Copper homeostasis in Enterococcus hirae

FEMS Microbiology Reviews

Volumn 27, Issue 2-3, 2003, Pages 183-195

  Solioz, Marc ^a   Stoyanov, Jivko V ^a  

^a UNIVERSITY OF BERN   (Switzerland)

Author keywords

ATPase; Copper; Enterococcus; Metallochaperone; Resistance; Silver

Indexed keywords

COPPER ION; OXIDOREDUCTASE;

BACTERIAL STRAIN; COPPER METABOLISM; ELECTRIC CAPACITANCE; ENTEROCOCCUS HIRAE; HOMEOSTASIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; REVIEW;

ENTEROCOCCUS; ENTEROCOCCUS HIRAE;

EID: 0037565100     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(03)00053-6     Document Type: Review

References (102)

1. Tylecote, R.F. (1992) A History of Metallurgy. Institute of Materials, London.
2. Karlin K.D. Metalloenzymes, structural motifs, and inorganic models. Science. 261:1993;701-708.
3. Bell P.F., Chen Y., Potts W.E., Chaney R.L., Angle J.S. A reevaluation of the Fe(III), Ca(II), Zn(II), and proton formation constants of 4,7-diphenyl-1,10-phenanthrolinedisulfonate. Biol. Trace Elem. Res. 30:1991;125-144.
4. +, ein Mittel zum Studium homogener Reaktionen des einwertigen Kupfers in wässriger Lösung. Experientia. 19:1963;488-489.
5. McPhail D.B., Goodman B.A. Tris buffer - a case for caution in its use in copper-containing systems (letter). Biochem. J. 221:1984;559-560.
6. Bissig K.D., Voegelin T.C., Solioz M. Tetrathiomolybdate inhibition of the Enterococcus hirae CopB copper ATPase. FEBS Lett. 507:2001;367-370.
7. Brewer G.J., Johnson V., Dick R.D., Kluin K.J., Fink J.K., Brunberg J.A. Treatment of Wilson disease with ammonium tetrathiomolybdate. II. Initial therapy in 33 neurologically affected patients and follow-up with zinc therapy. Arch. Neurol. 53:1996;1017-1025.
8. Andrews N.C. Metal transporters and disease. Curr. Opin. Chem. Biol. 6:2002;181-186.
9. Yoshida Y., Furuta S., Niki E. Effects of metal chelating agents on the oxidation of lipids induced by copper and iron. Biochim. Biophys. Acta. 1210:1993;81-88.
10. Cadenas, E., Brigelius, R., Akerboom, T. and Sies, H. (1983) Oxygen radicals and hydroperoxides in mammalian organs: aspects of redox cycling and hydrogen peroxide metabolism. In: 34. Kolloquium Moosbach; Biological Oxidations (Sund, H. and Ullrich, V., Eds.), pp. 288-310. Springer, Berlin.
11. Klotz, L.-O. and Weser, U. (1998) Biological chemistry of copper compounds. In: Copper and Zinc in Degenerative Diseases (Rainsford, K.D., Ed.), pp. 19-46. Kluwer Academic Publishers, Dordrecht.
12. Fahey R.C., Brown W.C., Adams W.B., Worsham M.B. Occurrence of glutathione in bacteria. J. Bacteriol. 133:1978;1126-1129.
13. Newton G.L., Arnold K., Price M.S., Sherrill C., Delcardayre S.B., Aharonowitz Y., Cohen G., Davies J., Fahey R.C., Davis C. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J. Bacteriol. 178:1996;1990-1995.
14. Freedman J.H., Ciriolo M.R., Peisach J. The role of glutathione in copper metabolism and toxicity. J. Biol. Chem. 264:1989;5598-5605.
15. Kocha T., Yamaguchi M., Ohtaki H., Fukuda T., Aoyagi T. Hydrogen peroxide-mediated degradation of protein: different oxidation modes of copper- and iron-dependent hydroxyl radicals on the degradation of albumin. Biochim. Biophys. Acta. 1337:1997;319-326.
16. Cha J.S., Cooksey D.A. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc. Natl. Acad. Sci. USA. 88:1991;8915-8919.
17. Solioz M., Bissig K.-D. How (deficient) copper causes illness. Schweiz. Med. Wochenschr. 128:1998;1175-1180.
18. Lu Z.H., Cobine P., Dameron C.T., Solioz M. How cells handle copper: A view from microbes. J. Trace Elem. Exp. Med. 12:1999;347-360.
19. Solioz M., Odermatt A., Krapf R. Copper pumping ATPases: common concepts in bacteria and man. FEBS Lett. 346:1994;44-47.
20. Wunderli-Ye H., Solioz M. Copper homeostasis in Enterococcus hirae. Adv. Exp. Med. Biol. 448:1999;255-264.
21. Solioz, M. and Stoyanov, J.V. (2002) How cells deal with copper: a lesson from bacteria. In: Macro and Trace Elements (Anke, M., Müller, R., Schäfer, U. and Stoeppler, M., Eds.), pp. 485-492. Schubert-Verlag, Leipzig.
22. Odermatt A., Suter H., Krapf R., Solioz M. An ATPase operon involved in copper resistance by Enterococcus hirae. Ann. N.Y. Acad. Sci. 671:1992;484-486.
23. Chelly J., Tumer Z., Tonnesen T., Petterson A., Ishikawa Brush Y., Tommerup N., Horn N., Monaco A.P. Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein. Nat. Genet. 3:1993;14-19.
24. Mercer J.F.B., Livingston J., Hall B., Paynter J.A., Begy C., Chandrasekharappa S., Lockhart P., Grimes A., Bhave M., Siemieniak D., Glover T.W. Isolation of a partial candidate gene for Menkes disease by positional cloning. Nat. Genet. 3:1993;20-25.
25. Vulpe C., Levinson B., Whitney S., Packman S., Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat. Genet. 3:1993;7-13.
26. Tanzi R.E., Petrukhin K., Chernov I., Pellequer J.L., Wasco W., Ross B., Romano D.M., Parano E., Pavone L., Brzustowicz L.M. The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene. Nat. Genet. 5:1993;344-350.
27. Bull P.C., Thomas G.R., Rommens J.M., Forbes J.R., Cox D.W. The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nat. Genet. 5:1993;327-337.
28. Solioz, M. (2001) Bacterial copper transport. In: Microbial Transport Systems (Winkelmann, G., Ed.), pp. 361-376. Wiley, Weinheim.
29. Bissig, K.-D., Wunderli-Ye, H. and Solioz, M. (2000) Copper Homeostasis in Enterococcus hirae: Pumps, Repressor, Chaperone, pp. 133-136. John Libbey Eurotext, Paris.
30. Solioz, M. (1998) Copper homeostasis by CPX-type ATPases, the subclass of heavy metal P-type ATPases. In: Ion Pumps (Andersen, J.P., Ed.), pp. 167-203. JAI Press, London.
31. Lu Z.H., Solioz M. Bacterial copper transport. Adv. Protein Chem. 60:2002;93-121.
32. Pedersen P.L., Carafoli E. Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem. Sci. 12:1987;146-150.
33. Toyoshima C., Nakasako M., Nomura H., Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature. 405:2000;647-655.
34. Lutsenko S., Kaplan J.H. Organization of P-type ATPases: Significance of structural diversity. Biochemistry. 34:1995;15607-15613.
35. Solioz M., Vulpe C. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21:1996;237-241.
36. Toyoshima C., Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature. 418:2002;605-611.
37. Tottey S., Rich P.R., Rondet S.A., Robinson N.J. Two Menkes-type atpases supply copper for photosynthesis in Synechocystis PCC 6803. J. Biol. Chem. 276:2001;19999-20004.
38. Rutherford J.C., Cavet J.S., Robinson N.J. Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase. J. Biol. Chem. 274:1999;25827-25832.
39. Rasmussen B. Filamentous microfossils in a 3,235-million-year-old volcanogenic massive sulphide deposit. Nature. 405:2000;676-679.
40. Zierenberg R.A., Adams M.W., Arp A.J. Life in extreme environments: Hydrothermal vents. Proc. Natl. Acad. Sci. USA. 97:2000;12961-12962.
41. Kaim W., Rall J. Copper - a 'modern' bioelement. Angew. Chem. Int. Ed. Engl. 35:1996;43-60.
42. + extrusion by CopB. Biochem. Biophys. Res. Commun. 202:1994;44-48.
43. Wunderli-Ye H., Solioz M. Purification and functional analysis of the copper ATPase CopA of Enterococcus hirae. Biochem. Biophys. Res. Commun. 280:2001;713-719.
44. 2Cys motifs are not required for copper resistance or transport. Biochem. Biophys. Res. Commun. 286:2001;414-418.
45. Solioz M., Odermatt A. Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae. J. Biol. Chem. 270:1995;9217-9221.
46. Voskoboinik I., Greenough M., La Fontaine S., Mercer J.F., Camakaris J. Functional studies on the Wilson copper P-Type ATPase and toxic milk mouse mutant. Biochem. Biophys. Res. Commun. 281:2001;966-970.
47. Voskoboinik I., Brooks H., Smith S., Shen P., Camakaris J. ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells. FEBS Lett. 435:1998;178-182.
48. Francis M.S., Thomas C.J. Mutants in the CtpA copper transporting P-type ATPase reduce virulence of Listeria monocytogenes. Microb. Pathog. 22:1997;67-78.
49. Francis M.S., Thomas C.J. The Listeria monocytogenes gene ctpA encodes a putative P-type ATPase involved in copper transport. Mol. Gen. Genet. 253:1997;484-491.
50. Lowe A.M., Beattie D.T., Deresiewicz R.L. Identification of novel staphylococcal virulence genes by in vivo expression technology. Mol. Microbiol. 27:1998;967-976.
51. Mellano M.A., Cooksey D.A. Nucleotide sequence and organization of copper resistance genes from Pseudomonas syringae pv. tomato. J. Bacteriol. 170:1988;2879-2883.
52. Cooksey D.A. Molecular mechanisms of copper resistance and accumulation in bacteria. FEMS Microbiol. Rev. 14:1994;381-386.
53. Wyler-Duda P., Solioz M. Phosphoenzyme formation by purified, reconstituted copper ATPase of Enterococcus hirae. FEBS Lett. 399:1996;143-146.
54. Bissig K.-D., Wunderli-Ye H., Duda P., Solioz M. Structure-function analysis of purified Enterococcus hirae CopB copper ATPase: Effect of Menkes/Wilson disease mutation homologues. Biochem. J. 357:2001;217-223.
55. Baerlocher, K. and Solioz, M. (2002) Disorders of copper, zinc and iron metabolism. In: A Physician's Guide to the Laboratory - Diagnosis of Inherited Metabolic Disease (Blau, N., Duran, M. and Blaskovics, M.E., Eds.), in press.
56. Lee Y.A., Hendson M., Panopoulos N.J., Schroth M.N. Molecular cloning, chromosomal mapping, and sequence analysis of copper resistance genes from Xanthomonas campestris pv Juglandis - homology with small blue copper proteins and multicopper oxidase. J. Bacteriol. 176:1994;173-188.
57. Mills S.D., Lim C.-K., Cooksey D.A. Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae. Mol. Gen. Genet. 244:1994;341-351.
58. Brown N.L., Barrett S.R., Camakaris J., Lee B.T.O., Rouch D.A. Molecular genetics and transport analysis of the copper-resistance determinant (pco) from Escherichia coli plasmid pRJ1004. Mol. Microbiol. 17:1995;1153-1166.
59. Outten F.W., Outten C.E., Hale J., O'Halloran T.V. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, CueR. J. Biol. Chem. 275:2000;31024-31029.
60. Stoyanov J.V., Hobman J.L., Brown N.L. CueR (YbbI) of Escherichia coli is a MerR family regulator controlling expression of the copper exporter CopA. Mol. Microbiol. 39:2001;502-512.
61. Odermatt A., Solioz M. Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J. Biol. Chem. 270:1995;4349-4354.
62. Odermatt A., Suter H., Krapf R., Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268:1993;12775-12779.
63. Himeno T., Imanaka T., Aiba S. Nucleotide sequence of the penicillinase repressor gene penI of Bacillus licheniformis and regulation of penP and penI by the repressor. J. Bacteriol. 168:1986;1128-1132.
64. Suzuki E., Kuwahara Arai K., Richardson J.F., Hiramatsu K. Distribution of mec regulator genes in methicillin-resistant Staphylococcus clinical strains. Antimicrob. Agents Chemother. 37:1993;1219-1226.
65. Rowland S.J., Dyke K.G. Tn552, a novel transposable element from Staphylococcus aureus. Mol. Microbiol. 4:1990;961-975.
66. Wittman V., Wong H.C. Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators. J. Bacteriol. 170:1988;3206-3212.
67. Anderson J.E., Ptashne M., Harrison S.C. Structure of the repressor-operator complex of bacteriophage 434. Nature. 326:1987;846-852.
68. Zhou P.B., Thiele D.J. Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 88:1991;6112-6116.
69. Dobi A., Dameron C.T., Hu S., Hamer D., Winge D.R. Distinct regions of Cu(I)·ACE1 contact two spatially resolved DNA major groove sites. J. Biol. Chem. 270:1995;10171-10178.
70. + coordination-dependent DNA binding of the transcription factor Mac1p in the regulation of copper transport. J. Biol. Chem. 276:2001;8793-8797.
71. 1 NMR assignments reflecting conformational heterogeneity at the C-terminus. Biochemistry. 32:1993;6773-6787.
72. Strausak D., Solioz M. CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases. J. Biol. Chem. 272:1997;8932-8936.
73. Wunderli-Ye H., Solioz M. Effects of promoter mutations on the in vivo regulation of the cop operon of Enterococcus hirae by copper(I) and copper(II). Biochem. Biophys. Res. Commun. 259:1999;443-449.
74. Cobine P., Wickramasinghe W.A., Harrison M.D., Weber T., Solioz M., Dameron C.T. The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor. FEBS Lett. 445:1999;27-30.
75. Cobine, P., Jones, C.E., Wickramasinghe, W.A., Solioz, M. and Dameron, C.T. (2002) Interaction of copper binding proteins from Enterococcus hirae. In: Handbook of Copper Pharmacology and Toxicology (Massaro, E.J., Ed.), pp. 177-186. Humana Press, Totowa, NJ.
76. Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M., Dameron C.T. Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: Metal coordination environments and protein interactions. Biochemistry. 41:2002;5822-5829.
77. Cobine P.A., Jones C.E., Dameron C.T. Role for zinc(II) in the copper(I) regulated protein CopY. J. Inorg. Biochem. 88:2002;192-196.
78. Endo G., Silver S. CadC, the transcriptional regulatory protein of the cadmium resistance system of Staphylococcus aureus plasmid pI258. J. Bacteriol. 177:1995;4437-4441.
79. O'Halloran T.V., Culotta V.C. Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275:2000;25057-25060.
80. Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C. Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry. 39:2000;14720-14727.
81. Huffman D.L., O'Halloran T.V. Function, structure, and mechanism of intracellular copper trafficking proteins. Annu. Rev. Biochem. 70:2001;677-701.
82. Harrison M.D., Jones C.E., Solioz M., Dameron C.T. Intracellular copper routing: The role of copper chaperones. Trends Biochem. Sci. 25:2000;29-32.
83. Rosenzweig A.C. Copper delivery by metallochaperone proteins. Acc. Chem. Res. 34:2001;119-128.
84. Wimmer R., Herrmann T., Solioz M., Wüthrich K. NMR structure and metal interactions of the CopZ copper chaperone. J. Biol. Chem. 274:1999;22597-22603.
85. Wimmer, R., Dameron, C.T. and Solioz, M. (2002) Molecular hardware of copper homeostasis in Enterococcus hirae. In: Handbook of Copper Pharmacology and Toxicology (Massaro, E.J., Ed.), pp. 527-542. Humana Press, Totowa, NJ.
86. Multhaup G., Strausak D., Bissig K.-D., Solioz M. Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance. Biochem. Biophys. Res. Commun. 288:2001;172-177.
87. Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V. Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J. Biol. Chem. 276:2001;41365-41376.
88. Brown N.L., Camakaris J., Lee B.T., Williams T., Morby A.P., Parkhill J., Rouch D.A. Bacterial resistances to mercury and copper. J. Cell Biochem. 46:1991;106-114.
89. Pufahl R.A., Singer C.P., Peariso K.L., Lin S., Schmidt P.J., Fahrni C.J., Culotta V.C., Penner-Hahn J.E., O'Halloran T.V. Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science. 278:1997;853-856.
90. Lu Z.H., Solioz M. Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae. J. Biol. Chem. 276:2001;47822-47827.
91. Lu Z.H., Dameron C.T., Solioz M. The Enterococcus hirae paradigm of copper homeostasis: Copper chaperone turnover, interactions, and transactions. Biometals. 16:2003;137-143.
92. Solioz M. Role of proteolysis in copper homeostasis. Biochem. Soc. Trans. 30:2002;688-691.
93. Gottesman S., Maurizi M.R. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56:1992;592-621.
94. Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:1996;465-506.
95. Ooi C.E., Rabinovich E., Dancis A., Bonifacino J.S., Klausner R.D. Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis. EMBO J. 15:1996;3515-3523.
96. Zhu Z., Labbe S., Pena M.M., Thiele D.J. Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor. J. Biol. Chem. 273:1998;1277-1280.
97. Li H.H., Merchant S. Degradation of plastocyanin in copper-deficient Chlamydomonas reinhardtii. Evidence for a protease-susceptible conformation of the apoprotein and regulated proteolysis. J. Biol. Chem. 270:1995;23504-23510.
98. Rapisarda V.A., Montelongo L.R., Farias R.N., Massa E.M. Characterization of an NADH-linked cupric reductase activity from the Escherichia coli respiratory chain. Arch. Biochem. Biophys. 370:1999;143-150.
99. Rapisarda V.A., Chehin R.N., De Las R.J., Rodriguez-Montelongo L., Farias R.N., Massa E.M. Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2. Arch. Biochem. Biophys. 405:2002;87-94.
100. Wunderli-Ye, H. and Solioz, M. (1998) Regulation of the cop operon of Enterococcus hirae by the CopY repressor and copper. In: Metal Ions in Biology and Medicine (Collery, P., Brätter, P., Negretti de Brätter, V., Khassanova, L. and Etienne, J.-C., Eds.), pp. 109-113. John Libbey Eurotext, Paris.
101. Hassett R., Kosman D.J. Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae. J. Biol. Chem. 270:1995;128-134.
102. Rawlings D.E. Heavy metal mining using microbes. Annu. Rev. Microbiol. 56:2002;65-91.