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Volumn 55, Issue 9, 2010, Pages 823-833

Co-suppressed glutamine synthetase2 gene modifies nitrogen metabolism and plant growth in rice

Author keywords

Chloroplastic glutamine synthetase 2; Chlorosis; Co suppression; Metabolic level; Nitrogen; Rice

Indexed keywords

AGROBACTERIUM TUMEFACIENS;

EID: 77952966803     PISSN: 10016538     EISSN: 18619541     Source Type: Journal    
DOI: 10.1007/s11434-010-0075-9     Document Type: Article
Times cited : (29)

References (35)
  • 1
    • 0001903111 scopus 로고    scopus 로고
    • Ammonium Assimilation
    • P. J. Lea and J. F. Morof Gaudry (Eds.), Berlin: Springer-Verlag
    • Hirel B, Lea P J. Ammonium Assimilation. In: Lea P J, Morof Gaudry J F, eds. Plant Nitrogen. Berlin: Springer-Verlag, 2001. 79-99.
    • (2001) Plant Nitrogen , pp. 79-99
    • Hirel, B.1    Lea, P.J.2
  • 3
    • 0002471323 scopus 로고    scopus 로고
    • The enzymes of glutamine, glutamate, asparagines and aspirate metabolism
    • B. K. Singh (Ed.), New York: Marcel Dekker
    • Ireland R J, Lea P J. The enzymes of glutamine, glutamate, asparagines and aspirate metabolism. In: Singh B K, ed. Plant Amino Acids: Biochemistry And Biotechnology. New York: Marcel Dekker, 1999. 49-109.
    • (1999) Plant Amino Acids: Biochemistry And Biotechnology , pp. 49-109
    • Ireland, R.J.1    Lea, P.J.2
  • 4
    • 0001047421 scopus 로고
    • Enzymes of glutamate formation: Glutamate dehydrogenase, glutamine synthetase and glutamate synthase
    • B. J. Miflin (Ed.), New York: Academic Press
    • Stewart G R, Mann A F, Fentem P A. Enzymes of glutamate formation: glutamate dehydrogenase, glutamine synthetase and glutamate synthase. In: Miflin B J, ed. The Biochemistry Of Plants: Amino Acids And Derivatives. New York: Academic Press, 1980. 271-327.
    • (1980) The Biochemistry Of Plants: Amino Acids And Derivatives , pp. 271-327
    • Stewart, G.R.1    Mann, A.F.2    Fentem, P.A.3
  • 5
    • 0004770691 scopus 로고    scopus 로고
    • Glutamine synthetase gene isolation from an alfalfa leaf cDNA library
    • Zozaya-Garza M, Sengupta-Gopalan C. Glutamine synthetase gene isolation from an alfalfa leaf cDNA library. Plant Physiol, 1999, 119: 1568.
    • (1999) Plant Physiol , vol.119 , pp. 1568
    • Zozaya-Garza, M.1    Sengupta-Gopalan, C.2
  • 6
    • 0002089333 scopus 로고
    • The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.: Nucleotide sequence, expression in different organs and uptake into isolated chloroplast
    • Lightfoot D A, Green N K, Cullimore J V. The chloroplast-located glutamine synthetase of Phaseolus vulgaris L.: nucleotide sequence, expression in different organs and uptake into isolated chloroplast. Plant Mol Biol, 1988, 11: 191-202.
    • (1988) Plant Mol Biol , vol.11 , pp. 191-202
    • Lightfoot, D.A.1    Green, N.K.2    Cullimore, J.V.3
  • 7
    • 0024288152 scopus 로고
    • Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo
    • Tingey S V, Tsai F-Y, Edwards J W, et al. Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo. J Biol Chem, 1988, 163: 9651-9657.
    • (1988) J Biol Chem , vol.163 , pp. 9651-9657
    • Tingey, S.V.1    Tsai, F.-Y.2    Edwards, J.W.3
  • 8
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing system of chloroplasts
    • Keegstra K, Cline K. Protein import and routing system of chloroplasts. Plant Cell, 1999, 11: 557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 9
    • 0033030860 scopus 로고    scopus 로고
    • Chloroplast precursor protein translocon
    • May T, Soll J. Chloroplast precursor protein translocon. FEBS Lett, 1999, 452: 53-56.
    • (1999) FEBS Lett , vol.452 , pp. 53-56
    • May, T.1    Soll, J.2
  • 10
    • 0029328626 scopus 로고
    • Use of Arabidopsis mutants and genes to study amide amino acid biosynthesis
    • Lam H-M, Coschigano K, Shultz C, et al. Use of Arabidopsis mutants and genes to study amide amino acid biosynthesis. Plant Cell, 1995, 7: 887-898.
    • (1995) Plant Cell , vol.7 , pp. 887-898
    • Lam, H.-M.1    Coschigano, K.2    Shultz, C.3
  • 11
    • 0029848219 scopus 로고    scopus 로고
    • 3 plants from photooxidation
    • 3 plants from photooxidation. Nature, 1996, 384: 557-560.
    • (1996) Nature , vol.384 , pp. 557-560
    • Kozaki, A.1    Tabeka, G.2
  • 12
    • 0033895244 scopus 로고    scopus 로고
    • Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase
    • Hoshida H, Tanaka Y, Hibino T, et al. Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase. Plant Mol Biol, 2000, 43: 103-111.
    • (2000) Plant Mol Biol , vol.43 , pp. 103-111
    • Hoshida, H.1    Tanaka, Y.2    Hibino, T.3
  • 13
    • 0036800968 scopus 로고    scopus 로고
    • + production in leaves of wild-type and glutamine synthetase 2 antisense oilseed rape
    • + production in leaves of wild-type and glutamine synthetase 2 antisense oilseed rape. Plant Physiol, 2002, 130: 989-998.
    • (2002) Plant Physiol , vol.130 , pp. 989-998
    • Husted, S.1    Mattsson, M.2    Mollers, C.3
  • 14
    • 18844379745 scopus 로고    scopus 로고
    • Construction and characterization of a normalized whole-life-cycle cDNA library of rice
    • Chu Z, Peng K, Zhang L, et al. Construction and characterization of a normalized whole-life-cycle cDNA library of rice. Chinese Sci Bull, 2003, 48: 229-235.
    • (2003) Chinese Sci Bull , vol.48 , pp. 229-235
    • Chu, Z.1    Peng, K.2    Zhang, L.3
  • 17
    • 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, et al. Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J, 1994, 6: 271-282.
    • (1994) Plant J , vol.6 , pp. 271-282
    • Hiei, Y.1    Ohta, S.2    Komari, T.3
  • 19
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon D I. Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol, 1949, 24: 1-15.
    • (1949) Plant Physiol , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 20
    • 0037986651 scopus 로고    scopus 로고
    • Expression of the plastid-located glutamine synthetase of Medicago truncatula. Accumulation of the precursor in root nodules reveals an in vivo control at the level of protein import into plastids
    • Melo P M, Lima L M, Santos I M, et al. Expression of the plastid-located glutamine synthetase of Medicago truncatula. Accumulation of the precursor in root nodules reveals an in vivo control at the level of protein import into plastids. Plant Physiol, 2003, 132: 390-399.
    • (2003) Plant Physiol , vol.132 , pp. 390-399
    • Melo, P.M.1    Lima, L.M.2    Santos, I.M.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding
    • Bradford M M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding. Anal Biochem, 1976, 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0015858498 scopus 로고
    • Glutamine synthetase of pea leaves: Purification, stabilization and pH optima
    • O'Neal D, Joy K W. Glutamine synthetase of pea leaves: Purification, stabilization and pH optima. Arch Biochem Biophys, 1973, 159: 113-122.
    • (1973) Arch Biochem Biophys , vol.159 , pp. 113-122
    • O'Neal, D.1    Joy, K.W.2
  • 23
    • 0018075429 scopus 로고
    • Optimal conditions for the estimation of ammonium by the Berthelot reaction
    • Gordon S A, Fleck A, Bell J. Optimal conditions for the estimation of ammonium by the Berthelot reaction. Ann Clin Biochem, 1978, 15: 270-275.
    • (1978) Ann Clin Biochem , vol.15 , pp. 270-275
    • Gordon, S.A.1    Fleck, A.2    Bell, J.3
  • 24
    • 0033926907 scopus 로고    scopus 로고
    • Enzyme redundancy and the importance of 2-oxoglutarate in higher plant ammonium assimilation
    • Lancien M, Gadal P, Hodges M. Enzyme redundancy and the importance of 2-oxoglutarate in higher plant ammonium assimilation. Plant Physiol, 2000, 123: 817-824.
    • (2000) Plant Physiol , vol.123 , pp. 817-824
    • Lancien, M.1    Gadal, P.2    Hodges, M.3
  • 25
    • 0001234970 scopus 로고
    • Barley mutants lacking chloroplast glutamine synthetase-biochemical and genetic analysis
    • Wallsgrove R M, Turner J C, Hall N P, et al. Barley mutants lacking chloroplast glutamine synthetase-biochemical and genetic analysis. Plant Physiol, 1987, 83: 155-158.
    • (1987) Plant Physiol , vol.83 , pp. 155-158
    • Wallsgrove, R.M.1    Turner, J.C.2    Hall, N.P.3
  • 26
    • 0025303564 scopus 로고
    • Cell specific expression in transgenic plants reveals nonoverlapping roles for chloroplast and cytosolic glutamine synthetase
    • Edwards J W, Walker E L, Coruzzi G M. Cell specific expression in transgenic plants reveals nonoverlapping roles for chloroplast and cytosolic glutamine synthetase. Proc Natl Acad Sci USA, 1990, 87: 3459-3463.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3459-3463
    • Edwards, J.W.1    Walker, E.L.2    Coruzzi, G.M.3
  • 27
    • 32644484885 scopus 로고    scopus 로고
    • Expression analysis of the glutamine synthetase and glutamate synthase gene families in young rice (Oryza sativa) seedlings
    • Zhao X Q, Shi W M. Expression analysis of the glutamine synthetase and glutamate synthase gene families in young rice (Oryza sativa) seedlings. Plant Sci, 2006, 170: 748-754.
    • (2006) Plant Sci , vol.170 , pp. 748-754
    • Zhao, X.Q.1    Shi, W.M.2
  • 28
    • 0000012994 scopus 로고
    • 2 fixation in barley deficient in glutamine synthetase and/or glutamate synthase
    • 2 fixation in barley deficient in glutamine synthetase and/or glutamate synthase. J Exp Bot, 1988, 39: 845-858.
    • (1988) J Exp Bot , vol.39 , pp. 845-858
    • Blackwell, R.D.1    Murray, A.J.S.2    Lea, P.J.3
  • 29
    • 0000784788 scopus 로고
    • Inhibition of photosynthesis in Arabidopsis mutants lacking leaf glutamate synthase activity
    • Somerville S R, Ogren W L. Inhibition of photosynthesis in Arabidopsis mutants lacking leaf glutamate synthase activity. Nature, 1980, 286: 257-259.
    • (1980) Nature , vol.286 , pp. 257-259
    • Somerville, S.R.1    Ogren, W.L.2
  • 30
    • 0032076005 scopus 로고    scopus 로고
    • Arabidopsis gls mutants and distinct Fd-GOGAT genes: Implications for photorespiration and primary nitrogen metabolism
    • Coschigano K T, Melo-Oliveira R, Lim J, et al. Arabidopsis gls mutants and distinct Fd-GOGAT genes: Implications for photorespiration and primary nitrogen metabolism. Plant Cell, 1998, 10: 741-752.
    • (1998) Plant Cell , vol.10 , pp. 741-752
    • Coschigano, K.T.1    Melo-Oliveira, R.2    Lim, J.3
  • 31
    • 0033907082 scopus 로고    scopus 로고
    • Modulation of amino acid metabolism in transformed tobacco plants deficient in Fd-GOGAT
    • Ferrario-Mery S, Suzuki A, Kunz C, et al. Modulation of amino acid metabolism in transformed tobacco plants deficient in Fd-GOGAT. Plant Soil, 2000, 221: 67-79.
    • (2000) Plant Soil , vol.221 , pp. 67-79
    • Ferrario-Mery, S.1    Suzuki, A.2    Kunz, C.3
  • 32
    • 0028035951 scopus 로고
    • Control of photosynthesis in barley leaves with reduced activities of glutamine synthetase and glutamate synthase: Plant characteristics and changes in nitrate, ammonium and amino acids
    • Hausler R E, Blackwell R D, Lea P J, et al. Control of photosynthesis in barley leaves with reduced activities of glutamine synthetase and glutamate synthase: Plant characteristics and changes in nitrate, ammonium and amino acids. Planta, 1994, 194: 406-417.
    • (1994) Planta , vol.194 , pp. 406-417
    • Hausler, R.E.1    Blackwell, R.D.2    Lea, P.J.3
  • 33
    • 0000382080 scopus 로고
    • Inhibition of photosynthesis in barley with decreased levels of chloroplastic glutamine synthetase activity
    • Blackwell R D, Murray A J S, Lea P J. Inhibition of photosynthesis in barley with decreased levels of chloroplastic glutamine synthetase activity. J Exp Bot, 1987, 38: 1799-1809.
    • (1987) J Exp Bot , vol.38 , pp. 1799-1809
    • Blackwell, R.D.1    Murray, A.J.S.2    Lea, P.J.3
  • 34
    • 0141563585 scopus 로고    scopus 로고
    • Nodule-specific modulation of glutamine synthetase in transgenic Medicago truncatula leads to inverse alterations in asparagines synthetase expression
    • Carvalho H G, Lopes-Cardoso I A, Lima L M, et al. Nodule-specific modulation of glutamine synthetase in transgenic Medicago truncatula leads to inverse alterations in asparagines synthetase expression. Plant Physiol, 2003, 133: 243-252.
    • (2003) Plant Physiol , vol.133 , pp. 243-252
    • Carvalho, H.G.1    Lopes-Cardoso, I.A.2    Lima, L.M.3
  • 35
    • 0141786918 scopus 로고    scopus 로고
    • Does lowering glutamine synthetase activity in nodules modifying nitrogen metabolism and growth of Lotus japonicus
    • Harrison J, Pou M A, Sene O, et al. Does lowering glutamine synthetase activity in nodules modifying nitrogen metabolism and growth of Lotus japonicus? Plant Physiol, 2003, 133: 253-262.
    • (2003) Plant Physiol , vol.133 , pp. 253-262
    • Harrison, J.1    Pou, M.A.2    Sene, O.3


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