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Volumn 232, Issue 2, 2010, Pages 299-311

Changes in nitrogen assimilation, metabolism, and growth in transgenic rice plants expressing a fungal NADP(H)-dependent glutamate dehydrogenase (gdhA)

Author keywords

Aspergillus niger; NADP(H) dependent glutamate dehydrogenase; Nitrogen metabolism; Rice

Indexed keywords

FUNGAL PROTEIN; GLUTAMATE DEHYDROGENASE (NADP); NITROGEN;

EID: 77955684963     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-010-1172-3     Document Type: Article
Times cited : (60)

References (43)
  • 1
    • 27744532348 scopus 로고    scopus 로고
    • Localization of NAD-isocitrate dehydrogenase and glutamate dehydrogenase in rice roots: Candidates for providing carbon skeletons to NADH-glutamate synthase
    • Abiko T, Obara M, Ushioda A, Hayakawa T, Hodges M, Yamaya T (2005) Localization of NAD-isocitrate dehydrogenase and glutamate dehydrogenase in rice roots: candidates for providing carbon skeletons to NADH-glutamate synthase. Plant Cell Physiol 46: 1724-1734.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1724-1734
    • Abiko, T.1    Obara, M.2    Ushioda, A.3    Hayakawa, T.4    Hodges, M.5    Yamaya, T.6
  • 2
    • 0033877037 scopus 로고    scopus 로고
    • Expression of the bacterial gdhA gene encoding a NADPH glutamate dehydrogenase in tobacco affects plant growth and development
    • Ameziane R, Bernhard K, Lightfoot D (2000) Expression of the bacterial gdhA gene encoding a NADPH glutamate dehydrogenase in tobacco affects plant growth and development. Plant Soil 221: 47-57.
    • (2000) Plant Soil , vol.221 , pp. 47-57
    • Ameziane, R.1    Bernhard, K.2    Lightfoot, D.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M (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.1
  • 4
    • 0034756692 scopus 로고    scopus 로고
    • Transgenic tobacco plants that overexpress alfalfa NADH-glutamate synthase have higher carbon and nitrogen content
    • Chichkova S, Arellano J, Vance CP, Hernández G (2001) Transgenic tobacco plants that overexpress alfalfa NADH-glutamate synthase have higher carbon and nitrogen content. J Exp Bot 52: 2079-2087.
    • (2001) J Exp Bot , vol.52 , pp. 2079-2087
    • Chichkova, S.1    Arellano, J.2    Vance, C.P.3    Hernández, G.4
  • 5
    • 0034943198 scopus 로고    scopus 로고
    • Over-expression of cytosolic glutamine synthetase increases photosynthesis and growth at low nitrogen concentrations
    • Fuentes SI, Allen DJ, Ortiz-Lopez A, Hernández G (2001) Over-expression of cytosolic glutamine synthetase increases photosynthesis and growth at low nitrogen concentrations. J Exp Bot 52: 1071-1081.
    • (2001) J Exp Bot , vol.52 , pp. 1071-1081
    • Fuentes, S.I.1    Allen, D.J.2    Ortiz-Lopez, A.3    Hernández, G.4
  • 6
    • 0028483231 scopus 로고
    • Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA
    • Hiei Y, Ohta S, Komari T, Kumashiro T (1994) Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J 6: 271-282.
    • (1994) Plant J , vol.6 , pp. 271-282
    • Hiei, Y.1    Ohta, S.2    Komari, T.3    Kumashiro, T.4
  • 7
    • 0001583742 scopus 로고
    • Glutamine synthetase in rice
    • Hirel B, Gadal P (1980) Glutamine synthetase in rice. Plant Physiol 66: 619-623.
    • (1980) Plant Physiol , vol.66 , pp. 619-623
    • Hirel, B.1    Gadal, P.2
  • 8
    • 0036010137 scopus 로고    scopus 로고
    • Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation
    • Hodges M (2002) Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation. J Exp Bot 53: 905-916.
    • (2002) J Exp Bot , vol.53 , pp. 905-916
    • Hodges, M.1
  • 9
    • 0002471323 scopus 로고    scopus 로고
    • The enzymes of glutamine, glutamate, asparagine, and aspartate metabolism
    • B. K. Singh (Ed.), New York: Marcel Dekker
    • Ireland RJ, Lea PJ (1999) The enzymes of glutamine, glutamate, asparagine, and aspartate metabolism. In: Singh BK (ed) Plant amino acids: biochemistry and biotechnology. Marcel Dekker, New York, pp 49-109.
    • (1999) Plant Amino Acids: Biochemistry and Biotechnology , pp. 49-109
    • Ireland, R.J.1    Lea, P.J.2
  • 10
    • 1942533430 scopus 로고    scopus 로고
    • Kinetic properties and ammonium-dependent regulation of cytosolic isoenzymes of glutamine synthetase in Arabidopsis
    • Ishiyama K, Inoue E, Watanabe-Takahashi A, Obara M, Yamaya T, Takahashi H (2004a) Kinetic properties and ammonium-dependent regulation of cytosolic isoenzymes of glutamine synthetase in Arabidopsis. J Biol Chem 16(279): 16598-16605.
    • (2004) J Biol Chem , vol.16 , Issue.279 , pp. 16598-16605
    • Ishiyama, K.1    Inoue, E.2    Watanabe-Takahashi, A.3    Obara, M.4    Yamaya, T.5    Takahashi, H.6
  • 11
    • 11144349043 scopus 로고    scopus 로고
    • Biochemical background and compartmentalized functions of cytosolic glutamine synthetase for active ammonium assimilation in rice roots
    • Ishiyama K, Inoue E, Tabuchi M, Yamaya T, Takahashi H (2004b) Biochemical background and compartmentalized functions of cytosolic glutamine synthetase for active ammonium assimilation in rice roots. Plant Cell Physiol 45: 1640-1647.
    • (2004) Plant Cell Physiol , vol.45 , pp. 1640-1647
    • Ishiyama, K.1    Inoue, E.2    Tabuchi, M.3    Yamaya, T.4    Takahashi, H.5
  • 12
    • 0000500127 scopus 로고
    • Vascular bundle-specific localization of cytosolic glutamine synthetase in rice leaves
    • Kamachi K, Yamaya T, Hayakawa T, Mae T, Ojima K (1992) Vascular bundle-specific localization of cytosolic glutamine synthetase in rice leaves. Plant Physiol 99: 1481-1486.
    • (1992) Plant Physiol , vol.99 , pp. 1481-1486
    • Kamachi, K.1    Yamaya, T.2    Hayakawa, T.3    Mae, T.4    Ojima, K.5
  • 13
    • 0015899509 scopus 로고
    • NAD and NADP l-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans
    • Kinghorn JR, Pateman JA (1973) NAD and NADP l-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans. J Gen Microbiol 78: 39-46.
    • (1973) J Gen Microbiol , vol.78 , pp. 39-46
    • Kinghorn, J.R.1    Pateman, J.A.2
  • 14
    • 0037212248 scopus 로고    scopus 로고
    • Transgenic tomato plant carrying a gene for NADP-dependent glutamate dehydrogenase (gdhA) from Aspergillus nidulans
    • Kisaka H, Kida T (2007) Transgenic tomato plant carrying a gene for NADP-dependent glutamate dehydrogenase (gdhA) from Aspergillus nidulans. Plant Sci 164: 35-42.
    • (2007) Plant Sci , vol.164 , pp. 35-42
    • Kisaka, H.1    Kida, T.2
  • 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
  • 18
    • 0016313599 scopus 로고
    • Alternative route for nitrogen assimilation in higher plants
    • Lea PJ, Miflin BJ (1974) Alternative route for nitrogen assimilation in higher plants. Nature 18: 614-616.
    • (1974) Nature , vol.18 , pp. 614-616
    • Lea, P.J.1    Miflin, B.J.2
  • 19
    • 0038560473 scopus 로고
    • Intracellular location and properties of plant l-glutamate dehydrogenases
    • Lea PJ, Thurman DA (1972) Intracellular location and properties of plant l-glutamate dehydrogenases. J Exp Bot 23: 440-449.
    • (1972) J Exp Bot , vol.23 , pp. 440-449
    • Lea, P.J.1    Thurman, D.A.2
  • 20
    • 0032906689 scopus 로고    scopus 로고
    • The Aspergillus nidulansgltA gene encoding glutamate synthase is required for ammonium assimilation in the absence of NADP-glutamate dehydrogenase
    • Macheda ML, Hynes MJ, Davis MA (1999) The Aspergillus nidulansgltA gene encoding glutamate synthase is required for ammonium assimilation in the absence of NADP-glutamate dehydrogenase. Curr Genet 34: 467-471.
    • (1999) Curr Genet , vol.34 , pp. 467-471
    • Macheda, M.L.1    Hynes, M.J.2    Davis, M.A.3
  • 21
    • 77957179743 scopus 로고
    • The remobilization of nitrogen related to leaf growth and senescence in rice plants (Oryza sativa L.)
    • Mae T, Ohira K (1981) The remobilization of nitrogen related to leaf growth and senescence in rice plants (Oryza sativa L.). Plant Cell Physiol 22: 1067-1074.
    • (1981) Plant Cell Physiol , vol.22 , pp. 1067-1074
    • Mae, T.1    Ohira, K.2
  • 23
    • 0030029406 scopus 로고    scopus 로고
    • Arabidopsis mutant analysis and gene regulation define a nonredundant role for glutamate dehydrogenase in nitrogen assimilation
    • Melo-Oliveira R, Oliveira IC, Coruzzi GM (1996) Arabidopsis mutant analysis and gene regulation define a nonredundant role for glutamate dehydrogenase in nitrogen assimilation. Proc Natl Acad Sci 14: 4718-4723.
    • (1996) Proc Natl Acad Sci , vol.14 , pp. 4718-4723
    • Melo-Oliveira, R.1    Oliveira, I.C.2    Coruzzi, G.M.3
  • 24
    • 43149084126 scopus 로고    scopus 로고
    • NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsisthaliana during dark-induced carbon starvation
    • Miyashita Y, Good AG (2008) NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsisthaliana during dark-induced carbon starvation. J Exp Bot 59: 667-680.
    • (2008) J Exp Bot , vol.59 , pp. 667-680
    • Miyashita, Y.1    Good, A.G.2
  • 25
    • 27744532654 scopus 로고    scopus 로고
    • Metabolite fingerprinting in transgenic Nicotiana tabacum altered by the Escherichia coli glutamate dehydrogenase gene
    • Mungur R, Glass AD, Goodenow DB, Lightfoot DA (2005) Metabolite fingerprinting in transgenic Nicotiana tabacum altered by the Escherichia coli glutamate dehydrogenase gene. J Biomed Biotechnol 30: 198-214.
    • (2005) J Biomed Biotechnol , vol.30 , pp. 198-214
    • Mungur, R.1    Glass, A.D.2    Goodenow, D.B.3    Lightfoot, D.A.4
  • 26
    • 19044375664 scopus 로고    scopus 로고
    • Allosteric NADP-glutamate dehydrogenase from aspergilli: Purification, characterization and implications for metabolic regulation at the carbon-nitrogen interface
    • Noor S, Punekar NS (2005) Allosteric NADP-glutamate dehydrogenase from aspergilli: purification, characterization and implications for metabolic regulation at the carbon-nitrogen interface. Microbiology 151: 1409-1419.
    • (2005) Microbiology , vol.151 , pp. 1409-1419
    • Noor, S.1    Punekar, N.S.2
  • 27
    • 0033999597 scopus 로고    scopus 로고
    • High contents of glutamine synthetase does not accompany a high activity of the enzyme in rice (Oryza sativa) leaves of indica cultivars
    • Obara M, Sato T, Yamaya T (2000) High contents of glutamine synthetase does not accompany a high activity of the enzyme in rice (Oryza sativa) leaves of indica cultivars. Physiol Plant 108: 11-18.
    • (2000) Physiol Plant , vol.108 , pp. 11-18
    • Obara, M.1    Sato, T.2    Yamaya, T.3
  • 28
    • 77957742556 scopus 로고    scopus 로고
    • + concentrations in hydroponic conditions. Theor Appl Genet. doi: 10. 1007/s00122-010-1328-3.
  • 29
    • 0035983932 scopus 로고    scopus 로고
    • Overexpression of cytosolic glutamine synthetase. Relation to nitrogen, light, and photorespiration
    • Oliveira IC, Brears T, Knight TJ, Clark A, Coruzzi GM (2002) Overexpression of cytosolic glutamine synthetase. Relation to nitrogen, light, and photorespiration. Plant Physiol 129: 170-180.
    • (2002) Plant Physiol , vol.129 , pp. 170-180
    • Oliveira, I.C.1    Brears, T.2    Knight, T.J.3    Clark, A.4    Coruzzi, G.M.5
  • 30
    • 0036886341 scopus 로고    scopus 로고
    • Cellular and subcellular localisation of glutamine synthetase and glutamate dehydrogenase in grapes gives new insights on the regulation of carbon and nitrogen metabolism
    • Paczek V, Dubois F, Sangwan R, Morot-Gaudry JF, Roubelakis-Angelakis KA, Hirel B (2003) Cellular and subcellular localisation of glutamine synthetase and glutamate dehydrogenase in grapes gives new insights on the regulation of carbon and nitrogen metabolism. Planta 216: 245-254.
    • (2003) Planta , vol.216 , pp. 245-254
    • Paczek, V.1    Dubois, F.2    Sangwan, R.3    Morot-Gaudry, J.F.4    Roubelakis-Angelakis, K.A.5    Hirel, B.6
  • 31
    • 33846342194 scopus 로고    scopus 로고
    • Tobacco isoenzyme 1 of NAD(H)-dependent glutamate dehydrogenase catabolizes glutamate in vivo
    • Purnell MP, Botella JR (2007) Tobacco isoenzyme 1 of NAD(H)-dependent glutamate dehydrogenase catabolizes glutamate in vivo. Plant Physiol 143: 530-539.
    • (2007) Plant Physiol , vol.143 , pp. 530-539
    • Purnell, M.P.1    Botella, J.R.2
  • 32
    • 84896580374 scopus 로고    scopus 로고
    • Modulation of higher-plant NAD(H)-dependent glutamate dehydrogenase activity in transgenic tobacco via alteration of beta subunit levels
    • Purnell MP, Skopelitis DS, Roubelakis-Angelakis KA, Botella JR (2005) Modulation of higher-plant NAD(H)-dependent glutamate dehydrogenase activity in transgenic tobacco via alteration of beta subunit levels. Planta 222: 167-180.
    • (2005) Planta , vol.222 , pp. 167-180
    • Purnell, M.P.1    Skopelitis, D.S.2    Roubelakis-Angelakis, K.A.3    Botella, J.R.4
  • 34
    • 5144227035 scopus 로고    scopus 로고
    • Simultaneous determination of the main metabolites in rice leaves using capillary electrophoresis mass spectrometry and capillary electrophoresis diode array detection
    • Sato S, Soga T, Nishioka T, Tomita M (2004) Simultaneous determination of the main metabolites in rice leaves using capillary electrophoresis mass spectrometry and capillary electrophoresis diode array detection. Plant J 40: 151-163.
    • (2004) Plant J , vol.40 , pp. 151-163
    • Sato, S.1    Soga, T.2    Nishioka, T.3    Tomita, M.4
  • 36
    • 20444439582 scopus 로고    scopus 로고
    • Severe reduction in growth rate and grain filling of rice mutants lacking OsGS1;1, a cytosolic glutamine synthetase1;1
    • Tabuchi M, Sugiyama K, Ishiyama K, Inoue E, Sato T, Takahashi H, Yamaya T (2005) Severe reduction in growth rate and grain filling of rice mutants lacking OsGS1; 1, a cytosolic glutamine synthetase1; 1. Plant J 42: 641-651.
    • (2005) Plant J , vol.42 , pp. 641-651
    • Tabuchi, M.1    Sugiyama, K.2    Ishiyama, K.3    Inoue, E.4    Sato, T.5    Takahashi, H.6    Yamaya, T.7
  • 37
    • 0027402664 scopus 로고
    • Modulation of glutamine synthetase gene expression in tobacco by the introduction of an alfalfa glutamine synthetase gene in sense and antisense orientation: Molecular and biochemical analysis
    • Temple SJ, Knight TJ, Unkefer PJ, Sengupta-Gopalan C (1993) Modulation of glutamine synthetase gene expression in tobacco by the introduction of an alfalfa glutamine synthetase gene in sense and antisense orientation: molecular and biochemical analysis. Mol Gen Genet 236: 315-325.
    • (1993) Mol Gen Genet , vol.236 , pp. 315-325
    • Temple, S.J.1    Knight, T.J.2    Unkefer, P.J.3    Sengupta-Gopalan, C.4
  • 38
    • 16644380661 scopus 로고    scopus 로고
    • Glutamate dehydrogenase of tobacco is mainly induced in the cytosol of phloem companion cells when ammonia is provided either externally or released during photorespiration
    • Tercé-Laforgue T, Dubois F, Ferrario-Méry S, de Crecenzo MA, Sangwan R, Hirel B (2004) Glutamate dehydrogenase of tobacco is mainly induced in the cytosol of phloem companion cells when ammonia is provided either externally or released during photorespiration. Plant Physiol 136: 4308-4317.
    • (2004) Plant Physiol , vol.136 , pp. 4308-4317
    • Tercé-Laforgue, T.1    Dubois, F.2    Ferrario-Méry, S.3    de Crecenzo, M.A.4    Sangwan, R.5    Hirel, B.6
  • 39
    • 77955703773 scopus 로고    scopus 로고
    • Wakayama M, Abiko T, Asano T, Kawakami A, Egami T, Aoki N, Sasaki H, Ohsugi R (2008) Analysis of carboxylic acids and amino acids in plant extracts by using the capillary zone electrophoresis/tandem mass spectroscopy. In: Conference abstract book, 5th international conference on plant metabolomics, 15-18 July 2008, Yokohama, Japan, pp 162-163.
  • 40
    • 0020711185 scopus 로고
    • Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases
    • Wootton JC (1983) Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Biochem J 209: 527-531.
    • (1983) Biochem J , vol.209 , pp. 527-531
    • Wootton, J.C.1
  • 41
    • 84950014120 scopus 로고
    • Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots
    • Yamaya T, Oaks A, Matsumoto H (1984) Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots. Plant Physiol 76: 1009-1013.
    • (1984) Plant Physiol , vol.76 , pp. 1009-1013
    • Yamaya, T.1    Oaks, A.2    Matsumoto, H.3
  • 42
    • 0001616144 scopus 로고
    • Tissue distribution of glutamate synthase and glutamine synthetase in rice leaves
    • Yamaya T, Hayakawa T, Tanasawa K, Kamachi K, Mae T, Ojima K (1992) Tissue distribution of glutamate synthase and glutamine synthetase in rice leaves. Plant Physiol 100: 1427-1432.
    • (1992) Plant Physiol , vol.100 , pp. 1427-1432
    • Yamaya, T.1    Hayakawa, T.2    Tanasawa, K.3    Kamachi, K.4    Mae, T.5    Ojima, K.6
  • 43
    • 0036010138 scopus 로고    scopus 로고
    • Genetic manipulation and quantitative-trait loci mapping for nitrogen recycling in rice
    • Yamaya T, Obara M, Nakajima H, Sasaki S, Hayakawa T, Sato T (2002) Genetic manipulation and quantitative-trait loci mapping for nitrogen recycling in rice. J Exp Bot 53: 917-925.
    • (2002) J Exp Bot , vol.53 , pp. 917-925
    • Yamaya, T.1    Obara, M.2    Nakajima, H.3    Sasaki, S.4    Hayakawa, T.5    Sato, T.6


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