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Volumn 405, Issue 3, 2007, Pages 523-531

The iron-responsive element (IRE)/iron-regulatory protein 1 (IRP1)-cytosolic aconitase iron-regulatory switch does not operate in plants

Author keywords

Arabidopsis thaliana; Cytosolic aconitase; Ferritin; Iron homoeostasis; Iron regulatory protein 1 (IRP1); Reactive oxygen species (ROS)

Indexed keywords

GENES; IRON COMPOUNDS; MUTAGENESIS; PLANTS (BOTANY); RNA;

EID: 34547480948     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061874     Document Type: Article
Times cited : (64)

References (45)
  • 1
    • 0028045384 scopus 로고
    • Iron: Nutritious, noxious, and not readily available
    • Guerinot, M. L. and Yi, Y. (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
  • 2
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor, G. and Foyer, C. H. (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 249-279
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.H.2
  • 3
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. and Arosio, P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 4
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze, M. W. and Kuhn, L. C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 93, 8175-8182
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 5
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., Rouault, T. A. and Harford, J. B. (1993) Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72, 19-28
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 6
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • Hirling, H., Henderson, B. R. and Kuhn, L. C. (1994) Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase. EMBO J. 13, 453-461
    • (1994) EMBO J , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kuhn, L.C.3
  • 7
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner, P. R., Raineri, I., Epstein, L. B. and White, C. W. (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270, 13399-13405
    • (1995) J. Biol. Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 8
    • 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
  • 9
    • 0028923497 scopus 로고
    • Structure, genomic organization, and expression of the Arabidopsis thaliana aconitase gene. Plant aconitase show significant homology with mammalian iron-responsive element-binding protein
    • Peyret, P., Perez, P. and Alric, M. (1995) Structure, genomic organization, and expression of the Arabidopsis thaliana aconitase gene. Plant aconitase show significant homology with mammalian iron-responsive element-binding protein. J. Biol. Chem. 270, 8131-8137
    • (1995) J. Biol. Chem , vol.270 , pp. 8131-8137
    • Peyret, P.1    Perez, P.2    Alric, M.3
  • 11
    • 0036077504 scopus 로고    scopus 로고
    • Nitric oxide mediates iron-induced ferritin accumulation in Arabidopsis
    • Murgia, I., Delledonne, M. and Soave, C. (2002) Nitric oxide mediates iron-induced ferritin accumulation in Arabidopsis. Plant J. 30, 521-528
    • (2002) Plant J , vol.30 , pp. 521-528
    • Murgia, I.1    Delledonne, M.2    Soave, C.3
  • 12
    • 0035504261 scopus 로고    scopus 로고
    • Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family
    • Petit, J. M., Briat, J. F. and Lobreaux, S. (2001) Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family. Biochem. J. 359, 575-582
    • (2001) Biochem. J , vol.359 , pp. 575-582
    • Petit, J.M.1    Briat, J.F.2    Lobreaux, S.3
  • 13
    • 33747667570 scopus 로고    scopus 로고
    • An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression
    • Arnaud, N., Murgia, I., Boucherez, J., Briat, J. F., Cellier, F. and Gaymard, F. (2006) An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression. J. Biol. Chem. 281, 23579-23588
    • (2006) J. Biol. Chem , vol.281 , pp. 23579-23588
    • Arnaud, N.1    Murgia, I.2    Boucherez, J.3    Briat, J.F.4    Cellier, F.5    Gaymard, F.6
  • 14
    • 0025851581 scopus 로고
    • Rapid inactivation of plant aconitase by hydrogen peroxide
    • Verniquet, F., Gaillard, J., Neuburger, M. and Douce, R. (1991) Rapid inactivation of plant aconitase by hydrogen peroxide. Biochem. J. 276, 643-648
    • (1991) Biochem. J , vol.276 , pp. 643-648
    • Verniquet, F.1    Gaillard, J.2    Neuburger, M.3    Douce, R.4
  • 16
    • 0025230751 scopus 로고
    • The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution
    • Rothenberger, S., Mullner, E. W. and Kuhn, L. C. (1990) The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution. Nucleic Acids Res. 18, 1175-1179
    • (1990) Nucleic Acids Res , vol.18 , pp. 1175-1179
    • Rothenberger, S.1    Mullner, E.W.2    Kuhn, L.C.3
  • 17
    • 0024361535 scopus 로고
    • Requirements for the translational repression of ferritin transcripts in wheat germ extracts by a 90-kDa protein trom rabbit liver
    • Brown, P. H., Daniels-McQueen, S., Walden, W. E., Patino, M. M., Gaffield, L., Bielser, D. and Thach, R. E. (1989) Requirements for the translational repression of ferritin transcripts in wheat germ extracts by a 90-kDa protein trom rabbit liver. J. Biol. Chem. 264, 13383-13386
    • (1989) J. Biol. Chem , vol.264 , pp. 13383-13386
    • Brown, P.H.1    Daniels-McQueen, S.2    Walden, W.E.3    Patino, M.M.4    Gaffield, L.5    Bielser, D.6    Thach, R.E.7
  • 18
    • 0032739921 scopus 로고    scopus 로고
    • Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
    • Tang, Y. and Guest, J. R. (1999) Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145, 3069-3079
    • (1999) Microbiology , vol.145 , pp. 3069-3079
    • Tang, Y.1    Guest, J.R.2
  • 19
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: Post-transcriptional regulation of sodA expression
    • Tang, Y., Quail, M. A., Artymiuk, P. J., Guest, J. R. and Green, J. (2002) Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148, 1027-1037
    • (2002) Microbiology , vol.148 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Guest, J.R.4    Green, J.5
  • 20
    • 33846066027 scopus 로고    scopus 로고
    • Aconitase plays a role in regulating resistance to oxidative stress and cell death in Arabidopsis and Nicotiana benthamiana
    • Moeder, W., Del Pozo, O., Navarre, D. A., Martin, G. B. and Klessig, D. F. (2006) Aconitase plays a role in regulating resistance to oxidative stress and cell death in Arabidopsis and Nicotiana benthamiana. Plant Mol. Biol. 63, 273-287
    • (2006) Plant Mol. Biol , vol.63 , pp. 273-287
    • Moeder, W.1    Del Pozo, O.2    Navarre, D.A.3    Martin, G.B.4    Klessig, D.F.5
  • 22
    • 1642465435 scopus 로고    scopus 로고
    • An Arabidopsis thaliana T-DNA mutagenized population (gabi-kat) for flanking sequence tag-based reverse genetics
    • Rosso, M. G., Li, Y., Strizhov, N., Reiss, B., Dekker, K. and Weisshaar, B. (2003) An Arabidopsis thaliana T-DNA mutagenized population (gabi-kat) for flanking sequence tag-based reverse genetics. Plant Mol. Biol. 53, 247-259
    • (2003) Plant Mol. Biol , vol.53 , pp. 247-259
    • Rosso, M.G.1    Li, Y.2    Strizhov, N.3    Reiss, B.4    Dekker, K.5    Weisshaar, B.6
  • 24
    • 0027472177 scopus 로고
    • Abscisic acid is involved in the iron-induced synthesis of maize ferritin
    • Lobréaux, S., Hardy, T. and Briat, J. F. (1993) Abscisic acid is involved in the iron-induced synthesis of maize ferritin. EMBO J. 12, 651-657
    • (1993) EMBO J , vol.12 , pp. 651-657
    • Lobréaux, S.1    Hardy, T.2    Briat, J.F.3
  • 25
    • 0035983839 scopus 로고    scopus 로고
    • IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth
    • Vert, G., Grotz, N., Dedaldechamp, F., Gaymard, F., Guerinot, M. L., Briat, J. F. and Curie, C. (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    Dedaldechamp, F.3    Gaymard, F.4    Guerinot, M.L.5    Briat, J.F.6    Curie, C.7
  • 26
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W. and Weissmann, C. (1973) A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56, 502-514
    • (1973) Anal. Biochem , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 27
    • 0026887039 scopus 로고
    • Iron induces ferritin synthesis in maize plantlets
    • Lobréaux, S., Massenet, O. and Briat, J. F. (1992) Iron induces ferritin synthesis in maize plantlets. Plant Mol. Biol. 19, 563-575
    • (1992) Plant Mol. Biol , vol.19 , pp. 563-575
    • Lobréaux, S.1    Massenet, O.2    Briat, J.F.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 22544481462 scopus 로고    scopus 로고
    • Siderophore-mediated upregulation of Arabidopsis ferritin expression in response to Erwinia chrysanthemi infection
    • Dellagi, A., Rigault, M., Segond, D., Roux, C., Kraepiel, Y., Cellier, F., Briat, J. F., Gaymard, F. and Expert, D. (2005) Siderophore-mediated upregulation of Arabidopsis ferritin expression in response to Erwinia chrysanthemi infection. Plant J. 43, 262-272
    • (2005) Plant J , vol.43 , pp. 262-272
    • Dellagi, A.1    Rigault, M.2    Segond, D.3    Roux, C.4    Kraepiel, Y.5    Cellier, F.6    Briat, J.F.7    Gaymard, F.8    Expert, D.9
  • 30
    • 0033677426 scopus 로고    scopus 로고
    • Algorithms for extracting structured motifs using a suffix tree with an application to promoter and regulatory site consensus identification
    • Marsan, L. and Sagot, M. F. (2000) Algorithms for extracting structured motifs using a suffix tree with an application to promoter and regulatory site consensus identification. J. Comput. Biol. 7, 345-362
    • (2000) J. Comput. Biol , vol.7 , pp. 345-362
    • Marsan, L.1    Sagot, M.F.2
  • 32
    • 0029891827 scopus 로고    scopus 로고
    • A novel iron-regulated metal transporter from plants identified by functional expression in yeast
    • Eide, D., Broderius, M., Fett, J. and Guerinot, M. L. (1996) A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. U.S.A. 93, 5624-5628
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 5624-5628
    • Eide, D.1    Broderius, M.2    Fett, J.3    Guerinot, M.L.4
  • 33
    • 0029788634 scopus 로고    scopus 로고
    • Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independent of abscisic acid
    • Gaymard, F., Boucherez, J. and Briat, J. F. (1996) Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independent of abscisic acid. Biochem. J. 318, 67-73
    • (1996) Biochem. J , vol.318 , pp. 67-73
    • Gaymard, F.1    Boucherez, J.2    Briat, J.F.3
  • 34
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • Theil, E. C. (1994) Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochem. J. 304, 1-11
    • (1994) Biochem. J , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 35
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood, J. L., Tonti-Filippini, J. S., Gout, A. M., Day, D. A., Whelan, J. and Millar, A. H. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16, 241-256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 36
    • 0015221388 scopus 로고
    • Separation and characterization of aconitate hydratase isoenzymes from pig tissues
    • Eanes, R. Z. and Kun, E. (1971) Separation and characterization of aconitate hydratase isoenzymes from pig tissues. Biochim. Biophys. Acta 227, 204-210
    • (1971) Biochim. Biophys. Acta , vol.227 , pp. 204-210
    • Eanes, R.Z.1    Kun, E.2
  • 37
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy, M. C., Mende-Mueller, L., Blondin, G. A. and Beinert, H. (1992) Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. U.S.A. 89, 11730-11734
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 38
    • 0025336743 scopus 로고
    • Molecular cloning of the yeast mitochondrial aconitase gene (aco1) and evidence of a synergistic regulation of expression by glucose plus glutamate
    • Gangloff, S. P., Marguet, D. and Lauquin, G. J. (1990) Molecular cloning of the yeast mitochondrial aconitase gene (aco1) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol. 10, 3551-3561
    • (1990) Mol. Cell. Biol , vol.10 , pp. 3551-3561
    • Gangloff, S.P.1    Marguet, D.2    Lauquin, G.J.3
  • 39
    • 24344441532 scopus 로고    scopus 로고
    • Yeast aconitase in two locations and two metabolic pathways: Seeing small amounts is believing
    • Regev-Rudzki, N., Karniely, S., Ben-Haim, N. N. and Pines, O. (2005) Yeast aconitase in two locations and two metabolic pathways: seeing small amounts is believing. Mol. Biol. Cell 16, 4163-4171
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4163-4171
    • Regev-Rudzki, N.1    Karniely, S.2    Ben-Haim, N.N.3    Pines, O.4
  • 40
    • 0000174341 scopus 로고
    • Characterization of a cytosolic aconitase in higher plant cells
    • Brouquisse, R., Nishimura, M., Gaillard, J. and Douce, R. (1987) Characterization of a cytosolic aconitase in higher plant cells. Plant Physiol. 84, 1402-1407
    • (1987) Plant Physiol , vol.84 , pp. 1402-1407
    • Brouquisse, R.1    Nishimura, M.2    Gaillard, J.3    Douce, R.4
  • 41
    • 84983384209 scopus 로고
    • Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons
    • De Bellis, L., Tsugeki, R., Alpi, A. and Nishimura, M. (1993) Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons. Physiol. Plant. 88, 485-492
    • (1993) Physiol. Plant , vol.88 , pp. 485-492
    • De Bellis, L.1    Tsugeki, R.2    Alpi, A.3    Nishimura, M.4
  • 42
    • 0344530381 scopus 로고    scopus 로고
    • Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in illuminated leaves of wild species tomato
    • Carrari, F., Nunes-Nesi, A., Gibon, Y., Lytovchenko, A., Loureiro, M. E. and Fernie, A. R. (2003) Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in illuminated leaves of wild species tomato. Plant Physiol. 133, 1322-1335
    • (2003) Plant Physiol , vol.133 , pp. 1322-1335
    • Carrari, F.1    Nunes-Nesi, A.2    Gibon, Y.3    Lytovchenko, A.4    Loureiro, M.E.5    Fernie, A.R.6
  • 43
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jansch, L., Werhahn, W. and Braun, H. P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127, 1694-1710
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.P.5
  • 44
    • 67651108027 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis mitochondrial proteome
    • Millar, A. H., Sweetlove, L. J., Giege, P. and Leaver, C. J. (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol. 127, 1711-1727
    • (2001) Plant Physiol , vol.127 , pp. 1711-1727
    • Millar, A.H.1    Sweetlove, L.J.2    Giege, P.3    Leaver, C.J.4
  • 45
    • 0033520955 scopus 로고    scopus 로고
    • Germination, senescence and pathogenic attack in soybean (Glycine max L.): Identification of the cytosolic aconitase participating in the glyoxylate cycle
    • Cots, J. and Widmer, F. (1999) Germination, senescence and pathogenic attack in soybean (Glycine max L.): identification of the cytosolic aconitase participating in the glyoxylate cycle. Plant Sci. 149, 95-104
    • (1999) Plant Sci , vol.149 , pp. 95-104
    • Cots, J.1    Widmer, F.2


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