Abstract
Copper acts as a redox-active cofactor in over 30 enzymes by means of its two oxidation states, Cu+ and Cu2+. But copper can also be very toxic to cells by its ability to form radicals. Thus, copper must be carefully controlled by all cells (Vulpe and Packman, 1995; Linder and Hazegh Azam, 1996). Two key elements of most, if not all, copper homeostatic mechanisms have only recently been discovered and are milestones in field of trace element research: the copper ATPases and the copper chaperones. Copper ATPases were first discovered in the Gram-positive bacteria Enterococcus hirae (Odermatt et al., 1992). Similar ATPases were later identified in humans as underlying the copper metabolic defects of Menkes and Wilson disease, respectively. More recently, copper ATPases were cloned from yeast and other organisms and over two dozen putative copper ATPases have been described today (Lutsenko and Kaplan, 1995; Solioz and Vulpe, 1996). In fact, copper ATPase genes have been found in every genome that has been completely sequenced, suggesting that these enzymes are ubiquitous.
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References
Anderson, J.E., Ptashne, M., and Harrison, S.C. (1987). Structure of the repressor-operator complex of bacteriophage 434. Nature 326, 846–852.
Fagan, M.J. and Saier, M.H., Jr. (1994). P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 38, 57–99.
Glerum, D.M., Shtanko, A., and Tzagoloff, A. (1996). Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 271, 14504–14509.
Graden, J.A. and Winge, D.R. (1997). Copper-mediated repression of the activation domain in the yeast Maclp transcription factor. Proc. Natl. Acad. Sci. USAP4, 5550–5555.
Hackbarth, CJ. and Chambers, H.R (1993). blal and blaR1 regulate ß-lactamase and PBP 2a production in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 37, 1144–1149.
Himeno, T., Imanaka, T., and Aiba, S. (1986). Nucleotide sequence of the penicillinase repressor gene penl of Bacillus licheniformis and regulation of penP and penlby the repressor (published erratum appears in J Bac-teriol 1987 Jul; 169(7):3392). J. Bacteriol. 168, 1128–1132.
Jungmann, J., Reins, H.A., Lee, J.W., Romeo, A., Hassett, R., Kosman, D., and Jentsch, S. (1993). MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. EMBO J. 12, 5051–5056.
Klomp, L.W., Lin, S.J., Yuan, D.S., Klausner, R.D., Culotta, V.C., and Gitlin, J.D. (1997). Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J. Biol. Chem. 272, 9221–9226.
Lin, S.J. and Culotta, V.C. (1995). The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc. Natl. Acad. Sci. USA 92, 3784–3788.
Linder, M.C. and Hazegh Azam, M. (1996). Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797S–811S.
Lutsenko, S. and Kaplan, J.H. (1995). Organization of P-type ATPases: Significance of structural diversity. Biochemistry 34, 15607–15613.
Moller, J.V., Juul, B., and Le Maire, M. (1996). Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta Rev. Biomembr. 1286, 1–51.
Ochman, H., Gerber, A.S., and Hartl, D.L. (1988). Genetic applications of an inverse polymerase chain reaction. Genetics 120, 621–623.
Odermatt, A., Suter, H., Krapf, R., and Solioz, M. (1993). Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268, 12775–12779.
Odermatt, A., Krapf, R., and Solioz, M. (1994). Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB. Biochem. Biophys. Res. Commun. 202, 44–48.
Odermatt, A. and Solioz, M. (1995). Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J. Biol. Chem. 270, 4349–4354.
Pedersen, RL. and Carafoli, E. (1987a). Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem. Sci. 12, 146–150.
Pedersen, P.L. and Carafoli, E. (1987b). Ion motive ATPases. II. Energy coupling and work output. Trends Biochem. Sci. 12, 186–189.
Peitsch, M.C. (1996). ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24, 274–279.
Pope, M.T. and Dale, B.W. (1968). Isopoly-vanadates,-niobates, and tantalates. Rev. Chem. Soc. 22, 527–545.
Pufahl, R.A., Singer, C.P., Peariso, K.L., Lin, S., Schmidt, P.J., Fahrni, C.J., Culotta, V.C, and Penner-Hahn, J.E. (1997). Metal ion chaperone function of the soluble Cu(I) receptor Atxl [see comments]. Science 278, 853–856.
Solioz, M. (1998). Copper homeostasis by CPX-type ATPases, the subclass of heavy metal P-type ATPases. In Ion pumps. J.P. Andersen, ed. (London: JAI Press, Inc.)
Solioz, M. and Odermatt, A. (1995). Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae. J. Biol. Chem. 270, 9217–9221.
Solioz, M. and Vulpe, C. (1996). CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21, 237–241.
Steele, R.A. and Opella, S.J. (1997). Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochemistry 36, 6885–6895.
Strausak, D. and Solioz, M. (1997). CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases. J. Biol. Chem. 272, 8932–8936.
Suzuki, E., Kuwahara Arai, K., Richardson, J.F., and Hiramatsu, K. (1993). Distribution of mec regulator genes in methicillin-resistant Staphylococcus clinical strains. Antimicrob. Agents Chemother. 37, 1219–1226
Vulpe, CD. and Packman, S. (1995). Cellular copper transport. Annu. Rev. Nutr. 15, 293–322.
Wittman, V. and Wong, H.C. (1988). Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators. J. Bacteriol. 170, 3206–3212.
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Wunderli-Ye, H., Solioz, M. (1999). Copper Homeostasis in Enterococcus hirae . In: Leone, A., Mercer, J.F.B. (eds) Copper Transport and Its Disorders. Advances in Experimental Medicine and Biology, vol 448. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4859-1_23
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DOI: https://doi.org/10.1007/978-1-4615-4859-1_23
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