Abstract
Copper and iron are essential micronutrients for all organisms because of their function as cofactors in enzymes that catalyze redox reactions in fundamental metabolic processes. Prominent examples of such enzymes include cytochrome oxidase in respiration, plastocyanin in photosynthesis, superoxide dismutase in oxidative stress, and ceruloplasmin in iron metabolism. Copper and iron carry out very similar functions in biology because both exhibit stable, redox-interchangeable ionic states with the potential to generate less stable electron-deficient intermediates during multielectron redox reactions involving oxygen chemistry. The major difference between copper and iron in biological systems derives from their individual ligand preferences and coordination geometries. The bioavailability of copper and iron is low so that organisms are faced with the challenge of acquiring sufficient copper and iron for cellular requirements while avoiding the buildup of levels that could lead to cellular toxicity. Over the last decade, it has become apparent that organisms have developed a suite of strategies to combat such challenges, so that an intricate balance between uptake, utilization, storage and detoxification, and efflux pathways for copper and iron exists.
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References
Askwith, C. and Kaplan, J. (1998) Iron and copper transport in yeast and its relevance to human disease. Trends Biochem. Sci. 23, 135–138.
Labbe, S. and Thiele, D. J. (1999) Pipes and wiring: the regulation of copper uptake and distribution in yeast. Trends Microbiol. 7, 500–505.
Dancis, A., Haile, D., Yuan, D. S., et al. (1994) The Saccharomyces cerevisiae copper transport protein (Ctrlp). J. Biol. Chem. 269, 25,660–25, 667.
Pena, M. M. O., Puig, S., and Thiele, D. J. (2000) Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3. J. Biol. Chem. 275, 33,244–33, 251.
Pena, M. M. O., Lee, J., and Thiele, D. J. (1999) A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129, 1251–1260.
Georgatsu, E., Mavrogiannis, L. A., Fragiadakis, G. S., et al. (1997) The yeast Frelp/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Maclp activator. J. Biol. Chem. 272, 13,786–13, 792.
Hassett, R. and Kosman, D. J. (1995) Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae. J. Biol. Chem. 270, 128–134.
Eide, D. J. (1998) The molecular biology of metal ion transport in Saccharomyces cerevisiae. Annu. Rev. Nutr. 18 441–469.
Gross, C., Kelleher, M., Iyer, V. R., et al. (2000) Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays. J. Biol. Chem. 275, 32,310–32, 316.
Winge, D. R., Jensen, L. T., and Srinivasan, C. (1998) Metal-ion regulation of gene expression in yeast. Curr. Opin. Chem. Biol. 2, 216–221.
Ooi, C. E., Rabinovich, E., Dancis, A., et aI. (1996) Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane transporter Ctrlp in the apparent absence of endocytosis. EMBO J. 15, 3515–3523.
Hassett, R., Dix, D. R. Eide, D. J., et al. (2000) The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saccharomyces cerevisiae. Biochem. J. 351 477–484.
Cohen, A., Nelson, H., and Nelson, N. (2000) The family of SMF metal ion transporters in yeast cells. J. Biol. Chem. 275, 33,388–33, 394.
Radisky, D. and Kaplan, J. (1999) Regulation of transition metal transport across the yeast plasma membrane. J. Biol. Chem. 274, 4481–4484.
Kampfenkel, K., Kushnir, S., Babiychuk, E., et al. (1995) Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue. J. Biol. Chem. 47, 28,479–28, 486.
Harrison, M., Jones, C. E., and Dameron, C. T. (1999) Copper chaperones: function, structure and coper-binding properties. J. Biol. Inorg. Chem. 4, 145–153.
Harrison, M. D., Jones, C. E., Solioz, M., et al. (2000) Intracellular copper routing: the role of copper chaperones. TIES 25, 29–32.
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.
Valentine, J. S. (1997) Delivering copper inside yeast and human cells. Science, 278, 817–818.
Culotta, V. C., Sturtz, L., Jensen, L., et al. (2001) Metals and oxidative stress: new insights from yeast. J. Exp. Bot. 52 (Suppl.). 61.
Yuan, D. S., Stearman, R., Dancis, A., et al. (1995) The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc. Natl. Acad. Sci. USA, 92, 2632–2636.
Davis-Kaplan, S. R., Askwith, C. C., Bengtzen, A. C., et al. (1998) Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels. Proc. Natl. Acad. Sci. USA 95, 13,641–13, 645.
Gaxiola, R. A., Yuan, D. S., Klausner, R. D., et al. (1998) The yeast CLC chloride channel functions in cation homeostasis. Proc. Natl. Acad. Sci. USA, 95, 4046–4050.
Glerum, D. M., Shtanko, A., and Tzagoloff, A. (1996) SCOI and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271 20,531–20,535.
Rentzsch, A., Krummeck-Weiß, G., Hofer, A., et al. (1999) Mitochondria) copper metabolism in yeast: mutational analysis of Scolp involved in the biogenesis of cytochrome c oxidase. Curr. Genet. 35, 10–108.
Martins, L. J., Jensen, L. T., Simons, J. R.. et al. (1998) Metalloregulation of FREI and FRE2 homology in Saccharomyces cerevisiae. J. Biol. Chem. 273 23,716–23,721.
Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., et al. (1996) A permease—oxidase complex involved in high-affinity iron uptake in yeast. Science 271, 1552–1557.
Askwith, C., Eide, D., Van Ho, A., et al. (1994) The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76, 403–410.
Askwith, C. and Kaplan, J. (1997) An oxidase—permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae. J. Biol. Chem. 272, 401–405.
Hammacott, J. E., Williams, P. H., and Cashmore, A. M. (2000) Candida albicans CFL1 encodes a functional ferric reductase activity that can rescue a Saccharomyces cerevisiae fie) mutant. Microbiology 146, 869–876.
Ramanan, N. and Wang, Y. (2000) A high-affinity iron permease essential for Candida albicans virulence. Science 288, 1062–1064.
Dix, D., Bridgham, J., Broderius, M., et al. (1997) Characterization of the FET4 protein of yeast. Evidence for a direct role in the transport of iron. J. Biol. Chen. 272, 11,770–11, 777.
Yun, C.-W., Ferea, T. Rashford, J. et al. (2000) Desferrioxamine-mediated iron uptake in Saccharomyces cereivisiae. Evidence for two pathways of iron uptake. J. Biol. Chem. 275 10,709–10,715.
Yun, C.-W., Tiedeman, J. S., Moore, R. E., et al. (2000) Siderophore—iron uptake in Saccharomyces cerevisiae. Identification of ferrichrome and fusarinine transporters. J. Biol. Chem. 275, 16,354–16, 359.
Heymann, P., Ernst, J. F., and Winkelmann, G. (1999) Identification of a fungal triacetylfusarinine C siderophore transport gene (TAFI) in Saccharomyces cerevisiae as a member of the major facilitator superfamily. Biometals 12, 301–306.
Heymann, P., Ernst, J. F., and Winkelmann, G. (2000) Identification and substrate specificity of a ferrichrome-type siderophore transporter (Arnlp) in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 186, 221–227.
Lesuisse, E., Blaiseau, P. L., Dancis, A., et al. (2001) Siderophore uptake and use by the yeast Saccharomyces cerevisiae. Microbiology 147 (Pt. 2), 289–298.
Lesuisse, E., Simon-Casteras, M., and Labbe, P. (1998) Siderophore-mediated iron uptake in Saccharomyces cerevisiae: the SIT1 gene encodes a ferrioxamine B permease that belongs to the major facilitator superfamily. Microbiology 144 (Pt. 2), 3455–3462.
Klionsky, D. J., Herman, P. K., and Emr, S. D. (1990) The fungal vacuole: composition, function and biogenesis. Microbiol. Rev. 54, 266–292.
Raguzzi, F., Lesuisse, E., and Chrichton, R.R. (1988) Iron storage in Saccharornyces cerevisiae. FEBS Lett. 231, 253258.
Urbanowski, J. L. and Piper, R. C. (1999) The iron transporter Fthlp forms a complex with the FetS iron oxidase and resides on the vacuolar membrane. J. Biol. Chem, 274, 38,061–38, 070.
Babcock, M., Silva, D. D., Oaks, R., et al. (1997) Regulation of mitochondrial iron accumulation by Yfhl, a putative homolog of frataxin. Science 276, 1709–1712.
Radisky, D. C., Babcock, M. C., and Kaplan, J. (1999) The yeast frataxin homologue mediates mitochondrial iron efflux. J. Biol. Chem. 274, 4497–4499.
Chen, O. S. and Kaplan, J. (2000) CCCI supresses mitochondrial damage in the yeast model of Friedreich’s ataxia by limiting mitochondrial iron accumulation. J. Biol. Chem. 275, 7626–7632.
Kispal, G., Csere, P., Prohl, C., et al. (1999) The mitochondrial proteins Atmlp and Nfslp are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981–3989.
Li, J., Kogan, M. Knight, S. A. B. et al. (1999) Yeast mitochondrial protein, Nfslp, coordinately regulates iron-sulphur cluster proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274 33,025–33,034.
Leighton, J. and Schatz, G. (1995) An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast. EMBO J. 4, 188–195.
Knight, S. A. B., Sepuri, N. B. V., Pain, D., et al. (1998) Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273 18,389–18,393.
Jensen, L. and Culotta, V. (2000) Role of Saccharomyces’ cerevisiae ISA1 and ISA2 in iron homeostasis. Mol. Cell. Biol. 20, 3919–3927.
Robertson, L. S., Causton, H. C., Young, R. A., et al. (2000) The yeast A kinases differentially regulate iron uptake and respiratory function. Proc. Natl. Acad. Sci. USA 97, 5984–5988.
Dancis, A., Roman, D. G., Anderson, G. J., et al. (1992) Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron. Proc. Natl. Acad. Sci. USA 89, 3869–3873.
Jungmann, J., Reins, H., Lee, J., et al. (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.
Lin, S.-J., Pufahl, R. A., Dancis, A., et al. (1997) A role for the Saccharomyces cerevisiae ATXI gene in copper trafficking and iron transport. J. Biol. Chem. 272, 9215–9220.
Yamaguchi-Iwai, Y., Stearman, R., Dancis, A., et al. (1996) Iron-regulated DNA binding by the AFT] protein controls the iron regulation in yeast. EMBO J. 15, 3377–3384.
Labbe, S., Pena, M. M. O., Fernandes, A. R., et al. (1999) A copper-sensing transcription factor regulates iron uptake genes in Saccharomyces pombe. J. Biol. Chem. 274, 36,252–36, 260.
Elvehjem, C. A. (1935) The biological significance of copper and its relation to iron metabolism. Physiol. Rev. 15, 471–507.
Hart, E. B., Steenbock, H., Waddell, J., et al. (1928) Iron in nutrition. VII. Copper as a supplement to iron for hemoglobin building in the rat. J. Biol. Chem. 77, 797–812.
Holmberg, C. G. and Laurell, C. B. (1948) Investigations in serum copper. II. Isolation of the copper-containing protein, and a description of some of its properties. Acta Chem. Scand. 2, 550–556.
Eisenstein, R. S. (2000) Discovery of the ceruloplasmin homologue hephaestin: new insight into the copper/iron connection. Nutr. Rev. 58, 22–26.
Vulpe, C. D., Kuo, Y. M., Murphy, T. L., et al. (1999) Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nature Genet. 21, 195–199.
Crampton, R. F., Matthews, D. M., and Poisner, R. (1965) Observations on the mechanism of absorption of copper by the small intestine. J. Physiol. 178, 111–126.
Van Campen, D.R. (] 971) Absorption of copper from the gastrointestinal tract, in Intestinal Absorption of Metal Ions, Trace Elements and Radionuclides (Skoryna, S. C. and Waldron-Edwards, D., eds.), Pergamon, Oxford, pp. 211–227.
Zhou, B. and Gitschier, J. (1997) hCTRI: a human gene for copper uptake identified by complementation in yeast. Proc. Natl. Acad. Sci. USA 94, 7481–7486.
Lee, J. and Thiele, D. J. (2001) Essential role for mammalian copper transporters in copper homeostasis and embryonic development. J. Exp. Bot. 52 (Suppl.), 84.
Hamza, I. Schaefer, M., Klomp, L. W. J. et al. (1999) Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis. Proc. Natl. Acad. Sci. USA 96 13,363–13,368.
Larin, D., Mekios, C., Das, K., et al. (1999) Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1P. J. Biol. Chem. 274, 28,497–28, 504.
Hamza, I., Chen, J. Gitlin, J. D., et al. (2001) Critical role for metallochaperone Atoxl in perinatal copper homeostasis. J. Exp. Bot. 52(Suppl.) 84.
Petris, M. J., Strausak, D. and Mercer, J. F. B. (2000) The Menkes copper transporter is required for the activation of tyrosinase. Hum. Mol. Genet. 9, 2845–2851.
Petris, M. J., Mercer, J. F. B., Culvenor, J. G. et al. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15, 6084–6095.
Petris, M. J., Mercer, J. F. B., and Camakaris, J. (1999) The cell biology of the Menkes disease protein. Adv. Exp. Biol. Med. 448, 53–66.
Petris, M. J., Camakaris, J., Greenough, M., et al. (1998) A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum. Mol. Genet. 7, 2063–2071.
Petris, M. J. and Mercer, J. F. B. (1999) The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum. Mol. Genet. 8, 2107–2115.
Linder, M. C., Wooten, L., Cerveza, P., et al. (1998) Copper transport. Am. J. Clin. Nutr. 67, 965S - 9715.
Hung, I. H., Suzuki, M., Yamaguchi, Y., et al. (1997) Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272, 21,461–21, 466.
Schaefer, M., Hopkins, R. G., Failla, M. A., et al. (1999) Hepatocyte-specific localization and copper-dependent trafficking of the Wilson’s disease protein in the liver. Am. J. Physiol. 276, G639 — G646.
Suzuki, M. and Gitlin, J. D. (1999) Intracellular localization of the Menkes and Wilson’s disease proteins and their role in intracellular copper transport. Pediatr. Int. 41, 436–442.
Terada, K., Aiba, N., Yang, X.-L. et al. (1999) Biliary excretion of copper in LEC rat after introduction of copper transporting P-type ATPase, ATP7B. FEBS Lett. 448, 53–56.
Terada, K., Nakako, T., Yang, X.-L., et al. (1998) Restoration of holoceruloplasmin synthesis in LEC rat after infusion of recombinant adenovirus bearing WND cDNA. J. Biol. Chem. 273, 1815–1820.
Sato, M. and Gitlin, J. D. (1991) Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin. J. Biol. Chem. 266, 5128–5134.
Holmberg. C. G. and Laurell, C. B. (1948) Investigations in serum copper. H. Isolation of the copper containing protein and a description of some of its properties. Acta Chem. Scand. 2, 550–556.
Winzerling, J. J. and Law, J. H. (1997) Comparative nutrition of iron and copper. Annu. Rev. Nutr. 17, 501–526.
Linder, M.C. (1991) Biochemistry of Copper, Plenum, New York.
Evans. G. W. (1973) Copper homeostasis in the mammalian system. Physiol. Rev. 53, 535–569.
Dameron, C. T. and Harrison, M. D. (1998) Mechanisms for protection against copper toxicity. Am. J. Clin. Nutr. 67 (Suppl.), 10915–1097S.
Miles, A. T., Hawksworth, G. M., Beattie, J. H., et al. (2000) Induction, regulation, degradation, and biological significance of mammalian metallothioneins. Crit. Rev. Biochem. Mol. Biol. 35, 35–70.
Vasak, M. and Hasler, D. W. (2000) Metallothioneins: new functional and structural insights. Curr. Opin. Chem. Biol. 4, 177–183.
Labbe, S., Simard, C., and Seguin, C. (1997) Metallothionein gene regulation in mouse cells, in Metal Ions in Gene Regulation ( Silver, S. and Walden, W., eds.), Chapman and Hall, New York, pp. 231–249.
Remondelli, P., Moltedo, O., Pascale, M. C., et al. (1999) Metal regulation of metallothionein gene transcription in mammals. Adv. Exp. Med. Biol. 448, 223–236.
Andrews, N. C. (1999) The iron transporter DMT1. Int. J. Biochem. Cell Biol. 31, 991–994.
Aisen, P., Wessling-Resnick, M., and Leibold, E. A. (1999) Iron metabolism. Curr. Opin. Chem. Biol. 3, 200–206.
Schneider, B. D. and Leibold, E. A. (2000) Regulation of mammalian iron homeostasis. Curr. Opin. Clin. Nutr. Metab. Care 3, 267–273.
Tandy, S., Williams, M., Leggett, A., et al. (2000) Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J. Biol. Chem. 275, 1023–1029.
Bennett, M. J., Lebron, J. A., and Bjorkman, P. J. (2000) Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 403, 46–53.
Riedel, H. D., Muckenthaler, M. U., Gehrke, S. G., et al. (1999) HFE downregulates iron uptake from transferrin and induces iron-regulatory protein activity in stably transfected cells. Blood 94, 3915–3921.
Han, O., Fleet, J. C., and Wood, R. J. (1999) Reciprocal regulation of HFE and Nramp2 gene expression by iron in human intestinal cells. J. Nutr. 129, 98–104.
Nelson, N. (1999) Metal ion transporters and homeostasis. EMBO J. 18, 4361–4371.
Haile, D. J. (1999) Regulation of genes of iron metabolism by the iron-response proteins. Am. J. Med. Sci. 318, 230–240.
Conrad, M. E., Umbreit, J. N., and Moore, E. G. (1999) Iron absorption and transport. Am. J. Med. Sci. 8, 213–229.
Donovan, A., Brownlie, A., Zhou, Y., et al. (2000) Positional cloning of zebrafish ferroportin 1 identifies a conserved vertebrate iron exporter. Nature 403, 776–781.
McKie, A. T., Marciani, P., Rolfs, A., et al. (2000) A novel duodenal iron-regulated membrane protein (Iregl) implicated in basolateral transfer of iron to the circulation. Mol. Cell, 5, 299–309.
Abboud, S. and Haile, D. J. (2000) A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275, 19,906–19, 912.
Kaplan, J. and Kushner, J. P. (2000) Mining the genome for iron. Nature 403, 712–713.
Andrews, N. C., Fleming, M. D., and Gunshin, H. (1999) Iron transport across biologic membranes. Nutr. Rev. 57, 745–748.
Tabuchi, M., Yoshimori, T., Yamaguchi, K., et al. (2000) Human NRAMP2/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells. J. Biol. Chem. 275, 22,22022, 228.
Rolfs, A. and Hediger, M. A. (2001) Intestinal metal ion absorption: an update. Curr. Opin. Gastroenterol. 17, 177–183.
Eisenstein, R. S. and Blemmings, K. P. (1998) Iron regulatory proteins, iron responsive elements and iron homeostasis. J. Nutr. 128, 2295–2298.
Kühn, L. C. (1998) Iron and gene expression: molecular mechanisms regulating cellular iron homeostasis. Nutr. Rev. 56, S11 — S19.
Thomson, A. M., Rogers, J. T., and Leedman, P. J. (1999) Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation. Int. J. Biochem. Cell Biol. 31, 1139–1152.
Fox, T. C. and Guerinot, M. L. (1998) Molecular biology of cation transport in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 669–696.
Hirayama, T., Kieber, J. J., Hirayama, N., et al. (1999) RESPONSE TO ANTAGONIST], a Menkes/Wilson disease-related copper transporter, is required for ethylene signaling in Arabidopsis. Cell, 97, 383–393.
Tabata, K., Kashiwagi, S., Mori, H., et al. (1997) Cloning of a cDNA encoding a putative metal-transporting P-type ATPase from Arabidopsis thaliana. Biochim. Biophys. Acta 1326, 1–6.
Pilon, M., Burkhead, J., and Pilon-Smits, E. A. H. (2001) Metal homeostasis in Arabidopsis chloroplasts: the roles of the copper binding protein AtCutAp and the P-type ATPase Paalp. J. Exp. Bot. 52(Suppl.) 65.
Kaneko, T., Kato, T., Sato, S., et al. (2000) Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the regions of 4,251,695 bp covered by ninety P1, TAC and BAC clones. DNA Res. 7, 217–221.
Zhu, H., Shipp, E., Sanchez, R. J., et al. (2000) Cobalt(2+) binding to human and tomato copper chaperone for superoxide dismutase: Implications for metal ion transfer mechanism. Biochemistry 39, 5413–5421.
Himelblau, E., Mira, H., Lin, S. J., et al. (1998) Identification of a functional homolog of the yeast and human homeostasis gene ATX1 from Ardabidopsis. Plant Physiol. 117, 1227–1234.
Lin, X., Kaul, S., Rounsley, S. D., et al. (1999) Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. Nature 402, 761–768.
Bleecker, A. B. and Kende, H. (2000) Ethylene: a gaseous signal molecule in plants. Annu. Rev. Cell Dev. Biol. 16, 1–18.
Hirayama, T. and Alonso, J. M. (2000) Ethylene captures a metal! Metal ions are involved in ethylene perception and signal transduction. Plant Cell Physiol. 41, 548–555.
Woeste, K. E. and Kieber, J. J. (2000) A strong loss-of-function mutation in RANI results in constitutive activation of the ethylene repsonse pathway as well as a rosette-lethal phenotype. Plant Cell 12, 443–455.
Williams, L. E., Pittman, J. K., and Hall, J. L. (2000) Emerging mechanisms for heavy metal transport in plants. Biochim. Biophys. Acta 1465 104–126.
Kanamaru, K., Kashiwagi, S., and Mizuno, T. (1994) A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus sp. PCC7942. Mol. Microbiol. 13, 369–377.
Phung, L. T., Ajlani, G. and Haselkorn, R. (1994) P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products. Proc. Natl. Acad. Sci. USA 91, 9651–9654.
Rutherford, J. C., Cavet, J. S., and Robinson, N. J. (1999) Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase. J. Biol. Chem. 274, 25,827–25, 832.
Thelwell, C., Robinson, N. J., and Turner-Cavet, J. S. (1998) An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter. Proc. Natl. Acad. Sci. USA 95, 10,728–10, 733.
Tottey, S., Rich, P. R., Rondet, S. A. M., et al. (2001) Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC6803. J. Biol. Chem. 276, 19,999–20, 004.
Tottey, S., Rondet, S. A., Borrelly, G. P., Robinson, P. J., Rich, P. R. and Robinson, N. J. (2002) A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition. J. Biol. Chem. 277, 5490–5497.
Mira, H. Martinez-Garcia, F., and Penarrubia, L. (2001) Evidence for the plant-specific intercellular transport of the Arabidopsis copper chaperone CCH. Plant J. 25 521–528.
Himelblau, E. and Amasino, R. M. (2000) Delivering copper within plant cells. Curr. Opin. Plant Biol. 3, 205–210.
Zhou, J. and Goldsbrough, P. B. (1994) Functional homologues of fungal metallothionein genes from Arabidopsis. Plant Cell 6, 875–884.
Dykema, P. E., Sipes, P. R., Marie, A., et al. (1999) A new class of proteins capable of binding transition metals. Plant Mol. Biol. 41, 139–150.
Robinson, N. J., Procter, C. M., Connolly, E. L., et al. (1999) A ferric-chelate reductase for iron uptake from soils. Nature 397, 694–697.
Yi, Y. and Guerinot, M. L. (1996) Genetic evidence that induction of root Fe(III) chelate reductase activity is necessary for iron uptake under iron deficiency. Plant J. 10, 835–844.
Guerinot, M. L., Grotz, N., Hibbard, S., et al. (2001) Molecular characterization of the uptake of iron and other divalent cations in Arabidopsis. J. Exp. Bot. 52 (Suppl.), 62.
Eide, D., Broderius, M., Fett, J., et al. (1996) A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. USA 93, 5624–5628.
Korshunova, Y., Eide, D., Clark, W. G., et al. (1999) The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range. Plant Mol. Biol. 40, 37–44.
Guerinot, M. L. (2000) The ZIP family of metal transporters. Biochim. Biophys. Acta 1465, 190–198.
Curie, C., Alonso, J. M., Jean, M. L., et al. (2000) Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem. J. 347, 749–755.
Thomine, S., Wang, R., Ward, J. M., et al. (2000) Cadmium and iron transport by members of a plant metal transporter family in Arabidopsis with homology to Nramp genes. Proc. Natl. Acad. Sci. USA 97, 4991–4996.
Bagnaresi, P., Thoiron, S., Mansion, M., et al. (1999) Cloning and characterization of a maize cytochrome-b5 reductase with Fe3+-chelate reduction capability. Biochem. J. 338 (Pt. 2), 499–505.
Curie, C., Panaviene, Z., Loulergue, C., et al. (2001) Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake. Nature 409, 346–349.
Bagnaresi, P., Mazars-Marty, D., Pupillo, P., et al. (2000) Tonoplast subcellular localization of maize cytochrome b5 reductases. Plant J. 24, 645–654.
Briat, J.-F. and Lobreaux, S. (1997) Iron transport and storage in plants. Trends Plant Sci. 2, 187–193.
Bell, W. D., Bogorad, L., and Mcllrath, W. J. (1958) Response of the yellow-stripe maize mutant (ysl) to ferrous and ferric iron. Bot. Gaz. 120, 36–39.
Theil, E. C. (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants and microorganisms. Annu. Rev. Biochem. 56, 289–315.
Briat, J. F., Lobreaux, S., Grignon, N., et al. (1999) Regulation of plant ferritin synthesis: how and why. Cell. Mol. Life Sci. 56, 155–166.
Van Wuytswinkel, O., Vansuyt, G., Grignon, N., et al. (1999) Iron homeostasis alteration in transgenic tobacco overexpressing ferritin. Plant J. 17, 93–97.
Briat, J. F. and Lobreaux, S. (1998) Iron storage and ferritin in plants. Metal Ions Biol. Syst. 35, 563–584.
Wei, J. and Theil, E. C. (2000) Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean). J. Biol. Chem. 275, 17,488–17, 493.
Petit, J.-M., Wuytswinkel, O. V., Briat, J.-F., et al. (2001) Characterization of an iron dependent regulatory sequence (IDRS) involved in the transcriptional control of AtFerl and ZmFerl plant ferritin genes by iron. J. Biol. Chem. 276, 5584–5590.
Cohen, C. K., Norvell, W. A., and Kochian, L. V. (1997) Induction of root cell plasma membrane ferric reductase. Plant Physiol. 114, 1061–1069.
Welch, R. M., Norvell, W. A., Schaefer, S. C., et al. (1993) Induction of iron (III) and copper (II) reduction in pea (Pisum sativum L.) roots by Fe and Cu status: does the root-cell plasmalemma Fe(III)-chelate reductase perform a general role in regulating uptake? Planta 190, 555–561.
Harris, E. H. (1989) The Chlamydomonas Sourcebook: A Comprehensive Guide to Biology and Laboratory Use, Academic, San Diego, CA.
Wood, P. M. (1978) Interchangeable copper and iron proteins in algal photosynthesis. Studies on plastocyanin and cytochrome c-552 in Chlarnydomonas. Eur. J. Biochem. 87, 8–19.
Li, H. H. and Merchant, S. (1995) Degradation of plastocyanin in copper-deficient Chlamydomonas reinhardtii. J. Biol. Chen. 270, 23,504–23, 510.
Quinn, J. M. and Merchant, S. (1995) Two copper-responsive elements associated with the Chlamydomonas Cyc6 gene function as targets for transcriptional activators. Plant Cell 7, 623–638.
Hill, K. L. and Merchant, S. (1992) In vivo competition between plastocyanin and a copper-dependent regulator of the Chlamydomonas reinhardtii cytochrome eb gene. Plant Physiol. 100, 319–326.
Li, H. H., Quinn, J., Culler, D., et al. (1996) Molecular genetic analysis of plastocyanin biosynthesis in Chlamydomonas reinhardtii. J. Biol. Chem. 271, 31,283–31, 289.
Merchant, S. and Bogorad, L. (1987) Metal ion regulated gene expression: use of a plastocyanin-less mutant of Chlamydomonas reinhardtii to study the Cu(II)-dependent expression of cytochrome c-552. EMBO J. 6, 2531–2535.
Hill, K. L., Hassett, R., Kosman, D., et al. (1996) Regulated copper uptake in Chlamydomonas reinhardtii in response to copper availability. Plant Physiol. 112, 697–704.
Howe, G. and Merchant, S. (1992) Heavy metal-activated synthesis of peptides in Chlarnydomonas reinhardtii. Plant Physiol. 98, 127–136.
Cobbett, C. S. (2000) Phytochelatin biosynthesis and function in heavy-metal detoxification. Curr. Opin. Plant Biol. 3, 211–216.
Hill, K. L. and Merchant, S. (1995) Coordinate expression of coproporphyrinogen oxidase and cytochrome c6 in the green alga Chlamydomonas reinhardtii in response to changes in copper availability. EMBO J. 14, 857–865.
Moseley, J., Quinn, J., Eriksson, M., et al. (2000) The Crdl gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 19, 2139–2151.
Quinn, J. M., Nakamoto, S. S., and Merchant, S. (1999) Induction of coproporphyrinogen oxidase in Chlamydomonas chloroplasts occurs via transcriptional regulation of Cpxl mediated by copper-response elements and increased translation from a copper-deficiency-specific form of the transcript. J. Biol. Chem. 274, 14,444–14, 454.
Quinn, J. M., Barraco, P., Eriksson, M., et al. (2000) Coordinate copper-and oxygen-responsive Cyc6 and Cpxl expression in Chlamydomonas is mediated by the same element. J. Biol. Chem. 275, 6080–6089.
Quinn, J. M., Eriksson, M., Moseley, J. L., and Merchant, S. (2002) Oxygen deficiency responsive gene expression in Chlamydomonas reinhardtii through a copper-sensing signal transduction pathway. Plant Physiol. 128, 463–471.
Eckhardt, U. and Buckout, T. J. (1998) Iron assimilation in Chlamydomonas reinhardtii involves ferric reduction and is similar to Strategy I higher plants. J. Exp. Bot. 49, 1219–1226.
Lynnes, J. A., Derzaph, T. L. M., and Weger, H. G. (1998) Iron limitation results in induction of ferricyanide reductase and ferric chelate reductase activities in Chlamydomonas reinhardtii. Planta 204, 360–365.
Weger, H. G. (1999) Ferric and cupric reductase activities in the green alga Chlamydomonas reinhardtii: experiments using iron-limited chemostats. Planta 207, 377–384.
Quinn, J. M., LaFontaine, S., Gohre, V., et al. (2000) Copper-dependent and copper-independent iron metabolism in Chlamydomonas reinhardtii. Plant Physiol. S961.
Herbik, A. and Buckhout, T. J. (2001) Is a ferroxidase involved in the high-affinity iron uptake in Chlamydomonas? J. Exp. Bot. 52 (Suppl.), 80.
Hortensteiner, S., Chinner, J., Matile, P., et al. (2000) Chlorophyll breakdown in Chlorella protothecoides: characterization of degreening and cloning of degreening-related genes. Plant Mol. Biol. 42, 439–450.
Osterberg, R. (1974) Origins of metal ions in biology. Nature 249, 382–383.
Nguyen, H. H., Shiemke, A. K., Jacobs, S. J., et al. (1994) The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269, 14,995–15, 005.
Lipscombe, J. D. (1994) Biochemistry of the soluble methane monooxygenase. Annu. Rev. Micobiol. 48, 371–399.
Neilsen, A. K., Gerdes, K., and Murrell, J. C. (1997) Copper-dependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium. Mol. Microbiol. 25, 399–409.
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Fontaine, S.L., Quinn, J., Merchant, S. (2002). Comparative Analysis of Copper and Iron Metabolism in Photosynthetic Eukaryotes vs Yeast and Mammals. 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_30
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