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Volumn 271, Issue 18, 2004, Pages 3657-3664

Evidence for the presence of ferritin in plant mitochondria

Author keywords

Arabidopsis thaliana; Ferritin; Iron; Mitochondria; Pisum sativum

Indexed keywords

FERRITIN;

EID: 4544388003     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04300.x     Document Type: Article
Times cited : (89)

References (41)
  • 3
    • 0001526860 scopus 로고
    • Mechanisms of oxygen activation during plant stress
    • Elstner, E.F. & Osswald, W. (1994) Mechanisms of oxygen activation during plant stress. Proc. Royal Soc. Edinburgh 102B, 131-154.
    • (1994) Proc. Royal Soc. Edinburgh , vol.102 B , pp. 131-154
    • Elstner, E.F.1    Osswald, W.2
  • 4
    • 0030484105 scopus 로고    scopus 로고
    • The role of activated oxygen species in plant disease resistance
    • Mehdy, M.C., Sharma, Y.K., Sathasivan, K. & Bays, N.W. (1996) The role of activated oxygen species in plant disease resistance. Physiol. Plant. 98, 365-374.
    • (1996) Physiol. Plant. , vol.98 , pp. 365-374
    • Mehdy, M.C.1    Sharma, Y.K.2    Sathasivan, K.3    Bays, N.W.4
  • 5
    • 0343145729 scopus 로고    scopus 로고
    • Iron transport and storage in plants
    • Briat, J.-F. & Lobréaux, S. (1997) Iron transport and storage in plants. Trends Plant Sci. 2, 187-192.
    • (1997) Trends Plant Sci. , vol.2 , pp. 187-192
    • Briat, J.-F.1    Lobréaux, S.2
  • 6
    • 0030970357 scopus 로고    scopus 로고
    • Reactive oxygen species and antioxidants: Relationship in green cells
    • Alscher, R.G., Donahue, J.N. & Cramer, C.L. (1997) Reactive oxygen species and antioxidants: relationship in green cells. Physiol. Plant. 100, 224-233.
    • (1997) Physiol. Plant. , vol.100 , pp. 224-233
    • Alscher, R.G.1    Donahue, J.N.2    Cramer, C.L.3
  • 7
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller, I.M. (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 561-591.
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 8
    • 84959964018 scopus 로고
    • Ferreting out the secrets of plant ferritin
    • Seckbach, S. (1982) Ferreting out the secrets of plant ferritin. J. Plant. Nutr. 5, 369-394.
    • (1982) J. Plant. Nutr. , vol.5 , pp. 369-394
    • Seckbach, S.1
  • 9
    • 0034716995 scopus 로고    scopus 로고
    • The role of mild uncoupling and non-coupled respiration in the regulation of hydrogen peroxide generation by plant mitochondria
    • Casolo, V., Braidot, E., Chiandussi, E., Macri, F. & Vianello, A. (2000) The role of mild uncoupling and non-coupled respiration in the regulation of hydrogen peroxide generation by plant mitochondria. FEBS Lett. 474, 53-57.
    • (2000) FEBS Lett. , vol.474 , pp. 53-57
    • Casolo, V.1    Braidot, E.2    Chiandussi, E.3    Macri, F.4    Vianello, A.5
  • 12
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • Theil, E.C. (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Ann. Rev. Biochem. 56, 289-315.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 13
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M. & 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
  • 14
    • 0024977973 scopus 로고
    • Mechansim of the transition from plant ferritin to phytosiderin
    • Laulhere, J.P., Laboure, A.-M. & Briat, J.-F. (1989) Mechansim of the transition from plant ferritin to phytosiderin. J. Biol. Chem. 264, 3629-3635.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3629-3635
    • Laulhere, J.P.1    Laboure, A.-M.2    Briat, J.-F.3
  • 15
    • 0029944620 scopus 로고    scopus 로고
    • Ferritin gene organization: Differences between plants and animals suggest possible kingdom-specific selective constraints
    • Proudhon, D., Wei, J., Briat, J.F. & Theil, E.C. (1996) Ferritin gene organization: differences between plants and animals suggest possible kingdom-specific selective constraints. J. Mol. Evol. 42, 325-336.
    • (1996) J. Mol. Evol. , vol.42 , pp. 325-336
    • Proudhon, D.1    Wei, J.2    Briat, J.F.3    Theil, E.C.4
  • 17
  • 18
    • 0027999314 scopus 로고
    • Lipoxygenase activity associated to isolated soybean plasma membranes
    • Macrì, F., Braidot, E., Petrussa, E. & Vianello, A. (1994) Lipoxygenase activity associated to isolated soybean plasma membranes. Biochim. Biophys. Acta 1215, 109-114.
    • (1994) Biochim. Biophys. Acta , vol.1215 , pp. 109-114
    • Macrì, F.1    Braidot, E.2    Petrussa, E.3    Vianello, A.4
  • 19
    • 0001407023 scopus 로고
    • The Golgi apparatus
    • Hall, J.L. & Moore, A.L., eds, Academic Press Inc., London
    • Green, J.R. (1983) The Golgi apparatus. In Isolation of Membranes and Organelles from Plant Cells (Hall, J.L. & Moore, A.L., eds), pp. 135-152. Academic Press Inc., London.
    • (1983) Isolation of Membranes and Organelles from Plant Cells , pp. 135-152
    • Green, J.R.1
  • 20
    • 0003350681 scopus 로고
    • Endoplasmic reticulum and ribosomes
    • Hall, J.L. & Moore, A.L., eds, Academic Press Inc., London
    • Lord, J.M. (1983) Endoplasmic reticulum and ribosomes. In Isolation of Membranes and Organelles from Plant Cells (Hall, J.L. & Moore, A.L., eds), pp. 119-134. Academic Press Inc., London.
    • (1983) Isolation of Membranes and Organelles from Plant Cells , pp. 119-134
    • Lord, J.M.1
  • 21
    • 0001003017 scopus 로고
    • Enzymes as biochemical reagents; glucose-6-phosphate dehydrogenase
    • Bergmeyer, H.U., ed., Academic Press Inc., London
    • Bergmeyer, H.U., Gawehn, K. & Grassl, M. (1974) Enzymes as biochemical reagents; glucose-6-phosphate dehydrogenase. In Methods of Enzymatic Analysis, Vol. 1 (Bergmeyer, H.U., ed.), pp. 458-459. Academic Press Inc., London.
    • (1974) Methods of Enzymatic Analysis , vol.1 , pp. 458-459
    • Bergmeyer, H.U.1    Gawehn, K.2    Grassl, M.3
  • 22
    • 0024297030 scopus 로고
    • Purification and characterization of ferritins from seed of maize, pea and soya bean: Distribution in various pea organs
    • Laulhere, J.P., Lescure, A.M. & Briat, J.F. (1988) Purification and characterization of ferritins from seed of maize, pea and soya bean: distribution in various pea organs. J. Biol. Chem. 262, 10289-10294.
    • (1988) J. Biol. Chem. , vol.262 , pp. 10289-10294
    • Laulhere, J.P.1    Lescure, A.M.2    Briat, J.F.3
  • 23
    • 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 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0035884102 scopus 로고    scopus 로고
    • Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labelling and MALDI mass spectrometry
    • Shevchenko, A. & Shevchenko, A. (2001) Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labelling and MALDI mass spectrometry. Anal. Biochem. 296, 279-283.
    • (2001) Anal. Biochem. , vol.296 , pp. 279-283
    • Shevchenko, A.1    Shevchenko, A.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0001115403 scopus 로고
    • Membrane-bound NAD(P)H dehydrogenases in higher plant cells
    • Møller, I.M. & Lin, W. (1986) Membrane-bound NAD(P)H dehydrogenases in higher plant cells. Ann. Rev. Plant Physiol. 37, 309-334.
    • (1986) Ann. Rev. Plant Physiol. , vol.37 , pp. 309-334
    • Møller, I.M.1    Lin, W.2
  • 28
    • 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. & 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
  • 29
    • 0027056014 scopus 로고
    • Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin
    • Lobréaux, S., Yewdall, S.J., Briat, J.-F. & Harrison, P.M. (1992) Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin. Biochem. J. 288, 931-939.
    • (1992) Biochem. J. , vol.288 , pp. 931-939
    • Lobréaux, S.1    Yewdall, S.J.2    Briat, J.-F.3    Harrison, P.M.4
  • 30
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: Influence of N-terminus deletions on protein solubility and core formation in vitro
    • Van Wuytswinkel, O., Savino & Briat, J.-F. (1995) Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro. Biochem. J. 305, 253-261.
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • Van Wuytswinkel, O.1    Savino2    Briat, J.-F.3
  • 31
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • Peeters, N. & Small, I. (2001) Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 1541, 54-63.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 32
    • 0030786269 scopus 로고    scopus 로고
    • A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria
    • Chow, K.S., Singh, D.P., Roper, J.M. & Smith, A.G. (1997) A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria. J. Biol. Chem. 272, 27565-27571.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27565-27571
    • Chow, K.S.1    Singh, D.P.2    Roper, J.M.3    Smith, A.G.4
  • 33
    • 0036499460 scopus 로고    scopus 로고
    • Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.)
    • Cornah, J.E., Roper, J.M., Pal Singh, D. & Smith, A.G. (2002) Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.). Biochem. J. 362, 423-432.
    • (2002) Biochem. J. , vol.362 , pp. 423-432
    • Cornah, J.E.1    Roper, J.M.2    Pal Singh, D.3    Smith, A.G.4
  • 34
    • 0035850871 scopus 로고    scopus 로고
    • Arabidopsis thaliana ferrochelatase-I and -II are not imported into Arabidopsis mitochondria
    • Lister, R., Chew, O., Rudhe, C., Lee, M.-N. & Whelan, J. (2001) Arabidopsis thaliana ferrochelatase-I and -II are not imported into Arabidopsis mitochondria. FEBS Lett. 506, 291-295.
    • (2001) FEBS Lett. , vol.506 , pp. 291-295
    • Lister, R.1    Chew, O.2    Rudhe, C.3    Lee, M.-N.4    Whelan, J.5
  • 35
    • 0033046063 scopus 로고    scopus 로고
    • Hydrogen peroxide generation by higher plant mitochondria oxidizing complex I or complex II substrates
    • Braidot, E., Petrussa, E., Vianello, A. & Macrì, F. (1999) Hydrogen peroxide generation by higher plant mitochondria oxidizing complex I or complex II substrates. FEBS Lett. 451, 347-350.
    • (1999) FEBS Lett. , vol.451 , pp. 347-350
    • Braidot, E.1    Petrussa, E.2    Vianello, A.3    Macrì, F.4
  • 36
    • 0035087896 scopus 로고    scopus 로고
    • Molecular mechanisms of plant metal tolerance and homeostasis
    • Clemens, S. (2001) Molecular mechanisms of plant metal tolerance and homeostasis. Planta 212, 475-486.
    • (2001) Planta , vol.212 , pp. 475-486
    • Clemens, S.1
  • 37
    • 0032991401 scopus 로고    scopus 로고
    • Iron homeostasis alteration in transgenic tobacco overexpressing ferritin
    • Van Wuytswinkel, O., Vansuyt, G., Grignon, N., Fourcroy, P. & Briat, J.-F. (1998) Iron homeostasis alteration in transgenic tobacco overexpressing ferritin. Plant J. 17, 93-97.
    • (1998) Plant J. , vol.17 , pp. 93-97
    • Van Wuytswinkel, O.1    Vansuyt, G.2    Grignon, N.3    Fourcroy, P.4    Briat, J.-F.5
  • 39
    • 0034817861 scopus 로고    scopus 로고
    • Plant ferritin accumulates in response to photoinhibition but its ectopic overespression does not protect against photoinhibition
    • Murgia, I., Briat, J.-F., Tarantino, D. & Soave, C. (2001) Plant ferritin accumulates in response to photoinhibition but its ectopic overespression does not protect against photoinhibition. Plant Physiol. Biochem. 39, 797-705.
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 797-1705
    • Murgia, I.1    Briat, J.-F.2    Tarantino, D.3    Soave, C.4
  • 40
    • 0019952734 scopus 로고
    • ATP-dependent and ionophore-induced proton translocation in pea stem microsomal vesicles
    • Vianello, A., Dell'Antone, P. & Macrì, F. (1982) ATP-dependent and ionophore-induced proton translocation in pea stem microsomal vesicles. Biochim. Biophys. Acta 689, 89-96.
    • (1982) Biochim. Biophys. Acta , vol.689 , pp. 89-96
    • Vianello, A.1    Dell'Antone, P.2    Macrì, F.3
  • 41
    • 0029751135 scopus 로고    scopus 로고
    • Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 by chlorophyll a or Zn-pheophytin a
    • Eichacker, L.A., Helfrich, M., Rüdiger, W. & Müller, B. (1996) Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 by chlorophyll a or Zn-pheophytin a. J. Biol. Chem. 271, 32174-32179.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32174-32179
    • Eichacker, L.A.1    Helfrich, M.2    Rüdiger, W.3    Müller, B.4


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