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Volumn 70, Issue , 2013, Pages 235-245

Overexpression of a tomato carotenoid ɛ-hydroxylase gene alleviates sensitivity to chilling stress in transgenic tobacco

Author keywords

Carotenoid e open hydroxylase gene; Chilling stress; Reactive oxygen species; Tomato; Transgenic tobacco

Indexed keywords

ARABIDOPSIS; LYCOPERSICON ESCULENTUM; NICOTIANA OBTUSIFOLIA; NICOTIANA TABACUM;

EID: 84879525501     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2013.05.035     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 0035204876 scopus 로고    scopus 로고
    • Protecting cotton photosynthesis during moderate chilling at high light intensity by increasing chloroplastic antioxidant enzyme activity
    • Payton P., Webb R., Kornyeyev D., Allen R., Holaday A.S. Protecting cotton photosynthesis during moderate chilling at high light intensity by increasing chloroplastic antioxidant enzyme activity. J.Exp. Bot. 2001, 52:2345-2354.
    • (2001) J.Exp. Bot. , vol.52 , pp. 2345-2354
    • Payton, P.1    Webb, R.2    Kornyeyev, D.3    Allen, R.4    Holaday, A.S.5
  • 2
    • 13944279926 scopus 로고    scopus 로고
    • Leaf movements and photoinhibition in relation to water stress in field-grown beans
    • Pastenes C., Pimentel P., Lillo J. Leaf movements and photoinhibition in relation to water stress in field-grown beans. J.Exp. Bot. 2005, 56:425-433.
    • (2005) J.Exp. Bot. , vol.56 , pp. 425-433
    • Pastenes, C.1    Pimentel, P.2    Lillo, J.3
  • 3
    • 3543058822 scopus 로고    scopus 로고
    • High light stress inducing photoinhibition and protein degradation of photosystem I in Brassica rapa
    • Jiao S., Emmanuel H., Guikema J.A. High light stress inducing photoinhibition and protein degradation of photosystem I in Brassica rapa. Plant Sci. 2004, 167:733-741.
    • (2004) Plant Sci. , vol.167 , pp. 733-741
    • Jiao, S.1    Emmanuel, H.2    Guikema, J.A.3
  • 4
    • 0023303085 scopus 로고
    • Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein
    • Mattoo A.K., Edelman M. Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:1497-1501.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 1497-1501
    • Mattoo, A.K.1    Edelman, M.2
  • 5
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II: inactivation, protein damage and turnover
    • Aro E.M., Virgin I., Andersson B. Photoinhibition of photosystem II: inactivation, protein damage and turnover. Biochim. Biophys. Acta 1993, 1143:113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 8
    • 0031633948 scopus 로고    scopus 로고
    • Antioxidant activity of carotenoids: an electron-spin resonance study on beta-carotene and lutein interaction with free radicals generated in a chemical system
    • Iannone A., Rota C., Bergamini S., Tomasi A., Canfield L.M. Antioxidant activity of carotenoids: an electron-spin resonance study on beta-carotene and lutein interaction with free radicals generated in a chemical system. J.Biochem. Mol. Toxicol. 1998, 12:299-304.
    • (1998) J.Biochem. Mol. Toxicol. , vol.12 , pp. 299-304
    • Iannone, A.1    Rota, C.2    Bergamini, S.3    Tomasi, A.4    Canfield, L.M.5
  • 9
    • 33644756597 scopus 로고    scopus 로고
    • Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3
    • Kim J., Dellapenna D. Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:3474-3479.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3474-3479
    • Kim, J.1    Dellapenna, D.2
  • 10
    • 0034108643 scopus 로고    scopus 로고
    • Pigment composition of freshwater charophyceae
    • Schagerl M., Pichler C. Pigment composition of freshwater charophyceae. Aquat. Bot. 2000, 67:117-129.
    • (2000) Aquat. Bot. , vol.67 , pp. 117-129
    • Schagerl, M.1    Pichler, C.2
  • 11
    • 11144304058 scopus 로고    scopus 로고
    • Carotenoid compositions of cladophora balls (aegagropila linnaei) and some members of the cladophorales (ulvophyceae, chlorophyta): their taxonomic and evolutionary implication
    • Yoshii Y., Hanyuda T., Wakana I., Miyaji K., Arai S., Ueda K., Inouye I. Carotenoid compositions of cladophora balls (aegagropila linnaei) and some members of the cladophorales (ulvophyceae, chlorophyta): their taxonomic and evolutionary implication. J.Phycol. 2004, 40:1170-1177.
    • (2004) J.Phycol. , vol.40 , pp. 1170-1177
    • Yoshii, Y.1    Hanyuda, T.2    Wakana, I.3    Miyaji, K.4    Arai, S.5    Ueda, K.6    Inouye, I.7
  • 12
    • 4544249478 scopus 로고    scopus 로고
    • Carotenoid composition of Delesseria lancifolia and other marine red algae from polar and temperate habitats
    • Marquardt J., Hanelt D. Carotenoid composition of Delesseria lancifolia and other marine red algae from polar and temperate habitats. Eur. J. Phycol. 2004, 39:285-292.
    • (2004) Eur. J. Phycol. , vol.39 , pp. 285-292
    • Marquardt, J.1    Hanelt, D.2
  • 13
    • 0037524332 scopus 로고    scopus 로고
    • Anovel type of lycopene epsilon-cyclase in the marine cyanobacterium Prochlorococcus marinus MED4
    • Stickforth P., Steiger S., Hess W.R., Sandmann G. Anovel type of lycopene epsilon-cyclase in the marine cyanobacterium Prochlorococcus marinus MED4. Arch. Microbiol. 2003, 179:409-415.
    • (2003) Arch. Microbiol. , vol.179 , pp. 409-415
    • Stickforth, P.1    Steiger, S.2    Hess, W.R.3    Sandmann, G.4
  • 14
    • 0346458625 scopus 로고    scopus 로고
    • The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid epsilon-ring hydroxylation activity
    • Tian L., Musetti V., Kim J., Magallanes-Lundback M., Dellapenna D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid epsilon-ring hydroxylation activity. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:402-407.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 402-407
    • Tian, L.1    Musetti, V.2    Kim, J.3    Magallanes-Lundback, M.4    Dellapenna, D.5
  • 15
    • 0034813551 scopus 로고    scopus 로고
    • Characterization of a second carotenoid beta-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus
    • Tian L., DellaPenna D. Characterization of a second carotenoid beta-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus. Plant Mol. Biol. 2001, 47:379-388.
    • (2001) Plant Mol. Biol. , vol.47 , pp. 379-388
    • Tian, L.1    DellaPenna, D.2
  • 17
    • 80255123357 scopus 로고    scopus 로고
    • Characterization of PSI recovery after chilling-induced photoinhibition in cucumber (Cucumis sativus L.) leaves
    • Zhang Z., Jia Y., Gao H., Zhang L., Li H., Meng Q. Characterization of PSI recovery after chilling-induced photoinhibition in cucumber (Cucumis sativus L.) leaves. Planta 2011, 234:883-889.
    • (2011) Planta , vol.234 , pp. 883-889
    • Zhang, Z.1    Jia, Y.2    Gao, H.3    Zhang, L.4    Li, H.5    Meng, Q.6
  • 18
    • 0035208410 scopus 로고    scopus 로고
    • Impacts of chilling temperatures on photosynthesis in warm-climate plants
    • Allen D.J., Ort D.R. Impacts of chilling temperatures on photosynthesis in warm-climate plants. Trends Plant Sci. 2001, 6:36-42.
    • (2001) Trends Plant Sci. , vol.6 , pp. 36-42
    • Allen, D.J.1    Ort, D.R.2
  • 19
    • 0028052392 scopus 로고
    • Mechanism of photosystem I photoinhibition in leaves of Cucumis sativus L
    • Sonoike K., Tereshima I. Mechanism of photosystem I photoinhibition in leaves of Cucumis sativus L. Planta 1994, 194:287-293.
    • (1994) Planta , vol.194 , pp. 287-293
    • Sonoike, K.1    Tereshima, I.2
  • 20
    • 11144313696 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I at chilling temperature and subsequent recovery in Arabidopsis thaliana
    • Zhang S., Scheller H.V. Photoinhibition of photosystem I at chilling temperature and subsequent recovery in Arabidopsis thaliana. Plant Cell Physiol. 2004, 45:1595-1602.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1595-1602
    • Zhang, S.1    Scheller, H.V.2
  • 21
    • 84860248901 scopus 로고    scopus 로고
    • Overexpression of thylakoidal ascorbate peroxidase shows enhanced resistance to chilling stress in tomato
    • Duan M., Feng H.L., Wang L.Y., Li D., Meng Q.W. Overexpression of thylakoidal ascorbate peroxidase shows enhanced resistance to chilling stress in tomato. J.Plant Physiol. 2012, 169:867-877.
    • (2012) J.Plant Physiol. , vol.169 , pp. 867-877
    • Duan, M.1    Feng, H.L.2    Wang, L.Y.3    Li, D.4    Meng, Q.W.5
  • 22
    • 34249960486 scopus 로고
    • Role of the xanthophyll cycle in photoprotection elucidated by measurements of light-induced absorbance changes, fluorescence and photosynthesis in leaves of Hedera canariensis
    • Bilger W., Björkman O. Role of the xanthophyll cycle in photoprotection elucidated by measurements of light-induced absorbance changes, fluorescence and photosynthesis in leaves of Hedera canariensis. Photosynth. Res. 1990, 25:173-185.
    • (1990) Photosynth. Res. , vol.25 , pp. 173-185
    • Bilger, W.1    Björkman, O.2
  • 23
    • 38949185731 scopus 로고    scopus 로고
    • Overexpression of zeaxanthin epoxidase gene enhances the sensitivity of tomato PSII photoinhibition to high light and chilling stress
    • Wang N., Fang W., Han H., Sui N., Li B., Meng Q.W. Overexpression of zeaxanthin epoxidase gene enhances the sensitivity of tomato PSII photoinhibition to high light and chilling stress. Physiol. Plant. 2008, 132:384-396.
    • (2008) Physiol. Plant. , vol.132 , pp. 384-396
    • Wang, N.1    Fang, W.2    Han, H.3    Sui, N.4    Li, B.5    Meng, Q.W.6
  • 24
    • 67650091977 scopus 로고    scopus 로고
    • Differential turnover of the photosystem II reaction centre D1 protein in mesophyll and bundle sheath chloroplasts of maize
    • Pokorska B., Zienkiewicz M., Powikrowska M., Drozak A., Romanowska E. Differential turnover of the photosystem II reaction centre D1 protein in mesophyll and bundle sheath chloroplasts of maize. Biochim. Biophys. Acta 2009, 1787:1161-1169.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1161-1169
    • Pokorska, B.1    Zienkiewicz, M.2    Powikrowska, M.3    Drozak, A.4    Romanowska, E.5
  • 25
    • 80052694671 scopus 로고    scopus 로고
    • The unsaturation of phosphatidylglycerol in thylakoid membrane alleviates PSII photoinhibition under chilling stress
    • Sun X.L., Yang S., Wang L.Y., Zhang Q.Y., Zhao S.J., Meng Q.W. The unsaturation of phosphatidylglycerol in thylakoid membrane alleviates PSII photoinhibition under chilling stress. Plant Cell Rep. 2011, 30:1939-1947.
    • (2011) Plant Cell Rep. , vol.30 , pp. 1939-1947
    • Sun, X.L.1    Yang, S.2    Wang, L.Y.3    Zhang, Q.Y.4    Zhao, S.J.5    Meng, Q.W.6
  • 26
    • 33746761616 scopus 로고    scopus 로고
    • Anew paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II
    • Nishiyama Y., Allakhverdiev S.I., Murata N. Anew paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II. Biochim. Biophys. Acta 2006, 1757:742-749.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 742-749
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Murata, N.3
  • 27
    • 10744226907 scopus 로고    scopus 로고
    • Oxidative modifications of the photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells
    • Lupinkova L., Komenda J. Oxidative modifications of the photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells. Photochem. Photobiol. 2004, 79:152-162.
    • (2004) Photochem. Photobiol. , vol.79 , pp. 152-162
    • Lupinkova, L.1    Komenda, J.2
  • 29
    • 0033523114 scopus 로고    scopus 로고
    • Cotranslational assembly of the D1 protein into photosystem II
    • Zhang L.X., Paakkarinen V., van Wijk K.J., Aro E.M. Cotranslational assembly of the D1 protein into photosystem II. J.Biol. Chem. 1999, 274:16062-16067.
    • (1999) J.Biol. Chem. , vol.274 , pp. 16062-16067
    • Zhang, L.X.1    Paakkarinen, V.2    van Wijk, K.J.3    Aro, E.M.4
  • 30
    • 80052867188 scopus 로고    scopus 로고
    • Cloning and molecular characterization of a mitogen-activated protein kinase gene from Poncirus trifoliata whose ectopic expression confers dehydration/drought tolerance in transgenic tobacco
    • Huang X.S., Luo T., Fu X.Z., Fan Q.J., Liu J.H. Cloning and molecular characterization of a mitogen-activated protein kinase gene from Poncirus trifoliata whose ectopic expression confers dehydration/drought tolerance in transgenic tobacco. J.Exp. Bot. 2011, 62:5191-5206.
    • (2011) J.Exp. Bot. , vol.62 , pp. 5191-5206
    • Huang, X.S.1    Luo, T.2    Fu, X.Z.3    Fan, Q.J.4    Liu, J.H.5
  • 31
    • 84862823232 scopus 로고    scopus 로고
    • Characterization of a wheat (Triticum aestivum L.) expansin gene, TaEXPB23, involved in the abiotic stress response and phytohormone regulation
    • Han Y.Y., Li A.X., Li F., Zhao M.R., Wang W. Characterization of a wheat (Triticum aestivum L.) expansin gene, TaEXPB23, involved in the abiotic stress response and phytohormone regulation. Plant Physiol. Biochem. 2012, 54:49-58.
    • (2012) Plant Physiol. Biochem. , vol.54 , pp. 49-58
    • Han, Y.Y.1    Li, A.X.2    Li, F.3    Zhao, M.R.4    Wang, W.5
  • 32
    • 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
  • 33
    • 34548524151 scopus 로고    scopus 로고
    • Overexpression of glycerol-3-phosphate acyltransferase gene improves chilling tolerance in tomato
    • Sui N., Li M., Zhao S.J., Li F., Liang H., Meng Q.W. Overexpression of glycerol-3-phosphate acyltransferase gene improves chilling tolerance in tomato. Planta 2007, 226:1097-1108.
    • (2007) Planta , vol.226 , pp. 1097-1108
    • Sui, N.1    Li, M.2    Zhao, S.J.3    Li, F.4    Liang, H.5    Meng, Q.W.6
  • 34
    • 0002479657 scopus 로고
    • Quantitative relation between the reaction of hydroxylamine and superoxide anion radicals in plants
    • Wang A.G., Luo G.H. Quantitative relation between the reaction of hydroxylamine and superoxide anion radicals in plants. Plant Physiol. Commun. 1990, 6:55-57.
    • (1990) Plant Physiol. Commun. , vol.6 , pp. 55-57
    • Wang, A.G.1    Luo, G.H.2
  • 35
    • 33750035480 scopus 로고    scopus 로고
    • Dehydroascorbate reductase affects leaf growth, development and function
    • Chen Z., Gallie D.R. Dehydroascorbate reductase affects leaf growth, development and function. Plant Physiol. 2006, 142:775-787.
    • (2006) Plant Physiol. , vol.142 , pp. 775-787
    • Chen, Z.1    Gallie, D.R.2
  • 36
    • 79961023543 scopus 로고    scopus 로고
    • Heterology expression of the sweet pepper CBF3 gene confers elevated tolerance to chilling stress in transgenic tobacco
    • Yang S., Tang X.F., Ma N.N., Wang L.Y., Meng Q.W. Heterology expression of the sweet pepper CBF3 gene confers elevated tolerance to chilling stress in transgenic tobacco. J.Plant Physiol. 2011, 168:1804-1812.
    • (2011) J.Plant Physiol. , vol.168 , pp. 1804-1812
    • Yang, S.1    Tang, X.F.2    Ma, N.N.3    Wang, L.Y.4    Meng, Q.W.5
  • 37
    • 0025429011 scopus 로고
    • Arabidopsis is susceptible to infection by downy mildew fungus
    • Koch E., Slusarenko A. Arabidopsis is susceptible to infection by downy mildew fungus. Plant Cell 1990, 2:437-445.
    • (1990) Plant Cell , vol.2 , pp. 437-445
    • Koch, E.1    Slusarenko, A.2
  • 38
    • 0000448097 scopus 로고
    • Analysis of xanthophylls cycle components in plant tissues by high performance liquid chromatography
    • Zhao S.J., Meng Q.W., Xu C.C., Han H.Y., Zou Q. Analysis of xanthophylls cycle components in plant tissues by high performance liquid chromatography. Plant Physiol. Commun. 1995, 31:438-442.
    • (1995) Plant Physiol. Commun. , vol.31 , pp. 438-442
    • Zhao, S.J.1    Meng, Q.W.2    Xu, C.C.3    Han, H.Y.4    Zou, Q.5
  • 39
    • 34249958267 scopus 로고
    • The use of chlorophyll fluorescence nomenclature in plant stress physiology
    • Kooten O., Snel J.F.H. The use of chlorophyll fluorescence nomenclature in plant stress physiology. Photosynth. Res. 1990, 25:147-150.
    • (1990) Photosynth. Res. , vol.25 , pp. 147-150
    • Kooten, O.1    Snel, J.F.H.2
  • 40
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence-a practical guide
    • Maxwell K., Johnson G.N. Chlorophyll fluorescence-a practical guide. J.Exp. Bot. 2000, 51:659-668.
    • (2000) J.Exp. Bot. , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 41
    • 0000490010 scopus 로고
    • Measuring fast fluorescence transients to address environmental questions: the JIP test
    • Kluwer Academic, Dordrecht, P. Mathis (Ed.)
    • Strasser B.J., Strasser R.J. Measuring fast fluorescence transients to address environmental questions: the JIP test. Photosynthesis: From Light to Biosphere 1995, 977-980. Kluwer Academic, Dordrecht. P. Mathis (Ed.).
    • (1995) Photosynthesis: From Light to Biosphere , pp. 977-980
    • Strasser, B.J.1    Strasser, R.J.2
  • 42
    • 0041851143 scopus 로고    scopus 로고
    • Characterization of the 820nm transmission signal paralleling the chlorophyll a fluorescence rise (OJIP) in pea leaves
    • Schansker G., Srivastava A., Govindjee, Strasser R.J. Characterization of the 820nm transmission signal paralleling the chlorophyll a fluorescence rise (OJIP) in pea leaves. Funct. Plant Biol. 2003, 30:785-796.
    • (2003) Funct. Plant Biol. , vol.30 , pp. 785-796
    • Schansker, G.1    Srivastava, A.2    Govindjee3    Strasser, R.J.4


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