메뉴 건너뛰기




Volumn 207, Issue 2, 1998, Pages 217-223

Excessive iron accumulation in the pea mutants dgl and brz: Subcellular localization of iron and ferritin

Author keywords

Ferritin localization; Iron localization; Iron toxicity; Mineral nutrition; Pisum (Fe toxicity)

Indexed keywords

BIOACCUMULATION; CYTOPLASM; DETERMINATION OF CONTENT; ELECTRON ENERGY LOSS SPECTROSCOPY; ELECTRON SPECTROMETRY; ENDOPLASMIC RETICULUM; FERRITIN; IMMUNOCYTOCHEMISTRY; IRON; MITOCHONDRION; MUTANT; NUTRIENT; OXIDATIVE STRESS; PRECIPITATION; PROTON; STRESS TOLERANCE;

EID: 0032406224     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050475     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0343432440 scopus 로고
    • The production and behaviour of phytoferritin particles during senescence of Phaseolus leaves
    • Barton R (1970) The production and behaviour of phytoferritin particles during senescence of Phaseolus leaves. Planta 94: 73-77
    • (1970) Planta , vol.94 , pp. 73-77
    • Barton, R.1
  • 2
    • 0028870197 scopus 로고
    • Subcellular localization and characterization of excessive iron in the nicotianamine-less tomato mutant chloronerva
    • Becker R, Fritz E, Manteuffel R (1995) Subcellular localization and characterization of excessive iron in the nicotianamine-less tomato mutant chloronerva. Plant Physiol 108: 269-275
    • (1995) Plant Physiol , vol.108 , pp. 269-275
    • Becker, R.1    Fritz, E.2    Manteuffel, R.3
  • 4
    • 0029970827 scopus 로고    scopus 로고
    • Roles of ferritin in plants
    • Briat JF (1996) Roles of ferritin in plants. J Plant Nutr 19: 1331-1342
    • (1996) J Plant Nutr , vol.19 , pp. 1331-1342
    • Briat, J.F.1
  • 6
    • 0007094149 scopus 로고
    • Phytic acid represents 10 to 15% of total phosphorus in alfalfa root and crown
    • Campbell M, Dunn R, Ditterline R, Pickett S, Raboy V (1991) Phytic acid represents 10 to 15% of total phosphorus in alfalfa root and crown. J Plant Nutr 14: 925-937
    • (1991) J Plant Nutr , vol.14 , pp. 925-937
    • Campbell, M.1    Dunn, R.2    Ditterline, R.3    Pickett, S.4    Raboy, V.5
  • 8
    • 0000027474 scopus 로고
    • Metabolism of activated oxygen species
    • Davies DD (ed) Academic Press, London
    • Elstner EF (1987) Metabolism of activated oxygen species. In: Davies DD (ed) The biochemistry of plants: a comprehensive treatise, vol 11. Academic Press, London, pp 253-315
    • (1987) The Biochemistry of Plants: A Comprehensive Treatise , vol.11 , pp. 253-315
    • Elstner, E.F.1
  • 9
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I (1995) Superoxide radical and superoxide dismutases. Annu Rev Biochem 64: 97-112
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 10
    • 0001934687 scopus 로고
    • Improvement of the selection value of gene dgl through recombination
    • Gottschalk W (1987) Improvement of the selection value of gene dgl through recombination. Pisum News Lett 19: 9-11
    • (1987) Pisum News Lett , vol.19 , pp. 9-11
    • Gottschalk, W.1
  • 11
    • 0023158642 scopus 로고
    • Phytochelatins, a class of heavy-metal binding peptides from plants, are functionally analogous to metallothioneins
    • Grill E, Winnacker EL, Zenk MH (1987) Phytochelatins, a class of heavy-metal binding peptides from plants, are functionally analogous to metallothioneins. Proc Natl Acad Sci USA 84: 439-443
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 439-443
    • Grill, E.1    Winnacker, E.L.2    Zenk, M.H.3
  • 12
    • 0030040731 scopus 로고    scopus 로고
    • Shoot-to-root signal transmission regulates root Fe(III) reductase activity in the dgl mutant of pea
    • Grusak MA, Pezeshgi S (1996) Shoot-to-root signal transmission regulates root Fe(III) reductase activity in the dgl mutant of pea. Plant Physiol 110: 329-334
    • (1996) Plant Physiol , vol.110 , pp. 329-334
    • Grusak, M.A.1    Pezeshgi, S.2
  • 13
    • 0001762944 scopus 로고
    • Physiological characterization of a single-gene mutant of Pisum sativum exhibiting excess iron accumulation. I. Root iron reduction and iron uptake
    • Grusak MA, Welch RM, Kochian LV (1990) Physiological characterization of a single-gene mutant of Pisum sativum exhibiting excess iron accumulation. I. Root iron reduction and iron uptake. Plant Physiol 93: 976-981
    • (1990) Plant Physiol , vol.93 , pp. 976-981
    • Grusak, M.A.1    Welch, R.M.2    Kochian, L.V.3
  • 14
    • 0028045384 scopus 로고
    • Iron: Nutritious, noxious, and not readily available
    • Guerinot ML, 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
  • 15
  • 16
    • 0001640621 scopus 로고
    • Pleiotropic effects of brz. A mutation in Pisum sativum (L.) cv. 'Sparkle' conditioning decreased nodulation and increased iron uptake and leaf necrosis
    • Kneen BE, LaRue TA, Welch RM, Weeden NF (1990) Pleiotropic effects of brz. A mutation in Pisum sativum (L.) cv. 'Sparkle' conditioning decreased nodulation and increased iron uptake and leaf necrosis. Plant Physiol 93: 717-722
    • (1990) Plant Physiol , vol.93 , pp. 717-722
    • Kneen, B.E.1    LaRue, T.A.2    Welch, R.M.3    Weeden, N.F.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 19
    • 0025970277 scopus 로고
    • Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development
    • Lobréaux S, Briat JF (1991) Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development. Biochem J 274: 601-606
    • (1991) Biochem J , vol.274 , pp. 601-606
    • Lobréaux, S.1    Briat, J.F.2
  • 20
    • 0028868155 scopus 로고
    • Induction of ferritin synthesis in maize leaves by an iron-mediated oxidative stress
    • Lobréaux S, Thoiron S, Briat JF (1995) Induction of ferritin synthesis in maize leaves by an iron-mediated oxidative stress. Plant J 8: 443-449
    • (1995) Plant J , vol.8 , pp. 443-449
    • Lobréaux, S.1    Thoiron, S.2    Briat, J.F.3
  • 22
    • 0028575839 scopus 로고
    • Three chemically distinct types of oxidants formed by iron-mediated Fenton reactions in the presence of DNA
    • Luo Y, Han Z, Chin SM, Linn S (1994) Three chemically distinct types of oxidants formed by iron-mediated Fenton reactions in the presence of DNA. Proc Natl Acad Sci USA 91: 12438-12442
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12438-12442
    • Luo, Y.1    Han, Z.2    Chin, S.M.3    Linn, S.4
  • 23
    • 3142635757 scopus 로고
    • Phytate: Its chemistry, occurrence, food interactions, nutrial significance, and methods of anlaysis
    • Maga JA (1982) Phytate: its chemistry, occurrence, food interactions, nutrial significance, and methods of anlaysis. J Agric Food Chem 30: 1-9
    • (1982) J Agric Food Chem , vol.30 , pp. 1-9
    • Maga, J.A.1
  • 24
    • 0024118810 scopus 로고
    • Preparation by two-dimensional electrophoresis of proteins for antibody production: Antibody against proteins whose synthesis is reduced by auxin in tobacco mesophyll protoplasts
    • Meyer Y, Grosset J, Chartier Y, Cleyet-Marel JC (1988) Preparation by two-dimensional electrophoresis of proteins for antibody production: antibody against proteins whose synthesis is reduced by auxin in tobacco mesophyll protoplasts. Electrophoresis 9: 704-712
    • (1988) Electrophoresis , vol.9 , pp. 704-712
    • Meyer, Y.1    Grosset, J.2    Chartier, Y.3    Cleyet-Marel, J.C.4
  • 25
    • 0001837569 scopus 로고
    • Structure of protein bodies and elemental composition of phytin from dry germ of maize (Zea mays L.)
    • Mikuš M, Bobák M, Lux A (1992) Structure of protein bodies and elemental composition of phytin from dry germ of maize (Zea mays L.). Bot Acta 105: 26-33
    • (1992) Bot Acta , vol.105 , pp. 26-33
    • Mikuš, M.1    Bobák, M.2    Lux, A.3
  • 26
    • 0001216002 scopus 로고
    • Ethylene production in rice bronzing leaves induced by ferrous iron
    • Peng XX, Yamauchi M (1993) Ethylene production in rice bronzing leaves induced by ferrous iron. Plant Soil 149: 227-234
    • (1993) Plant Soil , vol.149 , pp. 227-234
    • Peng, X.X.1    Yamauchi, M.2
  • 27
    • 36949088391 scopus 로고
    • Physiological disease of rice attributable to iron toxicity
    • Ponnamperuma FN, Bradfield R, Peech M (1955) Physiological disease of rice attributable to iron toxicity. Nature 175: 265
    • (1955) Nature , vol.175 , pp. 265
    • Ponnamperuma, F.N.1    Bradfield, R.2    Peech, M.3
  • 28
    • 0025186372 scopus 로고
    • Evidence for a conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland M, Briat JF, Gagnon J, Lauthére JP, Massenet O, Theil EC (1990) Evidence for a conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J Biol Chem 265: 18339-18344
    • (1990) J Biol Chem , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Lauthére, J.P.4    Massenet, O.5    Theil, E.C.6
  • 30
    • 84959964018 scopus 로고
    • Ferreting out the secrets of plant ferritin - A review
    • Seckbach J (1982) Ferreting out the secrets of plant ferritin - a review. J Plant Nutr 5: 369-394
    • (1982) J Plant Nutr , vol.5 , pp. 369-394
    • Seckbach, J.1
  • 31
    • 0021267177 scopus 로고
    • Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: Application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots
    • Smith DE, Fischer PA (1984) Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots. J Cell Biol 99: 20-28
    • (1984) J Cell Biol , vol.99 , pp. 20-28
    • Smith, D.E.1    Fischer, P.A.2
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 33
    • 0000164358 scopus 로고
    • Zinc tolerance and binding of zinc as zinc phytate in Lemna minor. X-ray microanalytical evidence
    • van Steveninck RFM, van Steveninck ME, Wells, AJ, Fernando DR (1990) Zinc tolerance and binding of zinc as zinc phytate in Lemna minor. X-ray microanalytical evidence. J Plant Physiol 137: 140-146
    • (1990) J Plant Physiol , vol.137 , pp. 140-146
    • Van Steveninck, R.F.M.1    Van Steveninck, M.E.2    Wells, A.J.3    Fernando, D.R.4
  • 34
    • 0001312850 scopus 로고
    • Physiological characteristics of Fe accumulation in the "bronze" mutant of Pisum sativum L., cv. "Sparkle" E 107 (brz brz)
    • Welch RM, La Rue TA (1990) Physiological characteristics of Fe accumulation in the "bronze" mutant of Pisum sativum L., cv. "Sparkle" E 107 (brz brz). Plant Physiol 93: 723-729
    • (1990) Plant Physiol , vol.93 , pp. 723-729
    • Welch, R.M.1    La Rue, T.A.2
  • 35
    • 0028836210 scopus 로고
    • Tissue specific localization of heat-stress proteins during embryo development
    • zur Nieden U, Neumann D, Bucka A, Nover L (1995) Tissue specific localization of heat-stress proteins during embryo development. Planta 196: 530-538
    • (1995) Planta , vol.196 , pp. 530-538
    • Zur Nieden, U.1    Neumann, D.2    Bucka, A.3    Nover, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.