Abstract
Copper is imported into prokaryotic cells by CPx-type ATPases. CPx-type ATPases have the transmembrane characteristics typical of P-type ATPases involved in the translocation of many ions. A conserved Cys-Pro-X (X = C or H) sequence within the transmembrane channel and a variable number of distinct amino-terminal domains define the CPx classification (1). The cytoplasmic subdomains of the CPx-ATPases have a MxCxxC or M/HxxMDHS/GxM metal-binding site (x = any amino acid). Intracellular copper is utilized in the activation of enzymes, such as cytochrome-c oxidase, superoxide dismutase, and lysyl oxidase. Copper also has the potential to cause cellular damage because of its redox properties. To overcome this dichotomy, the cell regulates copper levels and prevents toxicity with overlapping mechanisms: sequestration, export, and inhibition of entry.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Solioz, M. and Vulpe, C. (1996) CPx-type ATPasea class of P-type ATPases that pump heavy metals. TIBS 21, 237–241.
Vasak, M. and Hasler, D. W. (2000) Metallothioneins: new functional and structural insights. Curr. Opin. Chem. Biol. 4, 177–183.
Harrison, M. D. and Dameron, C. T. (1999) Molecular mechanisms of copper metabolism and the role of the Menkes disease protein. J. Biochem. Mol. Toxicol. 13, 93–106.
Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C., and O’Halloran, T. V. (1999) Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284, 805–808.
Harrison, M. D., Jones, C. E., Solioz, M., and Dameron, C. T. (2000) Intracellular copper routing: the role of copper chaperones. TIBS 25, 29–32.
Rosenzweig, A. C. and O’Halloran, T. V. (2000) Structure and chemistry of the copper chaperone proteins. Curr. Opin. Chem. Biol. 4, 140–147.
O’Halloran, T. V. and Culotta, V. C. (2000) Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275, 25,057–25, 060.
Cobine, P., Wickramasinghe, W. A., Harrison, M. D., Weber, T., Solioz, M., and Dameron, C.T. (1999) The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor. FEBS Lett. 445, 27–30.
Odermatt, A. and Solioz, M. (1995) Two trans-acting metalloregulatory proteins controlling expression of the copperATPases of Enterococcus hirae. J. Biol. Chem. 270, 4349–4354.
Strausak, D. and Solioz, M. (1997) CopY is a copper-inducible repressor of the Enterococcus hirae Copper ATPases. J. Biol. Chem. 272, 8932–8936.
Wimmer, R., Herrmann, T., Solioz, M., and Wuthrich, K. (1999) NMR structure and metal interactions of the CopZ copper chaperone. J. Biol. Chem. 99, 22,597–22, 603.
Richardson, J. S. (1981) The anatomy and taxonomy of protein structures. Adv. Protein Chem 34, 167–339.
Kobe, B., Jennings, I.G., House, C.M., Michell, B.J., Goodwill, K.E., Santarsiero, B.D., et al. (1999) Structural basis of autoregulation of phenylalanine hydroxylase. Nature Struct. Biol. 5, 442–448.
Vendrell, J., Billeter, M., Wider, G., Aviles, F. X., and Wutrich, K. (1991) The NMR structure of the activation domain isolated from porcine procarboxypeptidase B. EMBO J. 10(1) 11–15.
Kissinger, C. R., Sieker, L. C., Adman, E. T., and Jensen, L. H. (1991) Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 A. J. Mol. Biol. 219 (4), 693–715.
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.
Gitschier, J., Moffat, B., Reilly, D., Wood, W.I., and Fairbrother, W.J. (1998) solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nature Struct. Biol. 5, 47–54.
Rosenzweig, A. C., Huffman, D. L., Hou, M.Y., Wernimont, A. K., Pufahl, R. A., and O’Halloran, T. V. (1999) Crystal structure of the Atxl metallochaperone at 1.02 A resolution. Structure 7, 605–617.
Lamb, A. L., Wernimont, A. K., Pufahl, R. A., O’Halloran, T. V., and Rosenzweig, A. C. (1999) Crystal structure of the copper chaperone for superoxide dismutase. Nature Struct. Biol. 6, 724–729.
Lu, Z. H., Cobine, P., Dameron, C. T., and Solioz (1999) How cells handle copper: a view from microbes. J. Trace Elements Exp. Med. 12, 347–360.
Cobine, P. A., George, G. N., Wickramasinghe, W. A., Solioz, M., and Dameron, C. T. (2000) Coordination environment in the copper chaperone CopZ and its target, the repressor CopY. Biochemistry,in press.
Dameron, C. T., Winge, D. R., George, G. N., Sansone, M., Hu, S., and Hamer, D. (1991) A copper–thiolate poly-nuclear cluster in the ACE1 transcription factor. Proc. Natl. Acad. Sci. USA 88, 6127–6131.
Pufahl, R. A., Singer, C. P., Peariso, K. L., Lin, S.-J., Schmidt, P. J., Fahrni, C. J., et al. (1997) Metal ion chaperone function of the soluble Cu(I) receptor Atxl. Science 278, 853–856.
Cobine, P., George, G. N., Winzor, D. J., Harrison, M. D., Mogahaddas, S., and Dameron, C. T. (2000) Stoichiometry of complex formation between copper(I) and the N-terminal domain of the Menkes protein. Biochemistry 39, 6857–6863.
Ralle, M., Cooper, M. J., Lutsenko, S., and Blackburn, N. J. (1998) The Menkes disease protein binds copper via novel 2-coordinate Cu(I)-cysteines in the N-terminal comain. J. Am. Chem. Soc. 120, 13,525–13, 526.
DiDonato, M., Narindrasorasaki, S., Forbes, J. R., Cox, D. W., and Sarkar, B. (1997) Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B). J. Biol. Chem. 272, 33,279–33, 282.
Desideri, A., Hartmann, H. J., Morante, S., and Weser, U. (1990) An EXAFS study of the copper accumulated by yeast cells. Biol. Met. 3, 45–47.
Ford, P. C., Cariati, E., and Bourassa, J. (1999) Photoluminescence properties of multinuclear copper(I) compounds. Chem. Rev. 99 (12), 3625–3648.
Brown, N. L., Camakaris, J., Lee, B. T. O., Williams, T., Morby, A. P., Parkhill, J., et al. (1991) Bacterial resistances to mercury and copper. J. Cell. Biochem. 46, 106–114.
Thorvaldsen, J. L., Sewell, A. K., McCowen, C. L., and Winge, D. R. (1993) Regulation of metallothionein genes by the ACE1 and AMT] transcription factors. J. Biol. Chem. 268, 12,512–12, 518.
Georgatsou, E., Mavrogiannis, L. A., Fragiadakis, G. S., and Alexandraki, D. (1997) The yeast Frelp/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Maclp activator. J. Biol. Chem. 272(21), 13,786–13, 792.
Borghouts, C. and Osiewacz, H. D. (1998) GRISEA, a copper-modulated transcription factor from Podospora anserina involved in senescence and morphogenesis, is an orthology of MAC1 in Saccharomyces cerevisiae. Mol. Gen. Genet. 260 (5), 492–502.
Winge, D. R., Graden, J. A., Posewitz, M. C., Martins, L. J., Jensen, L. T., and Simon, J. R. (1997) Sensors that mediate copper-specific activation and repression of gene expression. J. Biol. Inorg. Chem. 2, 2–10.
Huffman, D. L. and O’Halloran, T. V. (2000) Energetics of copper trafficking between the Atxl metallochaperone and the intracellular copper transporter, Ccc2. J. Biol. Chem. 275, 18,611–18, 614.
Schmidt, P. J., Rae, T. D., Pufahl, R. A., Hamma, T., Strain, J., O’Halloran, T. V., et al. (1999) Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase. J. Biol. Chem. 274(34), 23,719–23, 725.
Eisses, J. F., Strasser, J. P., Ralle, M., Kaplan, J. H., and Blackburn, N. J. (2000) Domains I and III of the human copper chaperone for superoxide dismutase interact via a cysteine-bridged dicopper(I) cluster. Biochemistry 39 (25), 7337–7342.
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, 12, 775–12, 779.
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.
Voskoboinik, I., Strausak, D., Greenough, M., Brooks, H., Petris, M., Smith, S., et al. (1999) Functional analysis of the N-terminal CXXC metal-binding motifs in the human Menkes copper-transporting P-tuype ATPase expressed in cultured mammalian cells. J. Biol. Chem. 274, 22, 008–22, 012.
Harrison, M. D., Meier, S., and Dameron, C. T. (1999) Characterisation of copper-binding to the second subdomain of the Menkes protein (MNKr2). Biochim. Biophys. Acta 1453, 254–260.
Portnoy, M. E., Rosenzweig, A. C., Rae, R., Huffman, D. L., O’Halloran, T. V., and Culotta, V. C. (1999) Structure—function analysis of the ATXI metallochaperone. J. Biol. Chem. 274, 15,041–15, 045.
Cobine, P., Jones, C. E., Deecke, L. N., Wickramasinghe, W. A., and Dameron, C. T. (2000) Unlocking the key-lock mechanism for copper chaperones. Metal Ions in Biology and Medicine (Centeno, J. A., Collerry, P., Vernet, G., Finkelman, R. B., Gibb, H., and Etienne, J.-C., eds.), John Libbey Eurotext, Montrouge, France, Vol. 6, pp. 691–693.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media New York
About this chapter
Cite this chapter
Cobine, P.A., Jones, C.E., Wickramasinghe, W.A., Solioz, M., Dameron, C.T. (2002). Interaction of Copper-Binding Proteins from Enterococcus hirae . In: Massaro, E.J. (eds) Handbook of Copper Pharmacology and Toxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-288-3_9
Download citation
DOI: https://doi.org/10.1007/978-1-59259-288-3_9
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-61737-266-7
Online ISBN: 978-1-59259-288-3
eBook Packages: Springer Book Archive