombination with PMA2, both of which restore alpha-helical tendency [10].
  • These mutations were also introduced in an activated PMA2 mutant (Gln-14 --> Asp) characterized by a higher H(+) pumping activity [11].
  • Mutation of Thr-955 to alanine, aspartate, or a stop codon prevented PMA2 from complementing the yeast H(+)-ATPase [11].
  • In diauxic growth, during transition to stationary phase after ethanol depletion, a further strong activation (eight-fold) of PMA2 gene transcription was observed [12].

Regulatory relationships of PMA2


Other interactions of PMA2

  • 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 [4].
  • Unexpectedly, a fraction of the purified tagged PMA2 associated with the two yeast 14-3-3 regulatory proteins, BMH1 and BMH2 [11].

Analytical, diagnostic and therapeutic context of PMA2

  • The analysis of the PMA1 and PMA2 sequence alignment, compared with reported PMA1 mutations, points to a few residue substitutions as putative contributors to the observed kinetic changes [9].
  • The expression of the PMA1 and PMA2 genes during Saccharomyces cerevisiae growth in medium with glucose plus increasing concentrations of ethanol was monitored by using PMA1-lacZ and PMA2-lacZ fusions and Northern blot hybridizations of total RNA probed with PMA1 gene [13].


  1. Single point mutations in various domains of a plant plasma membrane H(+)-ATPase expressed in Saccharomyces cerevisiae increase H(+)-pumping and permit yeast growth at low pH. Morsomme, P., de Kerchove d'Exaerde, A., De Meester, S., Thinès, D., Goffeau, A., Boutry, M. EMBO J. (1996) [Pubmed]
  2. Phosphorylation of Thr-948 at the C terminus of the plasma membrane H(+)-ATPase creates a binding site for the regulatory 14-3-3 protein. Svennelid, F., Olsson, A., Piotrowski, M., Rosenquist, M., Ottman, C., Larsson, C., Oecking, C., Sommarin, M. Plant Cell (1999) [Pubmed]
  3. In-frame recombination between the yeast H(+)-ATPase isogenes PMA1 and PMA2: insights into the mechanism of recombination initiated by a double-strand break. Supply, P., de Kerchove d'Exaerde, A., Roganti, T., Goffeau, A., Foury, F. Mol. Cell. Biol. (1995) [Pubmed]
  4. A second transport ATPase gene in Saccharomyces cerevisiae. Schlesser, A., Ulaszewski, S., Ghislain, M., Goffeau, A. J. Biol. Chem. (1988) [Pubmed]
  5. Gene conversions and crossing over during homologous and homeologous ectopic recombination in Saccharomyces cerevisiae. Harris, S., Rudnicki, K.S., Haber, J.E. Genetics (1993) [Pubmed]
  6. Activity of plasma membrane H+-ATPase and expression of PMA1 and PMA2 genes in Saccharomyces cerevisiae cells grown at optimal and low pH. Carmelo, V., Bogaerts, P., Sá-Correia, I. Arch. Microbiol. (1996) [Pubmed]
  7. Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae. Supply, P., Wach, A., Thinès-Sempoux, D., Goffeau, A. J. Biol. Chem. (1993) [Pubmed]
  8. Function and regulation of the two major plant plasma membrane H+-ATPases. Woloszynska, M., Kanczewska, J., Drabkin, A., Maudoux, O., Dambly, S., Boutry, M. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  9. Enzymatic properties of the PMA2 plasma membrane-bound H(+)-ATPase of Saccharomyces cerevisiae. Supply, P., Wach, A., Goffeau, A. J. Biol. Chem. (1993) [Pubmed]
  10. Genetic probing of the stalk segments associated with M2 and M3 of the plasma membrane H+-ATPase from Saccharomyces cerevisiae. Soteropoulos, P., Perlin, D.S. J. Biol. Chem. (1998) [Pubmed]
  11. A plant plasma membrane H+-ATPase expressed in yeast is activated by phosphorylation at its penultimate residue and binding of 14-3-3 regulatory proteins in the absence of fusicoccin. Maudoux, O., Batoko, H., Oecking, C., Gevaert, K., Vandekerckhove, J., Boutry, M., Morsomme, P. J. Biol. Chem. (2000) [Pubmed]
  12. Transcription patterns of PMA1 and PMA2 genes and activity of plasma membrane H+-ATPase in Saccharomyces cerevisiae during diauxic growth and stationary phase. Fernandes, A.R., Sá-Correia, I. Yeast (2003) [Pubmed]
  13. 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]
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