메뉴 건너뛰기




Volumn 205, Issue 1, 1998, Pages 82-91

Antisense inhibition of cytosolic NADP-dependent isocitrate dehydrogenase in transgenic potato plants

Author keywords

Amino acid; Antisense inhibition; Isocitrate dehydrogenase; Solanum (transgenic); Transgenic plant (potato)

Indexed keywords

2 OXOGLUTARIC ACID; AMINO ACID METABOLISM; CAULIFLOWER MOSAIC VIRUS; ISOCITRATE DEHYDROGENASE; PHOTOSYNTHESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; TRANSGENIC PLANT;

EID: 0031949158     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050299     Document Type: Article
Times cited : (48)

References (48)
  • 1
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon DI (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol 14: 1-15
    • (1949) Plant Physiol , vol.14 , pp. 1-15
    • Arnon, D.I.1
  • 2
    • 0028005597 scopus 로고
    • Characterization of a mitochondrial NADP-dependent isocitrate dehydrogenase in axes of germinating sunflower seeds
    • Attucci S, Rivoal J, Brouquisse R, Carde J-P, Pradet A, Raymond P (1994) Characterization of a mitochondrial NADP-dependent isocitrate dehydrogenase in axes of germinating sunflower seeds. Plant Sci 102: 49-59
    • (1994) Plant Sci , vol.102 , pp. 49-59
    • Attucci, S.1    Rivoal, J.2    Brouquisse, R.3    Carde, J.-P.4    Pradet, A.5    Raymond, P.6
  • 4
    • 0028092438 scopus 로고
    • Differential expression of glutamine synthetase genes during the senescence of Arabidopsis thaliana rosette leaves
    • Bernhard WR, Matile P (1994) Differential expression of glutamine synthetase genes during the senescence of Arabidopsis thaliana rosette leaves. Plant Sci 98: 7-14
    • (1994) Plant Sci , vol.98 , pp. 7-14
    • Bernhard, W.R.1    Matile, P.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification 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
  • 7
    • 0000518813 scopus 로고
    • Do the mitochondria provide the 2-oxoglutarate needed for glutamate synthesis in higher plant chloroplasts?
    • Chen RD, Gadal P (1990) Do the mitochondria provide the 2-oxoglutarate needed for glutamate synthesis in higher plant chloroplasts? Plant Physiol Biochem 28: 141-145
    • (1990) Plant Physiol Biochem , vol.28 , pp. 141-145
    • Chen, R.D.1    Gadal, P.2
  • 8
    • 0024288496 scopus 로고
    • Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum) roots and green leaves
    • Chen RD, Le Maréchal P, Vidai J, Jacquot J-P, Gadal P (1988) Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum) roots and green leaves. Eur J Biochem 175: 565-572
    • (1988) Eur J Biochem , vol.175 , pp. 565-572
    • Chen, R.D.1    Le Maréchal, P.2    Vidai, J.3    Jacquot, J.-P.4    Gadal, P.5
  • 9
    • 0000164002 scopus 로고
    • The regulation of glycolysis and the pentose-phosphate pathway
    • Stumpf PK, Conn EE (eds) Academic Press, New York
    • Copeland L, Turner JE (1987) The regulation of glycolysis and the pentose-phosphate pathway. In Stumpf PK, Conn EE (eds) The Biochemistry of Plants, vol 11. Academic Press, New York, pp 107-125
    • (1987) The Biochemistry of Plants , vol.11 , pp. 107-125
    • Copeland, L.1    Turner, J.E.2
  • 10
    • 0027205318 scopus 로고
    • Lack of aconitase in glyoxysomes and peroxisomes
    • Courtois-Verniquet F, Douce R (1993) Lack of aconitase in glyoxysomes and peroxisomes. Biochem J 294: 103-107
    • (1993) Biochem J , vol.294 , pp. 103-107
    • Courtois-Verniquet, F.1    Douce, R.2
  • 11
    • 0028066301 scopus 로고
    • Immunological analysis of aconitase in pumpkin cotyledons: The absence of aconitase in glyoxysomes
    • De Bellis L, Hayashi M, Biagi PP, Hara-Nishimura I, Alpi A, Nishimura M (1994) Immunological analysis of aconitase in pumpkin cotyledons: the absence of aconitase in glyoxysomes. Physiol Plant 90: 757-762
    • (1994) Physiol Plant , vol.90 , pp. 757-762
    • De Bellis, L.1    Hayashi, M.2    Biagi, P.P.3    Hara-Nishimura, I.4    Alpi, A.5    Nishimura, M.6
  • 14
    • 0040271539 scopus 로고
    • Alpha-ketoglutarate supply for amino acid synthesis in higher plant chloroplasts. Intrachloroplastic localization of NADP-specific isocitrate dehydrogenase
    • Elias BA, Givan CV (1977) Alpha-ketoglutarate supply for amino acid synthesis in higher plant chloroplasts. Intrachloroplastic localization of NADP-specific isocitrate dehydrogenase. Plant Physiol 59: 738-740
    • (1977) Plant Physiol , vol.59 , pp. 738-740
    • Elias, B.A.1    Givan, C.V.2
  • 18
    • 0029111038 scopus 로고
    • +-linked isocitrate dehydrogenase during tomato fruit ripening. Characterization of the predominant cytosolic enzyme from green and ripe pericarp
    • +-linked isocitrate dehydrogenase during tomato fruit ripening. Characterization of the predominant cytosolic enzyme from green and ripe pericarp. Planta 196: 148-154
    • (1995) Planta , vol.196 , pp. 148-154
    • Gallardo, F.1    Gálvez, S.2    Gadal, P.3    Canovas, F.M.4
  • 20
    • 0027972175 scopus 로고
    • Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells
    • Gálvez S, Bismuth E, Sarda C, Gadal P (1994) Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells. Plant Physiol 105: 593-600
    • (1994) Plant Physiol , vol.105 , pp. 593-600
    • Gálvez, S.1    Bismuth, E.2    Sarda, C.3    Gadal, P.4
  • 21
    • 0029137301 scopus 로고
    • On the function of the NADP-dependent isocitrate dehydrogenase isoenzymes in living organisms
    • Gálvez S, Gadal P (1995) On the function of the NADP-dependent isocitrate dehydrogenase isoenzymes in living organisms. Plant Sci 105: 1-14
    • (1995) Plant Sci , vol.105 , pp. 1-14
    • Gálvez, S.1    Gadal, P.2
  • 25
    • 0027132883 scopus 로고
    • On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves
    • Hanning I, Heldt HW (1993) On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves. Plant Physiol 103: 1147-1154
    • (1993) Plant Physiol , vol.103 , pp. 1147-1154
    • Hanning, I.1    Heldt, H.W.2
  • 26
    • 0000746512 scopus 로고
    • Apoplastic expression of yeast-derived invertase in potato: Effects on photosynthesis, leaf solute composition, water relations, and tuber composition
    • Heineke D, Sonnewald U, Büssis D, Günter G, Leidreiter K, Wilke I, Raschke K, Willmitzer L, Heldt HW (1992) Apoplastic expression of yeast-derived invertase in potato: Effects on photosynthesis, leaf solute composition, water relations, and tuber composition. Plant Physiol 100: 301-308
    • (1992) Plant Physiol , vol.100 , pp. 301-308
    • Heineke, D.1    Sonnewald, U.2    Büssis, D.3    Günter, G.4    Leidreiter, K.5    Wilke, I.6    Raschke, K.7    Willmitzer, L.8    Heldt, H.W.9
  • 27
    • 0028039637 scopus 로고
    • Accumulation of hexoses in leaf vacuoles: Studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm
    • Heineke D, Wildenberger K, Sonnewald U, Willmitzer L, Heldt HW (1994) Accumulation of hexoses in leaf vacuoles: Studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm. Planta 194: 29-33
    • (1994) Planta , vol.194 , pp. 29-33
    • Heineke, D.1    Wildenberger, K.2    Sonnewald, U.3    Willmitzer, L.4    Heldt, H.W.5
  • 28
    • 85005725041 scopus 로고
    • +-isocitrate dehydrogenase from the host plant cytosol of lucerne (Medicago sativa.) root nodules
    • +-isocitrate dehydrogenase from the host plant cytosol of lucerne (Medicago sativa.) root nodules. Physiol Plant 67: 538-544
    • (1986) Physiol Plant , vol.67 , pp. 538-544
    • Henson, C.A.1    Duke, S.H.2    Collins, M.3
  • 29
    • 0001012359 scopus 로고
    • Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato (Solanum tuberosum)
    • Höfgen R, Willmitzer L (1990) Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato (Solanum tuberosum). Plant Sci 66: 221-230
    • (1990) Plant Sci , vol.66 , pp. 221-230
    • Höfgen, R.1    Willmitzer, L.2
  • 30
    • 0001051837 scopus 로고
    • Expression of maize phosphoenolpyruvate carboxylase in transgenic tobacco: Effects on biochemistry and physiology
    • Hudspeth RL, Grula JW, Dai Z, Edwards GE, Ku MSB (1992) Expression of maize phosphoenolpyruvate carboxylase in transgenic tobacco: Effects on biochemistry and physiology. Plant Physiol 98: 458-464
    • (1992) Plant Physiol , vol.98 , pp. 458-464
    • Hudspeth, R.L.1    Grula, J.W.2    Dai, Z.3    Edwards, G.E.4    Ku, M.S.B.5
  • 31
    • 0028913386 scopus 로고
    • Inhibition of flower formation by antisense repression of mitochondrial citrate synthase in transgenic plants leads to a specific disintegration of the ovary tissues of flowers
    • Landschütze V, Willmitzer L, Müller-Röber B (1995) Inhibition of flower formation by antisense repression of mitochondrial citrate synthase in transgenic plants leads to a specific disintegration of the ovary tissues of flowers. EMBO J 14: 660-666
    • (1995) EMBO J , vol.14 , pp. 660-666
    • Landschütze, V.1    Willmitzer, L.2    Müller-Röber, B.3
  • 32
    • 0028821004 scopus 로고
    • Leaf-specific antisense inhibition of starch biosynthesis in transgenic potato plants leads to an increase in photoassimilate export from source leaves during the light period
    • Leidreiter K, Heineke D, Heldt HW, Müller-Röber B, Sonnewald U, Willmitzer L (1995a) Leaf-specific antisense inhibition of starch biosynthesis in transgenic potato plants leads to an increase in photoassimilate export from source leaves during the light period. Plant Cell Physiol 36: 615-624
    • (1995) Plant Cell Physiol , vol.36 , pp. 615-624
    • Leidreiter, K.1    Heineke, D.2    Heldt, H.W.3    Müller-Röber, B.4    Sonnewald, U.5    Willmitzer, L.6
  • 34
    • 0002564432 scopus 로고
    • + -linked isocitrate dehydrogenase: Isolation, purification, and characterization of the protein from pea mitochondria
    • + -linked isocitrate dehydrogenase: isolation, purification, and characterization of the protein from pea mitochondria. Plant Physiol 100: 69-75
    • (1992) Plant Physiol , vol.100 , pp. 69-75
    • McIntosh, C.A.1    Oliver, D.J.2
  • 36
    • 0000167609 scopus 로고
    • Slow passive diffusion of orthophosphate between intact isolated chloroplasts and suspending medium
    • Mourioux G, Douce R (1981) Slow passive diffusion of orthophosphate between intact isolated chloroplasts and suspending medium. Plant Physiol 67: 470-473
    • (1981) Plant Physiol , vol.67 , pp. 470-473
    • Mourioux, G.1    Douce, R.2
  • 37
    • 0020174796 scopus 로고
    • Purification of plant mitochondria by isopycnic centrifugation in density gradients of percoll
    • Neuburger M, Journet E-P, Bligny R, Carde JP, Douce R (1982) Purification of plant mitochondria by isopycnic centrifugation in density gradients of percoll. Arch Biochem Biophys 217: 312-323
    • (1982) Arch Biochem Biophys , vol.217 , pp. 312-323
    • Neuburger, M.1    Journet, E.-P.2    Bligny, R.3    Carde, J.P.4    Douce, R.5
  • 38
    • 0029132584 scopus 로고
    • +-isocitrate dehydrogenase in germinating and senescing pumpkin cotyledons
    • +-isocitrate dehydrogenase in germinating and senescing pumpkin cotyledons. Physiol Plant 94: 351-355
    • (1995) Physiol Plant , vol.94 , pp. 351-355
    • Nieri, B.1    De Bellis, L.2    Biagi, P.P.3    Alpi, A.4
  • 39
    • 0008922229 scopus 로고
    • +-isocitrate dehydrogenase in Pisum sativum leaves
    • +-isocitrate dehydrogenase in Pisum sativum leaves. Plant Physiol 68: 70-73
    • (1981) Plant Physiol , vol.68 , pp. 70-73
    • Randall, D.D.1    Givan, C.V.2
  • 40
    • 0001148678 scopus 로고
    • Amino acid and sucrose content determined in the cytosolic, chloroplastic and vacuolar compartments and in the phloem sap of spinach leaves
    • Riens B, Lohaus G, Heineke D, Heldt HW (1991) Amino acid and sucrose content determined in the cytosolic, chloroplastic and vacuolar compartments and in the phloem sap of spinach leaves. Plant Physiol 97: 227-233
    • (1991) Plant Physiol , vol.97 , pp. 227-233
    • Riens, B.1    Lohaus, G.2    Heineke, D.3    Heldt, H.W.4
  • 41
    • 0028112285 scopus 로고
    • Production and diurnal utilization of assimilates in leaves of spinach (Spinacia oleracea L.) and barley (Hordeum vulgare L.)
    • Riens B, Lohaus G, Winter H, Heldt HW (1994) Production and diurnal utilization of assimilates in leaves of spinach (Spinacia oleracea L.) and barley (Hordeum vulgare L.). Planta 192: 497-501
    • (1994) Planta , vol.192 , pp. 497-501
    • Riens, B.1    Lohaus, G.2    Winter, H.3    Heldt, H.W.4
  • 44
    • 0345988389 scopus 로고
    • Studies on NADP-isocitrate dehydrogenase from maturing castor been seeds
    • Satoh Y (1972) Studies on NADP-isocitrate dehydrogenase from maturing castor been seeds. Plant Cell Physiol 13: 493-503
    • (1972) Plant Cell Physiol , vol.13 , pp. 493-503
    • Satoh, Y.1
  • 45
    • 0027025560 scopus 로고
    • Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L.)
    • Shorrosh BS, Dixon RA (1992) Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L.). Plant Mol Biol 20: 801-807
    • (1992) Plant Mol Biol , vol.20 , pp. 801-807
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 48
    • 0016426075 scopus 로고
    • Characterization of different plaque-forming and defective temperate phages in Agrobacterium strains
    • Vervliet G, Holster M, Teuchy H, van Montagu M, Schell J (1975) Characterization of different plaque-forming and defective temperate phages in Agrobacterium strains. J Gen Virol 26: 33-48
    • (1975) J Gen Virol , vol.26 , pp. 33-48
    • Vervliet, G.1    Holster, M.2    Teuchy, H.3    Van Montagu, M.4    Schell, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.