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Volumn 8, Issue 9, 2010, Pages 954-965

Nitrogen fixation persists under conditions of salt stress in transgenic Medicago truncatula plants expressing a cyanobacterial flavodoxin

Author keywords

Flavodoxin; Medicago truncatula; Nitrogen fixation; Nodule; Salt stress; Symbiosis

Indexed keywords

FLAVODOXIN; INORGANIC SALT;

EID: 78149484103     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/j.1467-7652.2010.00519.x     Document Type: Article
Times cited : (58)

References (81)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi, H. (1984) Catalase in vitro. Meth. Enzymol. 105, 121-126.
    • (1984) Meth. Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulphide in biological samples
    • Anderson, M.E. (1985) Determination of glutathione and glutathione disulphide in biological samples. Meth. Enzymol. 113, 548-555.
    • (1985) Meth. Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 3
    • 77957081754 scopus 로고
    • Chloroplasts: formation of active oxygen and its scavenging
    • Asada, K. (1984) Chloroplasts: formation of active oxygen and its scavenging. Meth. Enzymol. 105, 422-429.
    • (1984) Meth. Enzymol. , vol.105 , pp. 422-429
    • Asada, K.1
  • 4
    • 57249097070 scopus 로고    scopus 로고
    • Biotechnological approach of improving plant salt tolerance using antioxidants as markers
    • Ashraf, M. (2009) Biotechnological approach of improving plant salt tolerance using antioxidants as markers. Biotechnol. Adv. 27, 84-93.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 84-93
    • Ashraf, M.1
  • 5
    • 57649178867 scopus 로고    scopus 로고
    • +-PPase enhanced resistance to salt and drought stress in transgenic alfalfa (Medicago sativa L.)
    • +-PPase enhanced resistance to salt and drought stress in transgenic alfalfa (Medicago sativa L.). Plant Sci. 176, 232-240.
    • (2009) Plant Sci. , vol.176 , pp. 232-240
    • Bao, A.K.B.1    Wang, S.2    Wu, G.3    Xi, J.4    Zhang, J.5    Wang, C.6
  • 7
    • 43049173527 scopus 로고    scopus 로고
    • Transgenic approaches for abiotic stress tolerance in plants: retrospect and prospects
    • Bhatnagar-Mathur, P., Vadez, V. and Sharma, K.K. (2008) Transgenic approaches for abiotic stress tolerance in plants: retrospect and prospects. Plant Cell Rep. 27, 411-424.
    • (2008) Plant Cell Rep. , vol.27 , pp. 411-424
    • Bhatnagar-Mathur, P.1    Vadez, V.2    Sharma, K.K.3
  • 8
    • 0017184389 scopus 로고
    • Rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976) Rapid and sensitive methods 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
  • 10
    • 0031728716 scopus 로고    scopus 로고
    • Effect of salt stress on antioxidant defence system in soybean root nodules
    • Comba, M.E., Benavides, M.P. and Tomaro, M.L. (1998) Effect of salt stress on antioxidant defence system in soybean root nodules. Aust. J. Plant Physiol. 25, 665-671.
    • (1998) Aust. J. Plant Physiol. , vol.25 , pp. 665-671
    • Comba, M.E.1    Benavides, M.P.2    Tomaro, M.L.3
  • 11
    • 0000746853 scopus 로고
    • Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules
    • Dalton, D.A., Russel, S.A., Hanus, F.J., Pascoe, G.A. and Evans, H.J. (1986) Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules. Proc. Natl Acad. Sci. USA, 83, 3811-3815.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3811-3815
    • Dalton, D.A.1    Russel, S.A.2    Hanus, F.J.3    Pascoe, G.A.4    Evans, H.J.5
  • 12
    • 0026530853 scopus 로고
    • Purification and characterization of monodehydroascorbate reductase from soybean root nodules
    • Dalton, D.A., Langeberg, L. and Robbins, M. (1992) Purification and characterization of monodehydroascorbate reductase from soybean root nodules. Arch. Biochem. Biophys. 292, 281-286.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 281-286
    • Dalton, D.A.1    Langeberg, L.2    Robbins, M.3
  • 13
    • 84989762055 scopus 로고
    • Correlations between the ascorbate-glutathione pathway and effectiveness in legume root-nodules
    • Dalton, D.A., Langeberg, L. and Treneman, N.C. (1993) Correlations between the ascorbate-glutathione pathway and effectiveness in legume root-nodules. Plant Physiol. 87, 365-370.
    • (1993) Plant Physiol. , vol.87 , pp. 365-370
    • Dalton, D.A.1    Langeberg, L.2    Treneman, N.C.3
  • 14
    • 0027137704 scopus 로고
    • Nitrogen fixation and carbon metabolism by nodules and bacteroids of pea plants under sodium chloride
    • Delgado, M.J., Garrido, J.M., Ligero, F. and Lluch, C. (1993) Nitrogen fixation and carbon metabolism by nodules and bacteroids of pea plants under sodium chloride. Physiol. Plant. 89, 824-829.
    • (1993) Physiol. Plant. , vol.89 , pp. 824-829
    • Delgado, M.J.1    Garrido, J.M.2    Ligero, F.3    Lluch, C.4
  • 15
    • 0028164326 scopus 로고
    • Effects of salt stress on growth and nitrogen fixation by pea, faba-bean, common bean and soybean plants
    • Delgado, M.J., Ligero, F. and Lluch, C. (1994) Effects of salt stress on growth and nitrogen fixation by pea, faba-bean, common bean and soybean plants. Soil Biol. Biochem. 26, 371-376.
    • (1994) Soil Biol. Biochem. , vol.26 , pp. 371-376
    • Delgado, M.J.1    Ligero, F.2    Lluch, C.3
  • 17
    • 0033612696 scopus 로고    scopus 로고
    • Characterization of ferredoxin and flavodoxin as markers of iron limitation in marine phytoplankton
    • Erdner, D.L., Price, N.M., Doucette, G.J., Peleato, M.L. and Anderson, D.M. (1999) Characterization of ferredoxin and flavodoxin as markers of iron limitation in marine phytoplankton. Mar. Ecol. Prog. Ser. 184, 43-53.
    • (1999) Mar. Ecol. Prog. Ser. , vol.184 , pp. 43-53
    • Erdner, D.L.1    Price, N.M.2    Doucette, G.J.3    Peleato, M.L.4    Anderson, D.M.5
  • 18
    • 85018193218 scopus 로고
    • Effects of cianazine and linuron on chloroplast development, nodule activity and protein metabolism in Lupinus albus L
    • Fernández-Pascual, M., De Felipe, M.R., Serra, M.T. and Pozuelo, J.M. (1988) Effects of cianazine and linuron on chloroplast development, nodule activity and protein metabolism in Lupinus albus L. J. Plant Physiol. 133, 288-294.
    • (1988) J. Plant Physiol. , vol.133 , pp. 288-294
    • Fernández-Pascual, M.1    De Felipe, M.R.2    Serra, M.T.3    Pozuelo, J.M.4
  • 19
    • 0026005943 scopus 로고
    • Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119
    • Fillat, M.F., Borrias, W.E. and Weisbeek, P.J. (1991) Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119. Biochem. J. 280, 187-191.
    • (1991) Biochem. J. , vol.280 , pp. 187-191
    • Fillat, M.F.1    Borrias, W.E.2    Weisbeek, P.J.3
  • 20
    • 0030913865 scopus 로고    scopus 로고
    • A comparison between different methods for the determination of reduced and oxidized glutathione in mammalian tissues
    • Floreani, M., Petrone, M., Debetto, P. and Palatini, P. (1997) A comparison between different methods for the determination of reduced and oxidized glutathione in mammalian tissues. Free Radic. Res. 26, 449-455.
    • (1997) Free Radic. Res. , vol.26 , pp. 449-455
    • Floreani, M.1    Petrone, M.2    Debetto, P.3    Palatini, P.4
  • 21
    • 0028878440 scopus 로고
    • Antioxidant defenses against activated oxygen in pea nodules subjected to water stress
    • Gogorcena, Y., Iturbe-Ormaetxe, I., Escuredo, P.R. and Becana, M. (1995) Antioxidant defenses against activated oxygen in pea nodules subjected to water stress. Plant Physiol. 108, 753-759.
    • (1995) Plant Physiol. , vol.108 , pp. 753-759
    • Gogorcena, Y.1    Iturbe-Ormaetxe, I.2    Escuredo, P.R.3    Becana, M.4
  • 23
    • 0032819393 scopus 로고    scopus 로고
    • Sucrose synthase in legume nodules is essential for nitrogen fixation
    • Gordon, A.J., Minchin, F.R., James, C.L. and Komina, O. (1999) Sucrose synthase in legume nodules is essential for nitrogen fixation. Plant Physiol. 120, 867-877.
    • (1999) Plant Physiol. , vol.120 , pp. 867-877
    • Gordon, A.J.1    Minchin, F.R.2    James, C.L.3    Komina, O.4
  • 25
    • 0001569083 scopus 로고
    • New Agrobacterium helper plasmids for gene transfer to plants
    • Hood, E.E., Gelvin, S.B., Melchers, L.S. and Hoekema, A. (1993) New Agrobacterium helper plasmids for gene transfer to plants. Transgenic Res. 2, 208-218.
    • (1993) Transgenic Res. , vol.2 , pp. 208-218
    • Hood, E.E.1    Gelvin, S.B.2    Melchers, L.S.3    Hoekema, A.4
  • 26
    • 84989689704 scopus 로고
    • Transient increase of anaerobically-induced enzymes during short-term drought of alfalfa root nodules
    • Irigoyen, J.J., Sánchez-Díaz, M. and Emerich, D.W. (1992) Transient increase of anaerobically-induced enzymes during short-term drought of alfalfa root nodules. J. Plant Physiol. 139, 397-402.
    • (1992) J. Plant Physiol. , vol.139 , pp. 397-402
    • Irigoyen, J.J.1    Sánchez-Díaz, M.2    Emerich, D.W.3
  • 27
    • 23044462129 scopus 로고    scopus 로고
    • Changes in ascorbate peroxidase, catalase, guaiacol peroxidase and superoxide dismutase activities in common bean (Phaseolus vulgaris) nodules under salt stress
    • Jebara, S., Jebara, M., Limam, F. and Aouani, M.E. (2005) Changes in ascorbate peroxidase, catalase, guaiacol peroxidase and superoxide dismutase activities in common bean (Phaseolus vulgaris) nodules under salt stress. J. Plant Physiol. 162, 929-936.
    • (2005) J. Plant Physiol. , vol.162 , pp. 929-936
    • Jebara, S.1    Jebara, M.2    Limam, F.3    Aouani, M.E.4
  • 28
    • 0028871420 scopus 로고
    • Superoxide and the production of oxidative DNA damage
    • Keyer, K., Gort, A.S. and Imlay, J.A. (1995) Superoxide and the production of oxidative DNA damage. J. Bacteriol. 177, 6782-6790.
    • (1995) J. Bacteriol. , vol.177 , pp. 6782-6790
    • Keyer, K.1    Gort, A.S.2    Imlay, J.A.3
  • 29
    • 38649114739 scopus 로고    scopus 로고
    • Overexpression of sweetpotato swpa4 peroxidase results in increased hydrogen peroxide production and enhanced stress tolerance in tobacco
    • Kim, Y.H., Kim, C.Y., Song, W.K., Park, D.S., Kwon, S.Y., Lee, H.S., Bang, J.W. and Kwak, S.S. (2008) Overexpression of sweetpotato swpa4 peroxidase results in increased hydrogen peroxide production and enhanced stress tolerance in tobacco. Planta, 227, 867-881.
    • (2008) Planta , vol.227 , pp. 867-881
    • Kim, Y.H.1    Kim, C.Y.2    Song, W.K.3    Park, D.S.4    Kwon, S.Y.5    Lee, H.S.6    Bang, J.W.7    Kwak, S.S.8
  • 30
    • 0023051604 scopus 로고
    • Characterization of three different flavodoxins from Azotobacter vinelandii
    • Klugkist, J., Voorger, J., Haaker, H. and Veeger, C. (1986) Characterization of three different flavodoxins from Azotobacter vinelandii. Eur. J. Biochem. 155, 33-40.
    • (1986) Eur. J. Biochem. , vol.155 , pp. 33-40
    • Klugkist, J.1    Voorger, J.2    Haaker, H.3    Veeger, C.4
  • 31
    • 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, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0000829607 scopus 로고
    • Effect of nitrate on carbon metabolism and nitrogen fixation in lupin roots nodules Lupinus albus L. cv
    • Lang, P., Martin, R. and Golvano, P. (1993) Effect of nitrate on carbon metabolism and nitrogen fixation in lupin roots nodules Lupinus albus L. cv. Multolupa. Plant Physiol. Biochem. 31, 639-648.
    • (1993) Multolupa. Plant Physiol. Biochem. , vol.31 , pp. 639-648
    • Lang, P.1    Martin, R.2    Golvano, P.3
  • 33
    • 34247557623 scopus 로고    scopus 로고
    • Enhanced tolerance to oxidative stress in transgenic tobacco plants expressing three antioxidant enzymes in chloroplasts
    • Lee, Y.P., Kim, S.H., Bang, J.W., Lee, H.S., Kwak, S.S. and Kwon, S.Y. (2007) Enhanced tolerance to oxidative stress in transgenic tobacco plants expressing three antioxidant enzymes in chloroplasts. Plant Cell Rep. 26, 591-598.
    • (2007) Plant Cell Rep. , vol.26 , pp. 591-598
    • Lee, Y.P.1    Kim, S.H.2    Bang, J.W.3    Lee, H.S.4    Kwak, S.S.5    Kwon, S.Y.6
  • 34
    • 48949120155 scopus 로고    scopus 로고
    • Ascorbate and homoglutathione metabolism in common bean nodules under stress conditions and during natural senescence
    • Loscos, J., Matamoros, M.A. and Becana, M. (2008) Ascorbate and homoglutathione metabolism in common bean nodules under stress conditions and during natural senescence. Plant Physiol. 146, 1282-1292.
    • (2008) Plant Physiol. , vol.146 , pp. 1282-1292
    • Loscos, J.1    Matamoros, M.A.2    Becana, M.3
  • 36
  • 38
    • 0014691242 scopus 로고
    • Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 1155-1163.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1155-1163
    • McCord, J.M.1    Fridovich, I.2
  • 40
    • 0029824775 scopus 로고    scopus 로고
    • Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie, B.D., Bowley, S.R., Harjanto, E. and Leprince, O. (1996) Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase. Plant Physiol. 111, 1177-1181.
    • (1996) Plant Physiol. , vol.111 , pp. 1177-1181
    • McKersie, B.D.1    Bowley, S.R.2    Harjanto, E.3    Leprince, O.4
  • 41
    • 0032793927 scopus 로고    scopus 로고
    • Winter survival of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie, B.D., Bowley, S.R. and Jones, K.S. (1999) Winter survival of transgenic alfalfa overexpressing superoxide dismutase. Plant Physiol. 119, 839-848.
    • (1999) Plant Physiol. , vol.119 , pp. 839-848
    • McKersie, B.D.1    Bowley, S.R.2    Jones, K.S.3
  • 42
    • 0034001533 scopus 로고    scopus 로고
    • Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance
    • McKersie, B.D., Murnaghan, J., Jones, K.S. and Bowley, S.R. (2000) Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance. Plant Physiol. 122, 1427-1437.
    • (2000) Plant Physiol. , vol.122 , pp. 1427-1437
    • McKersie, B.D.1    Murnaghan, J.2    Jones, K.S.3    Bowley, S.R.4
  • 43
    • 0000440210 scopus 로고
    • A major error in the acetylene reduction assay: decreases in nodular nitrogenase activity under assay conditions
    • Minchin, F.R., Witty, J.F., Sheehy, J.E. and Müller, M. (1983) A major error in the acetylene reduction assay: decreases in nodular nitrogenase activity under assay conditions. J. Exp. Bot. 34, 641-649.
    • (1983) J. Exp. Bot. , vol.34 , pp. 641-649
    • Minchin, F.R.1    Witty, J.F.2    Sheehy, J.E.3    Müller, M.4
  • 44
    • 0000769546 scopus 로고
    • Sucrose synthase of soybean nodules
    • Morell, M. and Copeland, L. (1985) Sucrose synthase of soybean nodules. Plant Physiol. 78, 149-154.
    • (1985) Plant Physiol. , vol.78 , pp. 149-154
    • Morell, M.1    Copeland, L.2
  • 45
    • 77957183372 scopus 로고
    • Purification of ascorbate peroxidase in spinach chloroplasts: its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical
    • Nakano, Y. and Asada, K. (1987) Purification of ascorbate peroxidase in spinach chloroplasts: its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical. Plant Cell Physiol. 28, 131-140.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 46
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: keeping active oxygen under control
    • Noctor, N. and Foyer, C.H. (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 249-279.
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.49 , pp. 249-279
    • Noctor, N.1    Foyer, C.H.2
  • 48
    • 41049090626 scopus 로고    scopus 로고
    • Overexpression of cytosolic copper/zinc superoxide dismutase from a mangrove plant Avicennia marina in indica rice var. Pusa Basmati-1 confers abiotic stress tolerance
    • Prashanth, S.R., Sadhasivam, V. and Parida, A. (2008) Overexpression of cytosolic copper/zinc superoxide dismutase from a mangrove plant Avicennia marina in indica rice var. Pusa Basmati-1 confers abiotic stress tolerance. Transgenic Res. 17, 281-291.
    • (2008) Transgenic Res. , vol.17 , pp. 281-291
    • Prashanth, S.R.1    Sadhasivam, V.2    Parida, A.3
  • 50
    • 0026325678 scopus 로고
    • + reductase and flavodoxin from Anabaena PCC7119 and of their electrostatic and covalent complexes
    • + reductase and flavodoxin from Anabaena PCC7119 and of their electrostatic and covalent complexes. Eur. J. Biochem. 202, 1065-1071.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1065-1071
    • Pueyo, J.J.1    Gómez-Moreno, C.2    Mayhew, S.G.3
  • 53
    • 60249088680 scopus 로고    scopus 로고
    • Overexpression of flavodoxin in bacteroids induces changes in antioxidant metabolism leading to delayed senescence and starch accumulation in alfalfa root nodules
    • Redondo, F.J., Coba de la Peña, T., Morcillo, C.N., Lucas, M.M. and Pueyo, J.J. (2009) Overexpression of flavodoxin in bacteroids induces changes in antioxidant metabolism leading to delayed senescence and starch accumulation in alfalfa root nodules. Plant Physiol. 149, 1166-1178.
    • (2009) Plant Physiol. , vol.149 , pp. 1166-1178
    • Redondo, F.J.1    Coba de la Peña, T.2    Morcillo, C.N.3    Lucas, M.M.4    Pueyo, J.J.5
  • 55
    • 0036342304 scopus 로고    scopus 로고
    • Effects of water stress on antioxidant enzymes of leaves and nodules of transgenic alfalfa overexpressing superoxide dismutases
    • Rubio, M.C., González, E.M., Minchin, F.R., Webb, K.J., Arrese-Igor, C., Ramos, J. and Becana, M. (2002) Effects of water stress on antioxidant enzymes of leaves and nodules of transgenic alfalfa overexpressing superoxide dismutases. Physiol. Plant. 115, 531-540.
    • (2002) Physiol. Plant. , vol.115 , pp. 531-540
    • Rubio, M.C.1    González, E.M.2    Minchin, F.R.3    Webb, K.J.4    Arrese-Igor, C.5    Ramos, J.6    Becana, M.7
  • 56
    • 0004136246 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • and, 2nd edn, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. 2nd edn, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 57
    • 0000301329 scopus 로고
    • Consequences of the iron-dependent formation of ferredoxin and flavodoxin on photosynthesis and nitrogen-fixation on Anabaena strains
    • Sandmann, G., Peleato, M.L., Fillat, M.F., Lazaro, M.C. and Gómez-Moreno, C. (1990) Consequences of the iron-dependent formation of ferredoxin and flavodoxin on photosynthesis and nitrogen-fixation on Anabaena strains. Photosynth. Res. 26, 119-125.
    • (1990) Photosynth. Res. , vol.26 , pp. 119-125
    • Sandmann, G.1    Peleato, M.L.2    Fillat, M.F.3    Lazaro, M.C.4    Gómez-Moreno, C.5
  • 60
    • 0028812045 scopus 로고
    • Studies on nodule functioning and hydrogen-peroxide scavenging enzymes under salt stress in chickpea nodules
    • Sheokand, S., Dhandi, S. and Swaraj, K. (1995) Studies on nodule functioning and hydrogen-peroxide scavenging enzymes under salt stress in chickpea nodules. Plant Physiol. Biochem. 33, 561-566.
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 561-566
    • Sheokand, S.1    Dhandi, S.2    Swaraj, K.3
  • 62
    • 1642506307 scopus 로고    scopus 로고
    • Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803
    • Singh, A.K., Li, H. and Sherman, L.A. (2004) Microarray analysis and redox control of gene expression in the cyanobacterium Synechocystis sp. PCC 6803. Physiol. Plant. 120, 27-35.
    • (2004) Physiol. Plant. , vol.120 , pp. 27-35
    • Singh, A.K.1    Li, H.2    Sherman, L.A.3
  • 63
    • 0031875933 scopus 로고    scopus 로고
    • Effects of salt stress on growth, photosynthesis and nitrogen fixation in chickpea (Cicer arietinum L.)
    • Soussi, M., Ocaña, A. and Lluch, C. (1998) Effects of salt stress on growth, photosynthesis and nitrogen fixation in chickpea (Cicer arietinum L.). J. Exp. Bot. 49, 1329-1337.
    • (1998) J. Exp. Bot. , vol.49 , pp. 1329-1337
    • Soussi, M.1    Ocaña, A.2    Lluch, C.3
  • 64
    • 0032868438 scopus 로고    scopus 로고
    • Effect of salt stress on nodulation and nitrogen fixation in legumes
    • Swaraj, K. and Bishnoi, N.R. (1999) Effect of salt stress on nodulation and nitrogen fixation in legumes. Indian J. Exp. Bot. 37, 843-848.
    • (1999) Indian J. Exp. Bot. , vol.37 , pp. 843-848
    • Swaraj, K.1    Bishnoi, N.R.2
  • 65
    • 1642305379 scopus 로고    scopus 로고
    • Nitrogenase and antioxidant enzyme activities in Phaseolus vulgaris nodules formed by Rhizobium tropici isogenic strains with varying tolerance to salt stress
    • Tejera, N.A., Campos, R., Sanjuán, J. and Lluch, C. (2004) Nitrogenase and antioxidant enzyme activities in Phaseolus vulgaris nodules formed by Rhizobium tropici isogenic strains with varying tolerance to salt stress. J. Plant Physiol. 161, 329-338.
    • (2004) J. Plant Physiol. , vol.161 , pp. 329-338
    • Tejera, N.A.1    Campos, R.2    Sanjuán, J.3    Lluch, C.4
  • 66
    • 34547103995 scopus 로고    scopus 로고
    • Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride
    • Tejera-García, N.A., Iribarne, C., Palma, F. and Lluch, C. (2007) Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride. Plant Physiol. Biochem. 45, 535-541.
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 535-541
    • Tejera-García, N.A.1    Iribarne, C.2    Palma, F.3    Lluch, C.4
  • 67
    • 33747488135 scopus 로고    scopus 로고
    • Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance
    • Tognetti, V.B., Palatnik, J.F., Fillat, M.F., Melzer, M., Hajirezael, M.-R., Valle, E.M. and Carrillo, N. (2006) Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance. Plant Cell, 18, 2035-2050.
    • (2006) Plant Cell , vol.18 , pp. 2035-2050
    • Tognetti, V.B.1    Palatnik, J.F.2    Fillat, M.F.3    Melzer, M.4    Hajirezael, M.5    Valle, E.M.6    Carrillo, N.7
  • 68
    • 34250163890 scopus 로고    scopus 로고
    • Detoxification of 2,4-dinitrotoluene by transgenic plants expressing a bacterial flavodoxin
    • Tognetti, V.B., Monti, M.R., Valle, E.M., Carrillo, N. and Smania, A. (2007a) Detoxification of 2, 4-dinitrotoluene by transgenic plants expressing a bacterial flavodoxin. Environ. Sci. Technol. 41, 4071-4076.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 4071-4076
    • Tognetti, V.B.1    Monti, M.R.2    Valle, E.M.3    Carrillo, N.4    Smania, A.5
  • 69
    • 34547437241 scopus 로고    scopus 로고
    • Enhanced plant tolerance to iron starvation by functional substitution of chloroplast ferredoxin with a bacterial flavodoxin
    • Tognetti, V.B., Zurbriggen, M.D., Morandi, E.N., Fillat, M.F., Valle, E.M., Hajirezael, M.-R. and Carrillo, N. (2007b) Enhanced plant tolerance to iron starvation by functional substitution of chloroplast ferredoxin with a bacterial flavodoxin. Proc. Natl Acad. Sci. USA, 104, 11495-11500.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11495-11500
    • Tognetti, V.B.1    Zurbriggen, M.D.2    Morandi, E.N.3    Fillat, M.F.4    Valle, E.M.5    Hajirezael, M.6    Carrillo, N.7
  • 71
    • 0031944203 scopus 로고    scopus 로고
    • Rapid and efficient transformation of diploid Medicago truncatula and Medicago sativa ssp. falcata lines improved in somatic embryogenesis
    • Trinh, T.H., Ratet, P., Kondorosi, E., Durand, P., Kamaté, K., Bauer, P. and Kondorosi, A. (1998) Rapid and efficient transformation of diploid Medicago truncatula and Medicago sativa ssp. falcata lines improved in somatic embryogenesis. Plant Cell Rep. 17, 345-355.
    • (1998) Plant Cell Rep. , vol.17 , pp. 345-355
    • Trinh, T.H.1    Ratet, P.2    Kondorosi, E.3    Durand, P.4    Kamaté, K.5    Bauer, P.6    Kondorosi, A.7
  • 72
    • 0024361909 scopus 로고
    • Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae
    • Vandercammen, A., Francois, J. and Hers, H.G. (1989) Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae. Eur. J. Biochem. 182, 613-620.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 613-620
    • Vandercammen, A.1    Francois, J.2    Hers, H.G.3
  • 73
    • 2642583438 scopus 로고    scopus 로고
    • Differential organ-specific response to salt stress and water deficit in nodulated bean (Phaseolus vulgaris)
    • Verdoy, D., Lucas, M.M., Manrique, E., Covarrubias, A.A., De Felipe, M.R. and Pueyo, J.J. (2004) Differential organ-specific response to salt stress and water deficit in nodulated bean (Phaseolus vulgaris). Plant Cell Environ. 27, 757-767.
    • (2004) Plant Cell Environ. , vol.27 , pp. 757-767
    • Verdoy, D.1    Lucas, M.M.2    Manrique, E.3    Covarrubias, A.A.4    De Felipe, M.R.5    Pueyo, J.J.6
  • 74
    • 33747863801 scopus 로고    scopus 로고
    • Transgenic Medicago truncatula plants that accumulate proline display nitrogen-fixing activity with enhanced tolerance to osmotic stress
    • Verdoy, D., Coba de La Peña, T., Redondo, F.J., Lucas, M.M. and Pueyo, J.J. (2006) Transgenic Medicago truncatula plants that accumulate proline display nitrogen-fixing activity with enhanced tolerance to osmotic stress. Plant Cell Environ. 29, 1913-1923.
    • (2006) Plant Cell Environ. , vol.29 , pp. 1913-1923
    • Verdoy, D.1    Coba de La Peña, T.2    Redondo, F.J.3    Lucas, M.M.4    Pueyo, J.J.5
  • 75
    • 0032800433 scopus 로고    scopus 로고
    • Transgenic overexpression of the transcription factor Alfin1 enhances expression of the endogenous MsPRP2 gene in alfalfa and improves salinity tolerance of the plants
    • Winicov, I. and Bastola, D.R. (1999) Transgenic overexpression of the transcription factor Alfin1 enhances expression of the endogenous MsPRP2 gene in alfalfa and improves salinity tolerance of the plants. Plant Physiol. 120, 473-480.
    • (1999) Plant Physiol. , vol.120 , pp. 473-480
    • Winicov, I.1    Bastola, D.R.2
  • 76
    • 0347625655 scopus 로고    scopus 로고
    • Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and selected mutants
    • Yousef, N., Pistorius, E.K. and Michel, K.P. (2003) Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and selected mutants. Arch. Microbiol. 180, 471-483.
    • (2003) Arch. Microbiol. , vol.180 , pp. 471-483
    • Yousef, N.1    Pistorius, E.K.2    Michel, K.P.3
  • 77
    • 0032715073 scopus 로고    scopus 로고
    • Rhizobium-legume symbiosis and nitrogen fixation under severe conditions and in an arid climate
    • Zahran, H.H. (1999) Rhizobium-legume symbiosis and nitrogen fixation under severe conditions and in an arid climate. Microbiol. Mol. Biol. Rev. 63, 968-989.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 968-989
    • Zahran, H.H.1
  • 79
    • 34248581202 scopus 로고    scopus 로고
    • Stress-inducible flavodoxin from photosynthetic microorganisms, The mistery of flavodoxin loss from the plant genome
    • Zurbriggen, M.D., Tognetti, V.B. and Carrillo, N. (2007) Stress-inducible flavodoxin from photosynthetic microorganisms, The mistery of flavodoxin loss from the plant genome. IUBMB Life, 59, 1-6.
    • (2007) IUBMB Life , vol.59 , pp. 1-6
    • Zurbriggen, M.D.1    Tognetti, V.B.2    Carrillo, N.3
  • 81
    • 71649105851 scopus 로고    scopus 로고
    • Choroplast-generated reactive oxygen species play a major role in localized cell death during the non-host interaction between tobacco and Xanthomonas campestris pv. vesicatoria
    • Zurbriggen, M.D., Carrillo, N., Tognetti, V.B., Melzer, M., Peisker, M., Hause, B. and Hajirezaei, M.-R. (2009) Choroplast-generated reactive oxygen species play a major role in localized cell death during the non-host interaction between tobacco and Xanthomonas campestris pv. vesicatoria. Plant J. 60, 962-973.
    • (2009) Plant J. , vol.60 , pp. 962-973
    • Zurbriggen, M.D.1    Carrillo, N.2    Tognetti, V.B.3    Melzer, M.4    Peisker, M.5    Hause, B.6    Hajirezaei, M.7


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