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Gene Review

PMR1  -  Ca(2+)/Mn(2+)-transporting P-type ATPase PMR1

Saccharomyces cerevisiae S288c

Synonyms: BSD1, Bypass SOD defects protein 1, Calcium-transporting ATPase 1, G1666, Golgi Ca(2+)-ATPase, ...
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Disease relevance of PMR1


High impact information on PMR1

  • PMR1 is identical to SSC1, a gene previously identified by its effect on secretion of some foreign proteins from yeast [5].
  • The genes for two new P-type ATPases, PMR1 and PMR2, have been identified in yeast [5].
  • Proteins secreted from pmr1 mutants lack the outer chain glycosylation that normally results from passage through the Golgi [5].
  • Mutations in PMR1, a yeast gene encoding a calcium/manganese exporter, dramatically decrease Ty1 retrotransposition [6].
  • Cytoplasmic accumulation of Mn(2+) in pmr1 cells may directly affect reverse transcriptase (RT) activity [6].

Chemical compound and disease context of PMR1

  • Three classes of mutants were found: mutants indistinguishable from wild type (Class 1), mutants indistinguishable from the pmr1 null strain (Class 2), and mutants with differential sensitivity to BAPTA and Mn(2+) toxicity (Class 3) [7].
  • The pmr1 knockout (Deltapmr1) cells exhibited hypersensitivity to EGTA [8].

Biological context of PMR1

  • Additional studies with reporter genes and mutants indicate that PMR1 and PMR2A, encoding P-type ion pumps required for Mn2+ and Na+ tolerance, may also be induced physiologically in response to high-Mn2+ and -Na+ conditions through calcineurin-dependent mechanisms [9].
  • The effect of PMR1 on Golgi function is indicated by pleiotropic defects in various Golgi processes in pmr1 mutants, including impaired proteolytic processing of pro-alpha factor and incomplete outer chain glycosylation of invertase [10].
  • We previously reported that oxidative damage in yeast lacking copper/zinc superoxide dismutase (SOD1) can be alleviated through mutations in PMR1, encoding a calcium P-type ATPase homologue that also functions in manganese homeostasis [11].
  • Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance [12].
  • SUA5 was mapped to chromosome VII, immediately adjacent to the PMR1 gene [13].

Anatomical context of PMR1

  • Mutation in PMR1, a Ca(2+)-ATPase in Golgi, confers salt tolerance in Saccharomyces cerevisiae by inducing expression of PMR2, an Na(+)-ATPase in plasma membrane [14].
  • PMR1, a Ca(2+)-adenosine triphosphatase (ATPase) homologue in the yeast Saccharomyces cerevisiae localizes to a novel Golgi-like organelle [10].
  • In the yeast Saccharomyces cerevisiae, the Golgi PMR1 Ca(2+)-ATPase and the vacuole PMC1 Ca(2+)-ATPase function together in Ca2+ sequestration and Ca2+ tolerance [12].
  • The mutations were found to lie in the PMR1 gene, known to encode a "P-type" Ca(2+)-ATPase that transports Ca2+ and Mn2+ from the cytosol to the Golgi apparatus [15].
  • Detailed characterization of calcium transport by PMR1 showed that sensitivity to inhibitors (vanadate, thapsigargin, and cyclopiazonic acid) and affinity for substrates (MgATP and Ca2+) were different from the previously characterized sarco/endoplasmic reticulum and plasma membrane Ca2+-ATPases [16].

Associations of PMR1 with chemical compounds


Regulatory relationships of PMR1

  • Overexpression of Pmr1p suppressed some ret1 mutant phenotypes, namely, Ca2+ dependence and enhanced uPA secretion [21].

Other interactions of PMR1

  • A second Ca2+ ATPase homolog encoded by the PMR1 gene acts together with PMC1 to prevent lethal activation of calcineurin even in standard (low Ca2+) conditions [22].
  • Treating smf2Delta cells with manganese supplements corrected the SOD2 defect, as did elevating intracellular manganese through mutations in PMR1 [23].
  • Our studies indicate that, like PMR1, CCC1 functions in the homeostasis of both calcium and manganese ions [11].
  • However, PMR1 shows only partial colocalization with known Golgi markers, KEX2 and SEC7, in double-label immunofluorescence experiments [10].
  • The three other ORFs identified are partially (G1663) or completely (G1667 and G1669) overlapping with the PMR1 sequence on the complementary strand [24].

Analytical, diagnostic and therapeutic context of PMR1

  • Consistent with a Golgi localization, the bulk of PMR1 comigrates with Golgi markers in subcellular fractionation experiments, and staining of PMR1 by indirect immunofluorescence reveals a punctate pattern resembling Golgi staining in yeast [10].
  • Molecular cloning of YlPMR1, a S. cerevisiae PMR1 homologue encoding a novel P-type secretory pathway Ca2+ -ATPase, in the yeast Yarrowia lipolytica [25].
  • In addition, three PCR products were cloned which share homology with another SER Ca(2+)-ATPase, with the yeast secretory pathway Ca(2+)-ATPase PMR1 and its mammalian homologue, and with the alpha subunit of a Na+,K(+)-ATPase [26].
  • We have solubilized and purified the histidine-tagged yeast secretory pathway/Golgi ion pump Pmr1 to near homogeneity in one step, using nickel affinity chromatography [27].
  • However, in the case of the Saccharomyces pmr1 mutant, an alpha 1,3-mannosyltransferase was active in microsomal extracts, but the alpha 1,3-Man epitope could not be identified on Western blots of cellular glycoproteins using sugar linkage-specific antibodies or lectins [28].


  1. Isolation and characterisation of a mutation in the PMR1 gene encoding a Golgi membrane ATPase, which causes hypersensitivity to over-expression of Clb3 in Saccharomyces cerevisiae. Funakoshi, M., Kajiwara, R., Goda, T., Nishimoto, T., Kobayashi, H. Mol. Gen. Genet. (2000) [Pubmed]
  2. Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Lapinskas, P.J., Cunningham, K.W., Liu, X.F., Fink, G.R., Culotta, V.C. Mol. Cell. Biol. (1995) [Pubmed]
  3. Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. Kellermayer, R. FEBS Lett. (2005) [Pubmed]
  4. An N-terminal EF hand-like motif modulates ion transport by Pmr1, the yeast Golgi Ca(2+)/Mn(2+)-ATPase. Wei, Y., Marchi, V., Wang, R., Rao, R. Biochemistry (1999) [Pubmed]
  5. The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. Rudolph, H.K., Antebi, A., Fink, G.R., Buckley, C.M., Dorman, T.E., LeVitre, J., Davidow, L.S., Mao, J.I., Moir, D.T. Cell (1989) [Pubmed]
  6. Inhibition of reverse transcription in vivo by elevated manganese ion concentration. Bolton, E.C., Mildvan, A.S., Boeke, J.D. Mol. Cell (2002) [Pubmed]
  7. Phenotypic screening of mutations in Pmr1, the yeast secretory pathway Ca2+/Mn2+-ATPase, reveals residues critical for ion selectivity and transport. Wei, Y., Chen, J., Rosas, G., Tompkins, D.A., Holt, P.A., Rao, R. J. Biol. Chem. (2000) [Pubmed]
  8. Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively regulate cell morphogenesis in fission yeast: the importance of Mn2+ homeostasis. Maeda, T., Sugiura, R., Kita, A., Saito, M., Deng, L., He, Y., Yabin, L., Fujita, Y., Takegawa, K., Shuntoh, H., Kuno, T. Genes Cells (2004) [Pubmed]
  9. Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+ ATPases in Saccharomyces cerevisiae. Cunningham, K.W., Fink, G.R. Mol. Cell. Biol. (1996) [Pubmed]
  10. The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Antebi, A., Fink, G.R. Mol. Biol. Cell (1992) [Pubmed]
  11. The role of the Saccharomyces cerevisiae CCC1 gene in the homeostasis of manganese ions. Lapinskas, P.J., Lin, S.J., Culotta, V.C. Mol. Microbiol. (1996) [Pubmed]
  12. Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance. Degand, I., Catty, P., Talla, E., Thinès-Sempoux, D., de Kerchove d'Exaerde, A., Goffeau, A., Ghislain, M. Mol. Microbiol. (1999) [Pubmed]
  13. Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae. Na, J.G., Pinto, I., Hampsey, M. Genetics (1992) [Pubmed]
  14. Mutation in PMR1, a Ca(2+)-ATPase in Golgi, confers salt tolerance in Saccharomyces cerevisiae by inducing expression of PMR2, an Na(+)-ATPase in plasma membrane. Park, S.Y., Seo, S.B., Lee, S.J., Na, J.G., Kim, Y.J. J. Biol. Chem. (2001) [Pubmed]
  15. Involvement of thioredoxin peroxidase type II (Ahp1p) of Saccharomyces cerevisiae in Mn2+ homeostasis. Farcasanu, I.C., Hirata, D., Tsuchiya, E., Mizuta, K., Miyakawa, T. Biosci. Biotechnol. Biochem. (1999) [Pubmed]
  16. PMR1, a Ca2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps. Sorin, A., Rosas, G., Rao, R. J. Biol. Chem. (1997) [Pubmed]
  17. Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles. Lin, S.J., Culotta, V.C. Mol. Cell. Biol. (1996) [Pubmed]
  18. Antifungal activity in Saccharomyces cerevisiae is modulated by calcium signalling. Edlind, T., Smith, L., Henry, K., Katiyar, S., Nickels, J. Mol. Microbiol. (2002) [Pubmed]
  19. Secretory expression and purification of Aspergillus niger glucose oxidase in Saccharomyces cerevisiae mutant deficient in PMR1 gene. Ko, J.H., Hahm, M.S., Kang, H.A., Nam, S.W., Chung, B.H. Protein Expr. Purif. (2002) [Pubmed]
  20. The Golgi PMR1 P-type ATPase of Caenorhabditis elegans. Identification of the gene and demonstration of calcium and manganese transport. Van Baelen, K., Vanoevelen, J., Missiaen, L., Raeymaekers, L., Wuytack, F. J. Biol. Chem. (2001) [Pubmed]
  21. C-terminal truncation of alpha-COP affects functioning of secretory organelles and calcium homeostasis in Hansenula polymorpha. Chechenova, M.B., Romanova, N.V., Deev, A.V., Packeiser, A.N., Smirnov, V.N., Agaphonov, M.O., Ter-Avanesyan, M.D. Eukaryotic Cell (2004) [Pubmed]
  22. Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases. Cunningham, K.W., Fink, G.R. J. Cell Biol. (1994) [Pubmed]
  23. Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. Luk, E.E., Culotta, V.C. J. Biol. Chem. (2001) [Pubmed]
  24. A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae. Klima, R., Coglievina, M., Zaccaria, P., Bertani, I., Bruschi, C.V. Yeast (1996) [Pubmed]
  25. Molecular cloning of YlPMR1, a S. cerevisiae PMR1 homologue encoding a novel P-type secretory pathway Ca2+ -ATPase, in the yeast Yarrowia lipolytica. Park, C.S., Kim, J.Y., Crispino, C., Chang, C.C., Ryu, D.D. Gene (1998) [Pubmed]
  26. Cloning and characterization of a putative calcium-transporting ATPase gene from Schistosoma mansoni. de Mendonça, R.L., Beck, E., Rumjanek, F.D., Goffeau, A. Mol. Biochem. Parasitol. (1995) [Pubmed]
  27. Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport. Mandal, D., Woolf, T.B., Rao, R. J. Biol. Chem. (2000) [Pubmed]
  28. Mannosyltransferase activities in membranes from various yeast strains. Verostek, M.F., Trimble, R.B. Glycobiology (1995) [Pubmed]
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