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Volumn 6, Issue 10, 2007, Pages 1841-1852

FEA1, FEA2, and FRE1, encoding two homologous secreted proteins and a candidate ferrireductase, are expressed coordinately with FOX1 and FTR1 in iron-deficient Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

ALGAL PROTEIN; CARBON DIOXIDE; FERRIC CITRATE IRON REDUCTASE; FLAVINE MONONUCLEOTIDE REDUCTASE; IRON; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 35348925016     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00205-07     Document Type: Article
Times cited : (109)

References (92)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud, S., and D. J. Haile. 2000. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275:19906-19912.
    • (2000) J. Biol. Chem , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 2
    • 33846347693 scopus 로고    scopus 로고
    • Manganese deficiency in Chlamydomonas results in loss of photosystem II and MnSOD function, sensitivity to peroxides, and secondary phosphorus and iron deficiency
    • Allen, M. D., J. Kropat, S. Tottey, J. A. Del Campo, and S. S. Merchant. 2007. Manganese deficiency in Chlamydomonas results in loss of photosystem II and MnSOD function, sensitivity to peroxides, and secondary phosphorus and iron deficiency. Plant Physiol. 143:263-277.
    • (2007) Plant Physiol , vol.143 , pp. 263-277
    • Allen, M.D.1    Kropat, J.2    Tottey, S.3    Del Campo, J.A.4    Merchant, S.S.5
  • 3
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith, C., D. Eide, A. Van Ho, P. S. Bernard, L. Li, S. Davis-Kaplan, D. M. Sipe, and J. Kaplan. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76:403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Van Ho, A.3    Bernard, P.S.4    Li, L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 4
    • 0031024679 scopus 로고    scopus 로고
    • An oxidase-permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae
    • Askwith, C., and J. Kaplan. 1997. An oxidase-permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae. J. Biol. Chem. 272:401-405.
    • (1997) J. Biol. Chem , vol.272 , pp. 401-405
    • Askwith, C.1    Kaplan, J.2
  • 6
    • 0027947690 scopus 로고
    • High-affinity siderophore-mediated iron-transport system in the green-alga Scenedesmus incrassatulus
    • Benderliev, K. M., and N. I. Ivanova. 1994. High-affinity siderophore-mediated iron-transport system in the green-alga Scenedesmus incrassatulus. Planta 193:163-166.
    • (1994) Planta , vol.193 , pp. 163-166
    • Benderliev, K.M.1    Ivanova, N.I.2
  • 7
    • 0001690821 scopus 로고
    • Iron uptake by leaf mesophyll-cells - the role of the plasma membrane-bound ferric-chelate reductase
    • Brüggemann, W., K. Maaskantel, and P. R. Moog. 1993. Iron uptake by leaf mesophyll-cells - the role of the plasma membrane-bound ferric-chelate reductase. Planta 190:151-155.
    • (1993) Planta , vol.190 , pp. 151-155
    • Brüggemann, W.1    Maaskantel, K.2    Moog, P.R.3
  • 8
    • 84950042438 scopus 로고
    • Identification of extracellular carbonic anhydrase of Chlamydomonas reinhardtii
    • Coleman, J. R., J. A. Berry, R. K. Togasaki, and A. R. Grossman. 1984. Identification of extracellular carbonic anhydrase of Chlamydomonas reinhardtii. Plant Physiol. 76:472-477.
    • (1984) Plant Physiol , vol.76 , pp. 472-477
    • Coleman, J.R.1    Berry, J.A.2    Togasaki, R.K.3    Grossman, A.R.4
  • 10
    • 0345392723 scopus 로고    scopus 로고
    • Overexpression of the FRO2 ferric chelate reductase confers tolerance to growth on low iron and uncovers posttranscriptional control
    • Connolly, E. L., N. H. Campbell, N. Grotz, C. L. Prichard, and M. L. Guerinot. 2003. Overexpression of the FRO2 ferric chelate reductase confers tolerance to growth on low iron and uncovers posttranscriptional control. Plant Physiol. 133:1102-1110.
    • (2003) Plant Physiol , vol.133 , pp. 1102-1110
    • Connolly, E.L.1    Campbell, N.H.2    Grotz, N.3    Prichard, C.L.4    Guerinot, M.L.5
  • 11
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 12
    • 0035905794 scopus 로고    scopus 로고
    • Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake
    • Curie, C., Z. Panaviene, C. Loulergue, S. L. Dellaporta, J. F. Briat, and E. L. Walker. 2001. Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake. Nature 409:346-349.
    • (2001) Nature , vol.409 , pp. 346-349
    • Curie, C.1    Panaviene, Z.2    Loulergue, C.3    Dellaporta, S.L.4    Briat, J.F.5    Walker, E.L.6
  • 13
    • 0141489216 scopus 로고    scopus 로고
    • Iron transport and signaling in plants
    • Curie, C., and J.-F. Briat. 2003. Iron transport and signaling in plants. Annu. Rev. Plant Biol. 54:183-206.
    • (2003) Annu. Rev. Plant Biol , vol.54 , pp. 183-206
    • Curie, C.1    Briat, J.-F.2
  • 14
    • 0026506018 scopus 로고
    • Ferric reductase of Saccharomyces cerevisiae: Molecular characterization, role in iron uptake, and transcriptional control by iron
    • Dancis, A., D. G. Roman, G. J. Anderson, A. G. Hinnebusch, and R. D. Klausner. 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.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3869-3873
    • Dancis, A.1    Roman, D.G.2    Anderson, G.J.3    Hinnebusch, A.G.4    Klausner, R.D.5
  • 15
    • 0026695501 scopus 로고
    • Expression of the arylsulfatase gene from the β2-tubulin promoter in Chlamydomonas reinhardtii
    • Davies, J. P., D. P. Weeks, and A. R. Grossman. 1992. Expression of the arylsulfatase gene from the β2-tubulin promoter in Chlamydomonas reinhardtii. Nucleic Acids Res. 20:2959-2965.
    • (1992) Nucleic Acids Res , vol.20 , pp. 2959-2965
    • Davies, J.P.1    Weeks, D.P.2    Grossman, A.R.3
  • 16
    • 0028040811 scopus 로고
    • Sequences controlling transcription of the Chlamydomonas reinhardtii β2-tubulin gene after deflagellation and during the cell cycle
    • Davies, J. P., and A. R. Grossman. 1994. Sequences controlling transcription of the Chlamydomonas reinhardtii β2-tubulin gene after deflagellation and during the cell cycle. Mol. Cell. Biol. 14:5165-5174.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 5165-5174
    • Davies, J.P.1    Grossman, A.R.2
  • 17
    • 0024743663 scopus 로고
    • The argininosuccinate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus
    • Debuchy, R., S. Purton, and J. D. Rochaix. 1989. The argininosuccinate lyase gene of Chlamydomonas reinhardtii: an important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus. EMBO J. 8:2803-2809.
    • (1989) EMBO J , vol.8 , pp. 2803-2809
    • Debuchy, R.1    Purton, S.2    Rochaix, J.D.3
  • 18
    • 0023877363 scopus 로고
    • Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii
    • de Hostos, E. L., R. K. Togasaki, and A. Grossman. 1988. Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii. J. Cell Biol. 106:29-37.
    • (1988) J. Cell Biol , vol.106 , pp. 29-37
    • de Hostos, E.L.1    Togasaki, R.K.2    Grossman, A.3
  • 20
    • 0031842182 scopus 로고    scopus 로고
    • Iron assimilation in Chlamydomonas reinhardtii involves ferric reduction and is similar to strategy I higher plants
    • Eckhardt, U., and T. J. Buckhout. 1998. Iron assimilation in Chlamydomonas reinhardtii involves ferric reduction and is similar to strategy I higher plants. J. Exp. Bot. 49:1219-1226.
    • (1998) J. Exp. Bot , vol.49 , pp. 1219-1226
    • Eckhardt, U.1    Buckhout, T.J.2
  • 21
    • 0029891827 scopus 로고    scopus 로고
    • A novel iron-regulated metal transporter from plants identified by functional expression in yeast
    • Eide, D., M. Broderius, J. Fett, and M. L. Guerinot. 1996. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. USA 93:5624-5628.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5624-5628
    • Eide, D.1    Broderius, M.2    Fett, J.3    Guerinot, M.L.4
  • 22
    • 0033925355 scopus 로고    scopus 로고
    • Metal ion transport in eukaryotic microorganisms: Insights from Saccharomyces cerevisiae
    • Eide, D. J. 2000. Metal ion transport in eukaryotic microorganisms: insights from Saccharomyces cerevisiae. Adv. Microb. Physiol. 43:1-38.
    • (2000) Adv. Microb. Physiol , vol.43 , pp. 1-38
    • Eide, D.J.1
  • 23
    • 0033968052 scopus 로고    scopus 로고
    • Discovery of the ceruloplasmin homologue hephaestin: New insight into the copper/iron connection
    • Eisenstein, R. S. 2000. Discovery of the ceruloplasmin homologue hephaestin: new insight into the copper/iron connection. Nutr. Rev. 58:22-26.
    • (2000) Nutr. Rev , vol.58 , pp. 22-26
    • Eisenstein, R.S.1
  • 24
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., H. Nielsen, S. Brunak, and G. von Heijne. 2000. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300:1005-1016.
    • (2000) J. Mol. Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 25
    • 8544234958 scopus 로고    scopus 로고
    • Genetic dissection of nutritional copper signaling in Chlamydomonas distinguishes regulatory and target genes
    • Eriksson, M., J. L. Moseley, S. Tottey, J. A. del Campo, J. M. Quinn, Y. Kim, and S. Merchant. 2004. Genetic dissection of nutritional copper signaling in Chlamydomonas distinguishes regulatory and target genes. Genetics 168:795-807.
    • (2004) Genetics , vol.168 , pp. 795-807
    • Eriksson, M.1    Moseley, J.L.2    Tottey, S.3    del Campo, J.A.4    Quinn, J.M.5    Kim, Y.6    Merchant, S.7
  • 26
    • 0028150505 scopus 로고
    • Regulation of periplasmic carbonic anhydrase expression in Chlamydomonas reinhardtii by acetate and pH
    • Fett, J. P., and J. R. Coleman. 1994. Regulation of periplasmic carbonic anhydrase expression in Chlamydomonas reinhardtii by acetate and pH. Plant Physiol. 106:103-108.
    • (1994) Plant Physiol , vol.106 , pp. 103-108
    • Fett, J.P.1    Coleman, J.R.2
  • 27
    • 0029969718 scopus 로고    scopus 로고
    • Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase
    • Finegold, A. A., K. P. Shatwell, A. W. Segal, R. D. Klausner, and A. Dancis. 1996. Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase. J. Biol. Chem. 271:31021-31024.
    • (1996) J. Biol. Chem , vol.271 , pp. 31021-31024
    • Finegold, A.A.1    Shatwell, K.P.2    Segal, A.W.3    Klausner, R.D.4    Dancis, A.5
  • 28
    • 0032504198 scopus 로고    scopus 로고
    • Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrin
    • Fisher, M., A. Zamir, and U. Pick. 1998. Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrin. J. Biol. Chem. 273:17553-17558.
    • (1998) J. Biol. Chem , vol.273 , pp. 17553-17558
    • Fisher, M.1    Zamir, A.2    Pick, U.3
  • 29
    • 0032477866 scopus 로고    scopus 로고
    • Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming, M. D., M. A. Romano, M. A. Su, L. M. Garrick, M. D. Garrick, and N. C. Andrews. 1998. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. USA 95:1148-1153.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2    Su, M.A.3    Garrick, L.M.4    Garrick, M.D.5    Andrews, N.C.6
  • 30
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes, J. R., and P. Gros. 2001. Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol. 9:397-403.
    • (2001) Trends Microbiol , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 32
    • 0033784328 scopus 로고    scopus 로고
    • Acclimation of Chlamydomonas reinhardtii to its nutrient environment
    • Grossman, A. 2000. Acclimation of Chlamydomonas reinhardtii to its nutrient environment. Protist 151:201-224.
    • (2000) Protist , vol.151 , pp. 201-224
    • Grossman, A.1
  • 33
    • 0028045384 scopus 로고
    • Iron: Nutritious, noxious, and not readily available
    • Guerinot, M. L., and Y. Yi. 1994. Iron: nutritious, noxious, and not readily available. Plant Physiol. 104:815-820.
    • (1994) Plant Physiol , vol.104 , pp. 815-820
    • Guerinot, M.L.1    Yi, Y.2
  • 34
    • 0034192475 scopus 로고    scopus 로고
    • The ZIP family of metal transporters
    • Guerinot, M. L. 2000. The ZIP family of metal transporters. Biochim. Biophys. Acta 1465:190-198.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 190-198
    • Guerinot, M.L.1
  • 37
    • 19044390017 scopus 로고    scopus 로고
    • A comparative inventory of metal transporters in the green alga Chlamydomonas reinhardtii and the red alga Cyanidioschizon merolae
    • Hanikenne, M., U. Krämer, V. Demoulin, and D. Baurain. 2005. A comparative inventory of metal transporters in the green alga Chlamydomonas reinhardtii and the red alga Cyanidioschizon merolae. Plant Physiol. 137:428-446.
    • (2005) Plant Physiol , vol.137 , pp. 428-446
    • Hanikenne, M.1    Krämer, U.2    Demoulin, V.3    Baurain, D.4
  • 39
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris, Z. L., A. P. Durley, T. K. Man, and J. D. Gitlin. 1999. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. USA 96:10812-10817.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 40
    • 0038047698 scopus 로고    scopus 로고
    • Iron uptake, trafficking and homeostasis in plants
    • Hell, R., and U. W. Stephan. 2003. Iron uptake, trafficking and homeostasis in plants. Planta 216:541-551.
    • (2003) Planta , vol.216 , pp. 541-551
    • Hell, R.1    Stephan, U.W.2
  • 41
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M. W., M. U. Muckenthaler, and N. C. Andrews. 2004. Balancing acts: molecular control of mammalian iron metabolism. Cell 117:285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 42
    • 0036914858 scopus 로고    scopus 로고
    • The involvement of a multicopper oxidase in iron uptake by the green algae Chlamydomonas reinhardtii
    • Herbik, A., C. Bölling, and T. J. Buckhout. 2002. The involvement of a multicopper oxidase in iron uptake by the green algae Chlamydomonas reinhardtii. Plant Physiol. 130:2039-2048.
    • (2002) Plant Physiol , vol.130 , pp. 2039-2048
    • Herbik, A.1    Bölling, C.2    Buckhout, T.J.3
  • 43
    • 0036070114 scopus 로고    scopus 로고
    • Is a ferroxidase involved in the high-affinity iron uptake in Chlamydomonas reinhardtii?
    • Herbik, A., S. Haebel, and T. J. Buckhout. 2002. Is a ferroxidase involved in the high-affinity iron uptake in Chlamydomonas reinhardtii? Plant Soil 241:1-9.
    • (2002) Plant Soil , vol.241 , pp. 1-9
    • Herbik, A.1    Haebel, S.2    Buckhout, T.J.3
  • 44
    • 34248157691 scopus 로고    scopus 로고
    • Mining iron: Iron uptake and transport in plants
    • Kim, S. A., and M. L. Guerinot. 2007. Mining iron: iron uptake and transport in plants. FEBS Lett. 581:2273-2280.
    • (2007) FEBS Lett , vol.581 , pp. 2273-2280
    • Kim, S.A.1    Guerinot, M.L.2
  • 45
    • 0037099702 scopus 로고    scopus 로고
    • Ferrichrome induces endosome to plasma membrane cycling of the ferrichrome transporter, Arn1p
    • EMBO J
    • Kim, Y., C. W. Yun, and C. C. Philpott. 2002. Ferrichrome induces endosome to plasma membrane cycling of the ferrichrome transporter, Arn1p, in Saccharomyces cerevisiae. EMBO J 21:3632-3642.
    • (2002) Saccharomyces cerevisiae , vol.21 , pp. 3632-3642
    • Kim, Y.1    Yun, C.W.2    Philpott, C.C.3
  • 46
    • 0037341361 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in fungi
    • Kosman, D. J. 2003. Molecular mechanisms of iron uptake in fungi. Mol. Microbiol. 47:1185-1197.
    • (2003) Mol. Microbiol , vol.47 , pp. 1185-1197
    • Kosman, D.J.1
  • 49
    • 0029946913 scopus 로고    scopus 로고
    • Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain
    • Lesuisse, E., M. Casteras-Simon, and P. Labbe. 1996. Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain. J. Biol. Chem. 271:13578-13583.
    • (1996) J. Biol. Chem , vol.271 , pp. 13578-13583
    • Lesuisse, E.1    Casteras-Simon, M.2    Labbe, P.3
  • 51
    • 0031930231 scopus 로고    scopus 로고
    • Iron limitation results in induction of ferricyanide reductase and ferric chelate reductase activities in Chlamydomonas reinhardtii
    • Lynnes, J. A., T. L. M. Derzaph, and H. G. Weger. 1998. Iron limitation results in induction of ferricyanide reductase and ferric chelate reductase activities in Chlamydomonas reinhardtii. Planta 204:360-365.
    • (1998) Planta , vol.204 , pp. 360-365
    • Lynnes, J.A.1    Derzaph, T.L.M.2    Weger, H.G.3
  • 56
    • 0033152312 scopus 로고    scopus 로고
    • Iron acquisition by plants
    • Mori, S. 1999. Iron acquisition by plants. Curr. Opin. Plant Biol. 2:250-253.
    • (1999) Curr. Opin. Plant Biol , vol.2 , pp. 250-253
    • Mori, S.1
  • 57
    • 34547923150 scopus 로고    scopus 로고
    • Proposed carbon dioxide concentrating mechanism in Chlamydomonas reinhardtii
    • Moroney, J. V., and R. A. Ynalvez. 2007. Proposed carbon dioxide concentrating mechanism in Chlamydomonas reinhardtii. Eukaryot. Cell 6:1251-1259.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1251-1259
    • Moroney, J.V.1    Ynalvez, R.A.2
  • 59
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 60
    • 0036800145 scopus 로고    scopus 로고
    • The copper-iron connection: Hereditary aceruloplasminemia
    • Nittis, T., and J. D. Gitlin. 2002. The copper-iron connection: hereditary aceruloplasminemia. Semin. Hematol. 39:282-289.
    • (2002) Semin. Hematol , vol.39 , pp. 282-289
    • Nittis, T.1    Gitlin, J.D.2
  • 61
    • 34250689932 scopus 로고    scopus 로고
    • Palenik, B., J. Grimwood, A. Aerts, P. Rouzé, A. Salamov, N. Putnam, C. Dupont, R. Jorgensen, E. Derelle, S. Rombauts, K. Zhou, R. Otillar, S. S. Merchant, S. Podell, T. Gaasterland, C. Napoli, K. Gendler, A. Manuell, V. Tai, O. Vallon, G. Piganeau, S. Jancek, M. Heijde, K. Jabbari, C. Bowler, M. Lohr, S. Robbens, G. Werner, I. Dubchak, G. J. Pazour, Q. Ren, I. Paulsen, C. Delwiche, J. Schmutz, D. Rokhsar, Y. Van de Peer, H. Moreau, and I. V. Grigoriev. 2007. The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation. Proc. Natl. Acad. Sci. USA104:7705-7710.
    • Palenik, B., J. Grimwood, A. Aerts, P. Rouzé, A. Salamov, N. Putnam, C. Dupont, R. Jorgensen, E. Derelle, S. Rombauts, K. Zhou, R. Otillar, S. S. Merchant, S. Podell, T. Gaasterland, C. Napoli, K. Gendler, A. Manuell, V. Tai, O. Vallon, G. Piganeau, S. Jancek, M. Heijde, K. Jabbari, C. Bowler, M. Lohr, S. Robbens, G. Werner, I. Dubchak, G. J. Pazour, Q. Ren, I. Paulsen, C. Delwiche, J. Schmutz, D. Rokhsar, Y. Van de Peer, H. Moreau, and I. V. Grigoriev. 2007. The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation. Proc. Natl. Acad. Sci. USA104:7705-7710.
  • 62
    • 0017372980 scopus 로고
    • Extracellular phosphatases of Chlamydomonas reinhardi and their regulation
    • Patni, N. J., S. W. Dhawale, and S. Aaronson. 1977. Extracellular phosphatases of Chlamydomonas reinhardi and their regulation. J. Bacteriol. 130: 205-211.
    • (1977) J. Bacteriol , vol.130 , pp. 205-211
    • Patni, N.J.1    Dhawale, S.W.2    Aaronson, S.3
  • 63
    • 0030953624 scopus 로고    scopus 로고
    • Paulsen, I. T., and M. H. Saier, Jr. 1997. A novel family of ubiquitous heavy metal ion transport proteins. J. Membr. Biol. 156:99-103.
    • Paulsen, I. T., and M. H. Saier, Jr. 1997. A novel family of ubiquitous heavy metal ion transport proteins. J. Membr. Biol. 156:99-103.
  • 64
    • 34247884339 scopus 로고    scopus 로고
    • A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes
    • Paz, Y., A. Katz, and U. Pick. 2007. A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes. J. Biol. Chem. 282:8658-8666.
    • (2007) J. Biol. Chem , vol.282 , pp. 8658-8666
    • Paz, Y.1    Katz, A.2    Pick, U.3
  • 65
    • 1242317649 scopus 로고    scopus 로고
    • The SLC31 (Ctr) copper transporter family
    • Petris, M. J. 2004. The SLC31 (Ctr) copper transporter family. Pflugers Arch. 447:752-755.
    • (2004) Pflugers Arch , vol.447 , pp. 752-755
    • Petris, M.J.1
  • 67
    • 0029294085 scopus 로고
    • Two copper-responsive elements associated with the Chlamydomonas Cyc6 gene function as targets for transcriptional activators
    • Quinn, J. M., and S. Merchant. 1995. Two copper-responsive elements associated with the Chlamydomonas Cyc6 gene function as targets for transcriptional activators. Plant Cell 7:623-638.
    • (1995) Plant Cell , vol.7 , pp. 623-638
    • Quinn, J.M.1    Merchant, S.2
  • 68
    • 0031721060 scopus 로고    scopus 로고
    • Copper-responsive gene expression during adaptation to copper deficiency
    • Quinn, J. M., and S. Merchant. 1998. Copper-responsive gene expression during adaptation to copper deficiency. Methods Enzymol. 297:263-279.
    • (1998) Methods Enzymol , vol.297 , pp. 263-279
    • Quinn, J.M.1    Merchant, S.2
  • 69
    • 0030194559 scopus 로고    scopus 로고
    • Biochemical characterization of the extracellular phosphatases produced by phosphorus-deprived Chlamydomonas reinhardtii
    • Quisel, J. D., D. D. Wykoff, and A. R. Grossman. 1996. Biochemical characterization of the extracellular phosphatases produced by phosphorus-deprived Chlamydomonas reinhardtii. Plant Physiol. 111:839-848.
    • (1996) Plant Physiol , vol.111 , pp. 839-848
    • Quisel, J.D.1    Wykoff, D.D.2    Grossman, A.R.3
  • 70
    • 35348870468 scopus 로고    scopus 로고
    • Proteomic studies under iron stress: Iron deficiency-induced regulation of protein synthesis in the green alga Chlamydomonas reinhardtii
    • L. L. Barton and J. Abadia ed, Springer, New York, NY
    • Reinhardt, I., S. Haebel, A. Herbik, and T. J. Buckhout. 2006. Proteomic studies under iron stress: iron deficiency-induced regulation of protein synthesis in the green alga Chlamydomonas reinhardtii, p. 371-393. In L. L. Barton and J. Abadia (ed.), Iron nutrition in plants and rhizospheric microorganisms. Springer, New York, NY.
    • (2006) Iron nutrition in plants and rhizospheric microorganisms , pp. 371-393
    • Reinhardt, I.1    Haebel, S.2    Herbik, A.3    Buckhout, T.J.4
  • 71
    • 0033602102 scopus 로고    scopus 로고
    • A ferric-chelate reductase for iron uptake from soils
    • Robinson, N. J., C. M. Procter, E. L. Connolly, and M. L. Guerinot. 1999. A ferric-chelate reductase for iron uptake from soils. Nature 397:694-697.
    • (1999) Nature , vol.397 , pp. 694-697
    • Robinson, N.J.1    Procter, C.M.2    Connolly, E.L.3    Guerinot, M.L.4
  • 72
    • 0027269739 scopus 로고
    • + is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase
    • + is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase. Mol. Cell. Biol. 13:4342-4350.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 4342-4350
    • Roman, D.G.1    Dancis, A.2    Anderson, G.J.3    Klausner, R.D.4
  • 73
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault, T. A. 2006. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2:406-414.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 74
    • 0347297336 scopus 로고    scopus 로고
    • Cadmium- and iron-stress-inducible gene expression in the green alga Chlamydomonas reinhardtii: Evidence for H43 protein function in iron assimilation
    • Rubinelli, P., S. Siripornadulsil, F. Gao-Rubinelli, and R. T. Sayre. 2002. Cadmium- and iron-stress-inducible gene expression in the green alga Chlamydomonas reinhardtii: evidence for H43 protein function in iron assimilation. Planta 215:1-13.
    • (2002) Planta , vol.215 , pp. 1-13
    • Rubinelli, P.1    Siripornadulsil, S.2    Gao-Rubinelli, F.3    Sayre, R.T.4
  • 75
    • 1242277806 scopus 로고    scopus 로고
    • Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells
    • Rutherford, J. C., and A. J. Bird. 2004. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell. 3:1-13.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1-13
    • Rutherford, J.C.1    Bird, A.J.2
  • 78
    • 0025374557 scopus 로고
    • A Chlamydomonas gene encodes a G protein beta subunit-like polypeptide
    • Schloss, J. A. 1990. A Chlamydomonas gene encodes a G protein beta subunit-like polypeptide. Mol. Gen. Genet. 221:443-452.
    • (1990) Mol. Gen. Genet , vol.221 , pp. 443-452
    • Schloss, J.A.1
  • 79
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins on silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins on silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 80
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: A class of P-type ATPases that pump heavy metals
    • Solioz, M., and C. Vulpe. 1996. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21:237-241.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 81
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman, R., D. S. Yuan, Y. Yamaguchi-Iwai, R. D. Klausner, and A. Dancis. 1996. A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271:1552-1557.
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2    Yamaguchi-Iwai, Y.3    Klausner, R.D.4    Dancis, A.5
  • 82
    • 0038670716 scopus 로고    scopus 로고
    • Ferritin: At the crossroads of iron and oxygen metabolism
    • Theil, E. C. 2003. Ferritin: at the crossroads of iron and oxygen metabolism. J. Nutr. 133:1549S-1553S.
    • (2003) J. Nutr , vol.133
    • Theil, E.C.1
  • 83
    • 0034712741 scopus 로고    scopus 로고
    • Cadmium and iron transport by members of a plant metal transporter family in Arabidopsis with homology to Nramp genes
    • Thomine, S., R. Wang, J. M. Ward, N. M. Crawford, and J. I. Schroeder. 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.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4991-4996
    • Thomine, S.1    Wang, R.2    Ward, J.M.3    Crawford, N.M.4    Schroeder, J.I.5
  • 84
    • 0035983839 scopus 로고    scopus 로고
    • IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth
    • 84
    • 84. Vert, G., N. Grotz, F. Dédaldéchamp, F. Gaymard, M. L. Guerinot, J. F. Briat, and C. Curie. 2002. IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth. Plant Cell 14:1223-1233.
    • (2002) Plant Cell , vol.14 , pp. 1223-1233
    • Vert, G.1    Grotz, N.2    Dédaldéchamp, F.3    Gaymard, F.4    Guerinot, M.L.5    Briat, J.F.6    Curie, C.7
  • 85
    • 0027974805 scopus 로고
    • Iron inefficiency in maize mutant ys1 (Zea mays L. cv Yellow-Stripe) is caused by a defect in uptake of iron phytosiderophores
    • von Wiren, N., S. Mori, H. Marschner, and V. Romheld. 1994. Iron inefficiency in maize mutant ys1 (Zea mays L. cv Yellow-Stripe) is caused by a defect in uptake of iron phytosiderophores. Plant Physiol. 106:71-77.
    • (1994) Plant Physiol , vol.106 , pp. 71-77
    • von Wiren, N.1    Mori, S.2    Marschner, H.3    Romheld, V.4
  • 86
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe, C. D., Y. M. Kuo, T. L. Murphy, L. Cowley, C. Askwith, N. Libina, J. Gitschier, and G. J. Anderson. 1999. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 21:195-199.
    • (1999) Nat. Genet , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6    Gitschier, J.7    Anderson, G.J.8
  • 87
    • 0036073275 scopus 로고    scopus 로고
    • Ferric chelate reductase activity as affected by the iron-limited growth rate in four species of unicellular green algae (Chlorophyta)
    • Weger, H. G., J. K. Middlemiss, and C. D. Petterson. 2002. Ferric chelate reductase activity as affected by the iron-limited growth rate in four species of unicellular green algae (Chlorophyta). J. Phycol. 38:513-519.
    • (2002) J. Phycol , vol.38 , pp. 513-519
    • Weger, H.G.1    Middlemiss, J.K.2    Petterson, C.D.3
  • 88
    • 33748890474 scopus 로고    scopus 로고
    • Differences between two green algae in biological availability of iron bound to strong chelators
    • Weger, H. G., C. J. Matz, R. S. Magnus, C. N. Walker, M. B. Fink, and R. G. Treble. 2006. Differences between two green algae in biological availability of iron bound to strong chelators. Can. J. Bot. 84:400-411.
    • (2006) Can. J. Bot , vol.84 , pp. 400-411
    • Weger, H.G.1    Matz, C.J.2    Magnus, R.S.3    Walker, C.N.4    Fink, M.B.5    Treble, R.G.6
  • 89
    • 0032068061 scopus 로고    scopus 로고
    • The regulation of photosynthetic electron transport during nutrient deprivation in Chlamydomonas reinhardtii
    • Wykoff, D. D., J. P. Davies, A. Melis, and A. R. Grossman. 1998. The regulation of photosynthetic electron transport during nutrient deprivation in Chlamydomonas reinhardtii. Plant Physiol. 117:129-139.
    • (1998) Plant Physiol , vol.117 , pp. 129-139
    • Wykoff, D.D.1    Davies, J.P.2    Melis, A.3    Grossman, A.R.4
  • 90
    • 0030295014 scopus 로고    scopus 로고
    • Genetic evidence that induction of root Fe(III) chelate reductase activity is necessary for iron uptake under iron deficiency
    • Yi, Y., and M. L. Guerinot. 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.
    • (1996) Plant J , vol.10 , pp. 835-844
    • Yi, Y.1    Guerinot, M.L.2
  • 92
    • 0035971118 scopus 로고    scopus 로고
    • The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae
    • Yun, C. W., M. Bauler, R. E. Moore, P. E. Klebba, and C. C. Philpott. 2001. The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae. J. Biol. Chem. 276:10218-10223.
    • (2001) J. Biol. Chem , vol.276 , pp. 10218-10223
    • Yun, C.W.1    Bauler, M.2    Moore, R.E.3    Klebba, P.E.4    Philpott, C.C.5


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