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Volumn 51, Issue 342, 2000, Pages 123-130

Bundle sheath proteins are more sensitive to oxidative damage than those of the mesophyll in maize leaves exposed to paraquat or low temperatures

Author keywords

Maize; Oxidative damage; Protein degradation

Indexed keywords

ANTIOXIDANT; BUNDLE SHEATH PROTEIN; COLD TOLERANCE; ENZYME ACTIVITY; GENE PRODUCT; LOW TEMPERATURE; MAIZE; MESOPHYLL; OXIDATION; PARAQUAT; PHOTOSYSTEM II; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 0033959934     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/51.342.123     Document Type: Article
Times cited : (110)

References (41)
  • 1
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro E-M, Virgin I, Andersson B. 1993. Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochimica et Biophysica Acta 1143, 113-134.
    • (1993) Biochimica et Biophysica Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 3
    • 0038761280 scopus 로고
    • Perturbation of chloroplast development in maize by low growth temperature
    • Bredenkamp GJ, Nie GY, Baker NR. 1992. Perturbation of chloroplast development in maize by low growth temperature. Photosynthetica 27, 401-411.
    • (1992) Photosynthetica , vol.27 , pp. 401-411
    • Bredenkamp, G.J.1    Nie, G.Y.2    Baker, N.R.3
  • 4
    • 0000101694 scopus 로고    scopus 로고
    • Cyst(e)ine is the transport metabolite of assimilated sulfur from bundle-sheath to mesophyll cells in maize leaves
    • Burgener M, Suter M, Jones S, Brunhold C. 1998. Cyst(e)ine is the transport metabolite of assimilated sulfur from bundle-sheath to mesophyll cells in maize leaves. Plant Physiology 116, 1315-1322.
    • (1998) Plant Physiology , vol.116 , pp. 1315-1322
    • Burgener, M.1    Suter, M.2    Jones, S.3    Brunhold, C.4
  • 5
    • 84981566824 scopus 로고
    • The roles of low temperature and light in accumulation of a 31 kDa polypeptide in the light-harvesting apparatus of maize leaves
    • Covello PS, Hayden DB, Baker NR. 1988. The roles of low temperature and light in accumulation of a 31 kDa polypeptide in the light-harvesting apparatus of maize leaves. Plant, Cell and Environment 11, 481-486.
    • (1988) Plant, Cell and Environment , vol.11 , pp. 481-486
    • Covello, P.S.1    Hayden, D.B.2    Baker, N.R.3
  • 6
    • 0001165153 scopus 로고    scopus 로고
    • Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
    • Desimone M, Henke A, Wagner E. 1996. Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley. Plant Physiology 111, 789-796.
    • (1996) Plant Physiology , vol.111 , pp. 789-796
    • Desimone, M.1    Henke, A.2    Wagner, E.3
  • 7
    • 0002865296 scopus 로고
    • Herbicide action and effects on detoxification processes
    • Foyer CH, Mullineaux PM, eds. Boca Raton: CRC Press
    • Dodge AD. 1994. Herbicide action and effects on detoxification processes. In: Foyer CH, Mullineaux PM, eds. Causes of photooxidative stress and amelioration of defence systems in plants. Boca Raton: CRC Press, 219-237.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 219-237
    • Dodge, A.D.1
  • 9
    • 0029139047 scopus 로고
    • Oxidative modification of Rubisco from potato foliage in response to ozone
    • Eckardt NA, Pell EJ. 1995. Oxidative modification of Rubisco from potato foliage in response to ozone. Plant Physiology and Biochemistry 33, 273-282.
    • (1995) Plant Physiology and Biochemistry , vol.33 , pp. 273-282
    • Eckardt, N.A.1    Pell, E.J.2
  • 10
    • 2642690667 scopus 로고    scopus 로고
    • Protein degradation in C3 and C4 plants with particular reference to ribulose bisphosphate carboxylase and glycolate oxidase
    • Esquival MG, Ferreira RB, Teixeira AR. 1997. Protein degradation in C3 and C4 plants with particular reference to ribulose bisphosphate carboxylase and glycolate oxidase. Journal of Experimental Botany 49, 807-816.
    • (1997) Journal of Experimental Botany , vol.49 , pp. 807-816
    • Esquival, M.G.1    Ferreira, R.B.2    Teixeira, A.R.3
  • 12
    • 0028155031 scopus 로고
    • Oxidative modification and breakdown of ribulose 1,5-bisphosphale carboxylase/ oxygcnase induced in Euglena gracilis by nitrogen starvation
    • Garcia-Ferris C, Moreno J. 1994. Oxidative modification and breakdown of ribulose 1,5-bisphosphale carboxylase/ oxygcnase induced in Euglena gracilis by nitrogen starvation. Planta 193, 208-215.
    • (1994) Planta , vol.193 , pp. 208-215
    • Garcia-Ferris, C.1    Moreno, J.2
  • 13
    • 0000845599 scopus 로고
    • 4 photosynthesis
    • Stocking CR, Heber U, eds. Berlin: Springer-Verlag
    • 4 photosynthesis. In: Stocking CR, Heber U, eds. Encyclopedia of plant physiology, Vol. 3. Berlin: Springer-Verlag, 144-184.
    • (1976) Encyclopedia of Plant Physiology , vol.3 , pp. 144-184
    • Hatch, M.D.1    Osmond, C.B.2
  • 14
    • 0342385343 scopus 로고
    • Modification of the photosystem II light-harvesting chlorophyll a/b protein complex in maize during chill-induced photoinhibition
    • Hayden DB, Baker NR, Percival MP, Beckwith PB. 1986. Modification of the photosystem II light-harvesting chlorophyll a/b protein complex in maize during chill-induced photoinhibition. Biochimica et Biophysica Acta 851, 86-92.
    • (1986) Biochimica et Biophysica Acta , vol.851 , pp. 86-92
    • Hayden, D.B.1    Baker, N.R.2    Percival, M.P.3    Beckwith, P.B.4
  • 15
    • 0343254801 scopus 로고
    • Characterisation of a 31 kDa polypeptide that accumulates in the light-harvesting apparatus of maize leaves during chilling
    • Hayden DB, Covello PS, Baker NR. 1988. Characterisation of a 31 kDa polypeptide that accumulates in the light-harvesting apparatus of maize leaves during chilling. Photosynthesis Research 15, 257-270.
    • (1988) Photosynthesis Research , vol.15 , pp. 257-270
    • Hayden, D.B.1    Covello, P.S.2    Baker, N.R.3
  • 16
    • 0031113714 scopus 로고    scopus 로고
    • The large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase is fragmented into 37 kDa and 16 kDa polypeptides by active oxygen in the lysates of chloroplasts from primary leaves of wheat
    • Ishida H, Nishimori Y, Sugisawa M, Makino A, Mae T. 1997. The large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase is fragmented into 37 kDa and 16 kDa polypeptides by active oxygen in the lysates of chloroplasts from primary leaves of wheat. Plant and Cell Physiology 38, 471-479.
    • (1997) Plant and Cell Physiology , vol.38 , pp. 471-479
    • Ishida, H.1    Nishimori, Y.2    Sugisawa, M.3    Makino, A.4    Mae, T.5
  • 18
    • 0003011378 scopus 로고
    • Photoinhibition induced by low temperatures
    • Baker NR, Bowyer JR, eds. Oxford: Bios Scientific Publishers Ltd
    • Krause GH. 1994. Photoinhibition induced by low temperatures. In: Baker NR, Bowyer JR, eds. Photoinhihition of photosynthesis from molecular mechanisms to the field. Oxford: Bios Scientific Publishers Ltd, 331-348.
    • (1994) Photoinhihition of Photosynthesis from Molecular Mechanisms to the Field , pp. 331-348
    • Krause, G.H.1
  • 20
    • 0001401826 scopus 로고
    • 3-stressed hybrid poplar (Populus maximowizii × trichocarpa)
    • 3-stressed hybrid poplar (Populus maximowizii × trichocarpa). Plant Physiology 101, 1355-1362.
    • (1993) Plant Physiology , vol.101 , pp. 1355-1362
    • Landry, L.G.1    Pell, E.J.2
  • 21
    • 0031403568 scopus 로고    scopus 로고
    • Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit, CP29
    • Mauro S, Dainese P, Lannoye R, Bassi R. 1997. Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit, CP29. Plant Physiology 115, 171-180.
    • (1997) Plant Physiology , vol.115 , pp. 171-180
    • Mauro, S.1    Dainese, P.2    Lannoye, R.3    Bassi, R.4
  • 22
    • 0000586606 scopus 로고
    • Chloroplast photooxidation inhibits the expression of a set of nuclear genes
    • Mayfield SP, Taylor WC. 1987. Chloroplast photooxidation inhibits the expression of a set of nuclear genes. Molecular and General Genetics 208, 309-314.
    • (1987) Molecular and General Genetics , vol.208 , pp. 309-314
    • Mayfield, S.P.1    Taylor, W.C.2
  • 23
    • 0026795063 scopus 로고
    • Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1,5-bisphosphate carboxylase/ oxygenase
    • Mehta RA, Fawcett TW, Porath D, Mattoo AK. 1992. Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1,5-bisphosphate carboxylase/ oxygenase. Journal of Biological Chemistry 267, 2810-2816.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 2810-2816
    • Mehta, R.A.1    Fawcett, T.W.2    Porath, D.3    Mattoo, A.K.4
  • 24
    • 0029127671 scopus 로고
    • Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: Implications for the mechanism of degradation of D1 protein under illumination
    • Miyao M, Ikeuchi M, Yamamoto N, Ono T. 1995. Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: implications for the mechanism of degradation of D1 protein under illumination. Biochemistry 34, 10019-10026.
    • (1995) Biochemistry , vol.34 , pp. 10019-10026
    • Miyao, M.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.4
  • 25
    • 0002815007 scopus 로고
    • Modifications to thylakoid composition during development of maize leaves at low growth temperatures
    • Nie GY, Baker NR. 1991. Modifications to thylakoid composition during development of maize leaves at low growth temperatures. Plant Physiology 95, 184-191.
    • (1991) Plant Physiology , vol.95 , pp. 184-191
    • Nie, G.Y.1    Baker, N.R.2
  • 26
    • 12044252115 scopus 로고
    • Abrupt increase in the level of hydrogen peroxide in leaves of winter wheat is caused by cold treatment
    • Okuda T, Matsuda Y, Yamanaka A, Sagisaka S. 1991. Abrupt increase in the level of hydrogen peroxide in leaves of winter wheat is caused by cold treatment. Plant Physiology 97, 1265-1267.
    • (1991) Plant Physiology , vol.97 , pp. 1265-1267
    • Okuda, T.1    Matsuda, Y.2    Yamanaka, A.3    Sagisaka, S.4
  • 27
    • 0030482428 scopus 로고    scopus 로고
    • Mechanisms of chilling-induced oxidative stress injury and tolerance: Changes in antioxidant system, oxidation of proteins and lipids and protease activities
    • Prasad TK. 1996. Mechanisms of chilling-induced oxidative stress injury and tolerance: changes in antioxidant system, oxidation of proteins and lipids and protease activities. The Plant Journal 10, 1017-1026.
    • (1996) The Plant Journal , vol.10 , pp. 1017-1026
    • Prasad, T.K.1
  • 28
    • 0031397706 scopus 로고    scopus 로고
    • Role of catalase in inducing chilling tolerance in pre-emergent maize seedlings
    • Prasad TK. 1997. Role of catalase in inducing chilling tolerance in pre-emergent maize seedlings. Plant Physiology 114, 1369-1376.
    • (1997) Plant Physiology , vol.114 , pp. 1369-1376
    • Prasad, T.K.1
  • 29
    • 0028835512 scopus 로고
    • Localization and characterization of peroxidases in the mitochondria of chilling-acclimated maize seedlings
    • Prasad TK, Anderson MD, Stewart CR. 1995. Localization and characterization of peroxidases in the mitochondria of chilling-acclimated maize seedlings. Plant Physiology 108, 1597-1605.
    • (1995) Plant Physiology , vol.108 , pp. 1597-1605
    • Prasad, T.K.1    Anderson, M.D.2    Stewart, C.R.3
  • 30
    • 85051557193 scopus 로고    scopus 로고
    • Corn: Distribution of photoassimilates and source-sink relationships
    • Zamski E, Schaffer AA, eds. New York: Marcel Dekker
    • Prioul J-L. 1996. Corn: distribution of photoassimilates and source-sink relationships. In: Zamski E, Schaffer AA, eds. Photoassimilate distribution in plants and crops: source sink relationships. New York: Marcel Dekker, 549-594.
    • (1996) Photoassimilate Distribution in Plants and Crops: Source Sink Relationships , pp. 549-594
    • Prioul, J.-L.1
  • 31
    • 0001037552 scopus 로고
    • Photooxidative destruction of chloroplasts and its consequences for cytosolic enzyme levels and plant development
    • Reiß T, Bergfeld R, Link G, Mohr H. 1983. Photooxidative destruction of chloroplasts and its consequences for cytosolic enzyme levels and plant development. Planta 159, 518-528.
    • (1983) Planta , vol.159 , pp. 518-528
    • Reiß, T.1    Bergfeld, R.2    Link, G.3    Mohr, H.4
  • 32
    • 84989063367 scopus 로고
    • Chloroplast thylakoid protein changes induced by low growth temperature in maize revealed by immunocytology
    • Robertson EJ, Baker NR, Leech RM. 1993. Chloroplast thylakoid protein changes induced by low growth temperature in maize revealed by immunocytology. Plant, Cell and Environment 16, 809-618.
    • (1993) Plant, Cell and Environment , vol.16 , pp. 809-1618
    • Robertson, E.J.1    Baker, N.R.2    Leech, R.M.3
  • 33
    • 0018211912 scopus 로고
    • Biochemical and genetic studies of the synthesis and degradation of RuBP carboxylase
    • Siegelman HW, Hind G. eds. London: Plenum Press
    • Simpson E. 1978. Biochemical and genetic studies of the synthesis and degradation of RuBP carboxylase. In: Siegelman HW, Hind G. eds. Photosynthetic carbon assimilation. London: Plenum Press, 113-125.
    • (1978) Photosynthetic Carbon Assimilation , pp. 113-125
    • Simpson, E.1
  • 35
    • 0028855112 scopus 로고
    • Selective photoinhibition of photosystem I in isolated thylakoid membranes from cucumber and spinach
    • Sonoike K. 1995. Selective photoinhibition of photosystem I in isolated thylakoid membranes from cucumber and spinach. Plant and Cell Physiology 36, 825-830.
    • (1995) Plant and Cell Physiology , vol.36 , pp. 825-830
    • Sonoike, K.1
  • 36
    • 0000628304 scopus 로고    scopus 로고
    • Degradation of the psaB gene product, the reaction centre subunit of photosystem I, is caused during photoinhibition of photosystem I: Possible involvement of active oxygen species
    • Sonoike K. 1996. Degradation of the psaB gene product, the reaction centre subunit of photosystem I, is caused during photoinhibition of photosystem I: possible involvement of active oxygen species. Plant Science 115, 157-164.
    • (1996) Plant Science , vol.115 , pp. 157-164
    • Sonoike, K.1
  • 37
    • 0028052392 scopus 로고
    • Mechanism of the photosystem I photoinhibition in leaves of Cucumis sativus L
    • Sonoike K, Terashima I. 1994. Mechanism of the photosystem I photoinhibition in leaves of Cucumis sativus L. Planta 194, 287-293.
    • (1994) Planta , vol.194 , pp. 287-293
    • Sonoike, K.1    Terashima, I.2
  • 38
    • 0028985765 scopus 로고
    • Destruction of photosystem I iron-sulfur centres in leaves of Cucumis sativus L. by weak illumination at chilling temperatures
    • Sonoike K, Terashima I, Iwaki M, Itoh S. 1995. Destruction of photosystem I iron-sulfur centres in leaves of Cucumis sativus L. by weak illumination at chilling temperatures. FEBS Letters 362, 235-238.
    • (1995) FEBS Letters , vol.362 , pp. 235-238
    • Sonoike, K.1    Terashima, I.2    Iwaki, M.3    Itoh, S.4
  • 39
    • 0028025799 scopus 로고
    • The site of photoinhibition in leaves of Cucumis sativus L. at low temperatures is photosystem I. not photosystem II
    • Terashima I, Funayama S, Sonoike K. 1994. the site of photoinhibition in leaves of Cucumis sativus L. at low temperatures is photosystem I. not photosystem II. Planta 193, 300-306.
    • (1994) Planta , vol.193 , pp. 300-306
    • Terashima, I.1    Funayama, S.2    Sonoike, K.3
  • 40
    • 0029921367 scopus 로고    scopus 로고
    • The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity
    • Tyystjärvi E, Aro E-M. 1996. The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity. Proceedings of the National Academy of Science, USA 93, 2213-2218.
    • (1996) Proceedings of the National Academy of Science, USA , vol.93 , pp. 2213-2218
    • Tyystjärvi, E.1    Aro, E.-M.2
  • 41
    • 0028278197 scopus 로고
    • Role of plastoquinol oxidoreduction in regulation of photochemical reaction centre II D1 protein turnover in vivo
    • Zer H, Prasil O, Ohad I. 1994. Role of plastoquinol oxidoreduction in regulation of photochemical reaction centre II D1 protein turnover in vivo. Journal of Biological Chemistry 26, 17670-17676.
    • (1994) Journal of Biological Chemistry , vol.26 , pp. 17670-17676
    • Zer, H.1    Prasil, O.2    Ohad, I.3


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