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Volumn 148, Issue 2, 1999, Pages 131-138

Salt tolerance of transgenic rice overexpressing yeast mitochondrial Mn- SOD in chloroplasts

Author keywords

Mn SOD; Oxidative stress; Rice; Salt tolerance; Transgenic rice

Indexed keywords

ASCORBIC ACID; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTAMATE AMMONIA LIGASE; MITOCHONDRIAL ENZYME; PEROXIDASE; SODIUM CHLORIDE; SUPEROXIDE DISMUTASE;

EID: 0033615664     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(99)00133-8     Document Type: Article
Times cited : (177)

References (31)
  • 1
    • 0029922104 scopus 로고    scopus 로고
    • Salt tolerance in plants and microorganisms: Toxicity targets and defense responses
    • Serrano R. Salt tolerance in plants and microorganisms: toxicity targets and defense responses. Int. Rev. Cytol. 165:1996;1-52.
    • (1996) Int. Rev. Cytol. , vol.165 , pp. 1-52
    • Serrano, R.1
  • 3
    • 0031835232 scopus 로고    scopus 로고
    • Physiological responses of plant to salinity: A review
    • Volkmar K.M., Hu Y., Steppuhn H. Physiological responses of plant to salinity: a review. Can. J. Plant Sci. 78:1998;19-27.
    • (1998) Can. J. Plant Sci. , vol.78 , pp. 19-27
    • Volkmar, K.M.1    Hu, Y.2    Steppuhn, H.3
  • 4
    • 0029169261 scopus 로고
    • Synechococcus sp. PCC7942 transformed with Escherichia coli bet genes produces glycine betaine from choline and aquires resistance to salt stress
    • Nomura M., Ishitani M., Takabe T., Rai A.K., Takabe T. Synechococcus sp. PCC7942 transformed with Escherichia coli bet genes produces glycine betaine from choline and aquires resistance to salt stress. Plant Physiol. 107:1995;703-708.
    • (1995) Plant Physiol. , vol.107 , pp. 703-708
    • Nomura, M.1    Ishitani, M.2    Takabe, T.3    Rai, A.K.4    Takabe, T.5
  • 5
    • 0027464813 scopus 로고
    • Stress protection of transgenic tobacco by production of the osmolyte mannitol
    • Tarczynski M.C., Jensen R.G., Bohnert H.J. Stress protection of transgenic tobacco by production of the osmolyte mannitol. Science. 259:1993;508-510.
    • (1993) Science , vol.259 , pp. 508-510
    • Tarczynski, M.C.1    Jensen, R.G.2    Bohnert, H.J.3
  • 6
    • 0029882770 scopus 로고    scopus 로고
    • Oxidative stress and responses in Arabidopsis thaliana and Oryza sativa subjected to chilling and salinity stress
    • Burdon R.H., O'Kane D., Fadzillah N., Gill V., Boyd P.A., Finch R.P. Oxidative stress and responses in Arabidopsis thaliana and Oryza sativa subjected to chilling and salinity stress. Biochem. Soc. Trans. 24:1996;468-472.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 468-472
    • Burdon, R.H.1    O'Kane, D.2    Fadzillah, N.3    Gill, V.4    Boyd, P.A.5    Finch, R.P.6
  • 7
    • 0027947876 scopus 로고
    • Antioxidant response to salt stress in salt-tolerant and salt-sensitive cultivars of cotton
    • Gossett D.R., Millhollon E.P., Lucas M.C. Antioxidant response to salt stress in salt-tolerant and salt-sensitive cultivars of cotton. Crop Sci. 34:1994;706-714.
    • (1994) Crop Sci. , vol.34 , pp. 706-714
    • Gossett, D.R.1    Millhollon, E.P.2    Lucas, M.C.3
  • 9
    • 0028005662 scopus 로고
    • ABA as a modulator of the response of Pisum sativum to salt stress
    • Fendina I.S., Tsonev T.D., Guleva E.I. ABA as a modulator of the response of Pisum sativum to salt stress. J. Plant Physiol. 143:1994;245-249.
    • (1994) J. Plant Physiol. , vol.143 , pp. 245-249
    • Fendina, I.S.1    Tsonev, T.D.2    Guleva, E.I.3
  • 10
    • 0001453595 scopus 로고
    • Perspectives on photoinhibition: And photorespiration in the field: Quintessential inefficiencies of the light and dark reactions of photosynthesis?
    • Osmond C.B., Grace S.C. Perspectives on photoinhibition: and photorespiration in the field: quintessential inefficiencies of the light and dark reactions of photosynthesis? J. Exp. Bot. 46:1995;1351-1362.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1351-1362
    • Osmond, C.B.1    Grace, S.C.2
  • 11
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • C.H. Foyer, & P.M. Mullineaux. Boca Raton, FL: CRC Press
    • Asada K. Production and action of active oxygen species in photosynthetic tissues. Foyer C.H., Mullineaux P.M. Causes of Photooxidative Stress in Plants and Amelioration of Defense Systems. 1994;77-104 CRC Press, Boca Raton, FL.
    • (1994) Causes of Photooxidative Stress in Plants and Amelioration of Defense Systems , pp. 77-104
    • Asada, K.1
  • 13
    • 84994930460 scopus 로고
    • Protection against oxygen radicals: An important defence mechanism studied in transgenic plants
    • Foyer C.H., Descourvieres P., Kunert K.J. Protection against oxygen radicals: an important defence mechanism studied in transgenic plants. Plant Cell Environ. 17:1994;507-523.
    • (1994) Plant Cell Environ. , vol.17 , pp. 507-523
    • Foyer, C.H.1    Descourvieres, P.2    Kunert, K.J.3
  • 14
    • 0027141553 scopus 로고
    • Overexpression of superoxide dismutase protects plants from oxidative stress
    • Gupta A.S., Webb R.P., Holaday A.S., Allen R.D. Overexpression of superoxide dismutase protects plants from oxidative stress. Plant Physiol. 103:1993;1067-1073.
    • (1993) Plant Physiol. , vol.103 , pp. 1067-1073
    • Gupta, A.S.1    Webb, R.P.2    Holaday, A.S.3    Allen, R.D.4
  • 16
    • 0029824775 scopus 로고    scopus 로고
    • Water-deficient tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie B.D., Bowley S.R., Harjanto E., Leprince O. Water-deficient tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase. Plant Physiol. 111:1996;1171-1177.
    • (1996) Plant Physiol. , vol.111 , pp. 1171-1177
    • McKersie, B.D.1    Bowley, S.R.2    Harjanto, E.3    Leprince, O.4
  • 17
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • Van Camp W., Capiau K., Van Montagu M., Inze D., Slooten L. Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts. Plant Physiol. 112:1996;1703-1714.
    • (1996) Plant Physiol. , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiau, K.2    Van Montagu, M.3    Inze, D.4    Slooten, L.5
  • 18
    • 0030856013 scopus 로고    scopus 로고
    • Over-expression of chloroplast-targeted Mn superoxide dismutase in cotton (Gossypium hirsutum L., cv. Coker 312) does not alter the reduction of photosynthesis after short exposures to low temperature and high light intensity
    • Payton P., Allen R.D., Trolinder N., Holaday A.S. Over-expression of chloroplast-targeted Mn superoxide dismutase in cotton (Gossypium hirsutum L., cv. Coker 312) does not alter the reduction of photosynthesis after short exposures to low temperature and high light intensity. Photosynth. Res. 52:1997;233-244.
    • (1997) Photosynth. Res. , vol.52 , pp. 233-244
    • Payton, P.1    Allen, R.D.2    Trolinder, N.3    Holaday, A.S.4
  • 20
    • 0030945883 scopus 로고    scopus 로고
    • Salinity, oxidative stress and antioxidant responses in shoot cultures of rice
    • Fadzilla N.M., Finch R.P., Burdon R.H. Salinity, oxidative stress and antioxidant responses in shoot cultures of rice. J. Exp. Bot. 48:1997;325-331.
    • (1997) J. Exp. Bot. , vol.48 , pp. 325-331
    • Fadzilla, N.M.1    Finch, R.P.2    Burdon, R.H.3
  • 21
    • 0022425508 scopus 로고
    • Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron-sulphur protein
    • Marres C.A., Van Loon A.P., Oudshoorn P., Van Steeg H., Grivell L.A., Slater E.C. Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron-sulphur protein. Eur. J. Biochem. 147:1985;153-161.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 153-161
    • Marres, C.A.1    Van Loon, A.P.2    Oudshoorn, P.3    Van Steeg, H.4    Grivell, L.A.5    Slater, E.C.6
  • 22
    • 36849147927 scopus 로고
    • Fertile transgenic rice plants regenerated from transformed protoplasts
    • Shimamoto K., Terada R., Izawa T., Fujimoto H. Fertile transgenic rice plants regenerated from transformed protoplasts. Nature. 338:1989;274-276.
    • (1989) Nature , vol.338 , pp. 274-276
    • Shimamoto, K.1    Terada, R.2    Izawa, T.3    Fujimoto, H.4
  • 23
    • 0025831646 scopus 로고
    • Reconstitution of mature plastocyanin from precursor apo-plastocyanin expressed in Escherichia coli
    • Hibino T., Douwe de Boer A., Weisbeek P.J., Takabe T. Reconstitution of mature plastocyanin from precursor apo-plastocyanin expressed in Escherichia coli. Biochim. Biophys. Acta. 1058:1991;107-112.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 107-112
    • Hibino, T.1    Douwe De Boer, A.2    Weisbeek, P.J.3    Takabe, T.4
  • 24
    • 0015848053 scopus 로고
    • Isozymes of superoxide dismutase from wheat germ
    • Beauchamp C.O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim. Biophys. Acta. 317:1973;50-64.
    • (1973) Biochim. Biophys. Acta , vol.317 , pp. 50-64
    • Beauchamp, C.O.1    Fridovich, I.2
  • 25
    • 0031452246 scopus 로고    scopus 로고
    • Electron flow from NAD(P)H dehydrogenase to Photosystem I is required for adaptation to salt shock in cyanobacterium Synechocystis sp. PCC 6803
    • Tanaka Y., Katada S., Ishikawa H., Ogawa T., Takabe T. Electron flow from NAD(P)H dehydrogenase to Photosystem I is required for adaptation to salt shock in cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 38:1997;1311-1318.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1311-1318
    • Tanaka, Y.1    Katada, S.2    Ishikawa, H.3    Ogawa, T.4    Takabe, T.5
  • 26
    • 12044251905 scopus 로고
    • Chlorophyll fluorescence and phytosynthesis: The basics
    • Krause G.H., Weis E. Chlorophyll fluorescence and phytosynthesis: the basics. Annu. Rev. Plant Physiol. 42:1991;313-349.
    • (1991) Annu. Rev. Plant Physiol. , vol.42 , pp. 313-349
    • Krause, G.H.1    Weis, E.2
  • 27
    • 0021348561 scopus 로고
    • Localization of lysosomal and peroxisomal enzymes in the specific granules of rat intestinal eosinophil leukocytes revealed by immunoelectron microscopic techniques
    • Yokota S., Tsuji H., Kato K. Localization of lysosomal and peroxisomal enzymes in the specific granules of rat intestinal eosinophil leukocytes revealed by immunoelectron microscopic techniques. J. Histochem. Cytochem. 32:1984;267-274.
    • (1984) J. Histochem. Cytochem. , vol.32 , pp. 267-274
    • Yokota, S.1    Tsuji, H.2    Kato, K.3
  • 28
    • 0002879407 scopus 로고
    • Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail
    • Kanematsu S., Asada K. Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail. Plant Cell Physiol. 31:1990;99-112.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 99-112
    • Kanematsu, S.1    Asada, K.2
  • 29
    • 0029169262 scopus 로고
    • Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing manganese superoxide dismutase in the chloroplasts
    • Slooten L., Capiau K., Van Camp W., Van Montagu M., Sybesma C., Inze D. Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing manganese superoxide dismutase in the chloroplasts. Plant Physiol. 107:1995;737-750.
    • (1995) Plant Physiol. , vol.107 , pp. 737-750
    • Slooten, L.1    Capiau, K.2    Van Camp, W.3    Van Montagu, M.4    Sybesma, C.5    Inze, D.6
  • 30
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell. 79:1994;583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 31
    • 0028801954 scopus 로고
    • Attachment of CuZn-superoxide dismutase to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplasts: Detection by immuno-gold labeling after rapid freezing and substitution method
    • Ogawa K., Kanematsu S., Takabe K., Asada K. Attachment of CuZn-superoxide dismutase to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplasts: detection by immuno-gold labeling after rapid freezing and substitution method. Plant Cell Physiol. 36:1995;565-573.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 565-573
    • Ogawa, K.1    Kanematsu, S.2    Takabe, K.3    Asada, K.4


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