메뉴 건너뛰기




Volumn 143, Issue 4, 2011, Pages 355-366

Overexpression of SsCHLAPXs confers protection against oxidative stress induced by high light in transgenic Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBATE PEROXIDASE; CATALASE; CHLOROPHYLL; MALONALDEHYDE; PLANT DNA; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; THYLAKOID MEMBRANE PROTEIN; VEGETABLE PROTEIN;

EID: 80555122913     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2011.01515.x     Document Type: Article
Times cited : (60)

References (44)
  • 1
    • 0030925516 scopus 로고    scopus 로고
    • Use of transgenic plants to study antioxidant defenses.
    • Allen RD, Webb RP, Schake SA (1997) Use of transgenic plants to study antioxidant defenses. Free Radic Biol Med 23: 473-479
    • (1997) Free Radic Biol Med , vol.23 , pp. 473-479
    • Allen, R.D.1    Webb, R.P.2    Schake, S.A.3
  • 2
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: metabolism, oxidative stress, and signal transduction.
    • Apel K, Hirt H (2004) Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55: 373-399
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 3
    • 84983392009 scopus 로고
    • Ascorbate peroxidase - a hydrogen peroxide-scavenging enzyme in plants.
    • Asada K (1992) Ascorbate peroxidase - a hydrogen peroxide-scavenging enzyme in plants. Physiol Plant 85: 235-241
    • (1992) Physiol Plant , vol.85 , pp. 235-241
    • Asada, K.1
  • 4
    • 2942615094 scopus 로고    scopus 로고
    • Over-expression of ascorbate peroxidase in tobacco chloroplasts enhances the tolerance to salt stresses and water deficit.
    • Badawi GH, Kawano N, Yamauchi Y, Shimada E, Sasaki R, Kubo A, Tanaka K (2004) Over-expression of ascorbate peroxidase in tobacco chloroplasts enhances the tolerance to salt stresses and water deficit. Physiol Plant 121: 231-238
    • (2004) Physiol Plant , vol.121 , pp. 231-238
    • Badawi, G.H.1    Kawano, N.2    Yamauchi, Y.3    Shimada, E.4    Sasaki, R.5    Kubo, A.6    Tanaka, K.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
    • Bradford MM (1976) A rapid and sensitive method 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
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction.
    • Chomczynski P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana.
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 10
    • 0000597483 scopus 로고
    • Superoxide dismutases I. Occurrence in higher plants.
    • Giannopolitis CN, Ries SK (1977) Superoxide dismutases I. Occurrence in higher plants. Plant Physiol 59: 309-314
    • (1977) Plant Physiol , vol.59 , pp. 309-314
    • Giannopolitis, C.N.1    Ries, S.K.2
  • 11
    • 0031449067 scopus 로고    scopus 로고
    • Salt and oxidative stress: similar and specific responses and their relation to salt tolerance in Citrus.
    • Gueta-Dahan Y, Yaniv Z, Zilinskas BA, Ben-Hayyim G (1997) Salt and oxidative stress: similar and specific responses and their relation to salt tolerance in Citrus. Planta 203: 460-469
    • (1997) Planta , vol.203 , pp. 460-469
    • Gueta-Dahan, Y.1    Yaniv, Z.2    Zilinskas, B.A.3    Ben-Hayyim, G.4
  • 13
    • 0030210553 scopus 로고    scopus 로고
    • Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies.
    • Hayashi M, Aoki M, Kato A, Kondo M, Nishimura M (1996) Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J 10: 225-234
    • (1996) Plant J , vol.10 , pp. 225-234
    • Hayashi, M.1    Aoki, M.2    Kato, A.3    Kondo, M.4    Nishimura, M.5
  • 14
    • 0030773115 scopus 로고    scopus 로고
    • From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase.
    • Jespersen HM, Kjærsgård IVH, Østergaard L, Welinder KG (1997) From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase. Biochem J 326: 305-310
    • (1997) Biochem J , vol.326 , pp. 305-310
    • Jespersen, H.M.1    Kjærsgård, I.V.H.2    Østergaard, L.3    Welinder, K.G.4
  • 15
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves.
    • Jiménez A, Hernández JA, del Río LA, Sevilla F (1997) Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol 114: 275-284
    • (1997) Plant Physiol , vol.114 , pp. 275-284
    • Jiménez, A.1    Hernández, J.A.2    del Río, L.A.3    Sevilla, F.4
  • 16
    • 7944239352 scopus 로고    scopus 로고
    • Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves.
    • Jiménez A, Hernández JA, Pastori G, del Río LA, Sevilla F (1998) Role of the ascorbate-glutathione cycle of mitochondria and peroxisomes in the senescence of pea leaves. Plant Physiol 118: 1327-1335
    • (1998) Plant Physiol , vol.118 , pp. 1327-1335
    • Jiménez, A.1    Hernández, J.A.2    Pastori, G.3    del Río, L.A.4    Sevilla, F.5
  • 18
    • 77957068711 scopus 로고
    • Chlorophylls and carotenoids: pigments of photosynthetic biomembranes.
    • Lichtenthaler HK (1987) Chlorophylls and carotenoids: pigments of photosynthetic biomembranes. Methods Enzymol 148: 350-382
    • (1987) Methods Enzymol , vol.148 , pp. 350-382
    • Lichtenthaler, H.K.1
  • 19
    • 0030836047 scopus 로고    scopus 로고
    • Stromal and thylakoid-bound ascorbate peroxidases are produced by alternative splicing in pumpkin.
    • Mano S, Yamaguchi K, Hayashi M, Nishimura M (1997) Stromal and thylakoid-bound ascorbate peroxidases are produced by alternative splicing in pumpkin. FEBS Lett 413: 21-26
    • (1997) FEBS Lett , vol.413 , pp. 21-26
    • Mano, S.1    Yamaguchi, K.2    Hayashi, M.3    Nishimura, M.4
  • 20
    • 48949104251 scopus 로고    scopus 로고
    • The integration of glutathione homeostasis and redox signaling.
    • Meyer AJ (2008) The integration of glutathione homeostasis and redox signaling. J Plant Physiol 165: 1390-1403
    • (2008) J Plant Physiol , vol.165 , pp. 1390-1403
    • Meyer, A.J.1
  • 21
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance.
    • Mittler R (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7: 405-410
    • (2002) Trends Plant Sci , vol.7 , pp. 405-410
    • Mittler, R.1
  • 23
    • 2942717138 scopus 로고    scopus 로고
    • Arabidopsis thaliana plants overexpressing thylakoidal ascorbate peroxidase show increased resistance to paraquat-induced photooxidative stress and to nitric oxide-induced cell death.
    • Murgia I, Tarantino D, Vannini C, Bracale M, Carrabvieri S, Soave C (2004) Arabidopsis thaliana plants overexpressing thylakoidal ascorbate peroxidase show increased resistance to paraquat-induced photooxidative stress and to nitric oxide-induced cell death. Plant J 38: 940-953
    • (2004) Plant J , vol.38 , pp. 940-953
    • Murgia, I.1    Tarantino, D.2    Vannini, C.3    Bracale, M.4    Carrabvieri, S.5    Soave, C.6
  • 24
    • 0036001076 scopus 로고    scopus 로고
    • Hydrogen peroxide and nitric oxide as signalling molecules in plants.
    • Neill SJ, Desikan R, Clarke A, Hurst RD, Hancock JT (2002a) Hydrogen peroxide and nitric oxide as signalling molecules in plants. J Exp Bot 53: 1237-1242
    • (2002) J Exp Bot , vol.53 , pp. 1237-1242
    • Neill, S.J.1    Desikan, R.2    Clarke, A.3    Hurst, R.D.4    Hancock, J.T.5
  • 26
    • 0035983670 scopus 로고    scopus 로고
    • Heat stress and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis.
    • Panchuk II, Volkov RA, Schöffl F (2002) Heat stress and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis. Plant Physiol 129: 838-853
    • (2002) Plant Physiol , vol.129 , pp. 838-853
    • Panchuk, I.I.1    Volkov, R.A.2    Schöffl, F.3
  • 28
    • 0035983613 scopus 로고    scopus 로고
    • Common components, networks, and pathways of cross-tolerance to stress. The central role of 'redox' and abscisic acid-mediated controls.
    • Pastori GM, Foyer CH (2002) Common components, networks, and pathways of cross-tolerance to stress. The central role of 'redox' and abscisic acid-mediated controls. Plant Physiol 129: 460-468
    • (2002) Plant Physiol , vol.129 , pp. 460-468
    • Pastori, G.M.1    Foyer, C.H.2
  • 31
    • 0036293238 scopus 로고    scopus 로고
    • Changes in antioxidant activity in sub-cellular fractions of tolerant and susceptible wheat genotypes in response to long term salt stress.
    • Sairam RK, Srivastava GC (2002) Changes in antioxidant activity in sub-cellular fractions of tolerant and susceptible wheat genotypes in response to long term salt stress. Plant Sci 162: 897-904
    • (2002) Plant Sci , vol.162 , pp. 897-904
    • Sairam, R.K.1    Srivastava, G.C.2
  • 32
    • 0001857314 scopus 로고    scopus 로고
    • Catalase in plants: gene structure, properties, regulation, and expression.
    • In: Scandalios JG (ed) Cold Spring Harbor Laboratory Press, New York
    • Scandalios JG, Guan L, Polidoros AN (1997) Catalase in plants: gene structure, properties, regulation, and expression. In: Scandalios JG (ed) Oxidative Stress and the Molecular Biology of Antioxidant Defenses. Cold Spring Harbor Laboratory Press, New York, pp 343-406
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defenses. , pp. 343-406
    • Scandalios, J.G.1    Guan, L.2    Polidoros, A.N.3
  • 33
    • 0033771378 scopus 로고    scopus 로고
    • Antioxidative enzymes in wheat subjected to increasing water deficit and rewatering.
    • Sgherri CLM, Maffei M, Navari-lzzo F (2000) Antioxidative enzymes in wheat subjected to increasing water deficit and rewatering. J Plant Physiol 157: 273-279
    • (2000) J Plant Physiol , vol.157 , pp. 273-279
    • Sgherri, C.L.M.1    Maffei, M.2    Navari-lzzo, F.3
  • 35
    • 0021105282 scopus 로고
    • Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids.
    • Takahashi MA, Asada K (1983) Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch Biochem Biophys 226: 558-566
    • (1983) Arch Biochem Biophys , vol.226 , pp. 558-566
    • Takahashi, M.A.1    Asada, K.2
  • 36
    • 34548132846 scopus 로고    scopus 로고
    • Acclimation to heat and high light intensity during the development of oat leaves increases the NADH DH complex and PTOX levels in chloroplasts.
    • Tallón C, Quiles MJ (2007) Acclimation to heat and high light intensity during the development of oat leaves increases the NADH DH complex and PTOX levels in chloroplasts. Plant Sci 173: 438-445
    • (2007) Plant Sci , vol.173 , pp. 438-445
    • Tallón, C.1    Quiles, M.J.2
  • 37
    • 0030748530 scopus 로고    scopus 로고
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction.
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction. Plant J 11: 1187-1194
    • (1997) Plant J , vol.11 , pp. 1187-1194
    • Thordal-Christensen, H.1    Zhang, Z.2    Wei, Y.3    Collinge, D.B.4
  • 38
    • 0031403534 scopus 로고    scopus 로고
    • Overproduction of ascorbate peroxidase in the tobacco chloroplast does not provide protection against ozone.
    • Torsethaugen G, Pitcher LH, Zilinskas BA, Pell EJ (1997) Overproduction of ascorbate peroxidase in the tobacco chloroplast does not provide protection against ozone. Plant Physiol 114: 529-537
    • (1997) Plant Physiol , vol.114 , pp. 529-537
    • Torsethaugen, G.1    Pitcher, L.H.2    Zilinskas, B.A.3    Pell, E.J.4
  • 39
    • 0035200535 scopus 로고    scopus 로고
    • Effect of salt treatment and osmotic stress on V-ATPase and V-PPase in leaves of the halophyte Suaeda salsa.
    • Wang BS, Lüttge U, Ratajczak R (2001) Effect of salt treatment and osmotic stress on V-ATPase and V-PPase in leaves of the halophyte Suaeda salsa. J Exp Bot 52: 2355-2365
    • (2001) J Exp Bot , vol.52 , pp. 2355-2365
    • Wang, B.S.1    Lüttge, U.2    Ratajczak, R.3
  • 40
    • 0024707622 scopus 로고
    • Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis.
    • Werneke JM, Chatfield JM, Ogren WL (1989) Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis. Plant Cell 1: 815-825
    • (1989) Plant Cell , vol.1 , pp. 815-825
    • Werneke, J.M.1    Chatfield, J.M.2    Ogren, W.L.3
  • 41
    • 0036954219 scopus 로고    scopus 로고
    • Thylakoid membrane-bound ascorbate peroxidase is a limiting factor of antioxidative systems under photo-oxidative stress.
    • Yabuta Y, Motoki T, Yoshimura K, Takeda T, Ishikawa T, Shigeoka S (2002) Thylakoid membrane-bound ascorbate peroxidase is a limiting factor of antioxidative systems under photo-oxidative stress. Plant J 32: 915-925
    • (2002) Plant J , vol.32 , pp. 915-925
    • Yabuta, Y.1    Motoki, T.2    Yoshimura, K.3    Takeda, T.4    Ishikawa, T.5    Shigeoka, S.6
  • 42
    • 0033557879 scopus 로고    scopus 로고
    • Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves.
    • Yoshimura K, Yabuta Y, Tamoi M, Ishikawa T, Shigeoka S (1999) Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves. Biochem J 338: 41-48
    • (1999) Biochem J , vol.338 , pp. 41-48
    • Yoshimura, K.1    Yabuta, Y.2    Tamoi, M.3    Ishikawa, T.4    Shigeoka, S.5
  • 43
    • 0034033939 scopus 로고    scopus 로고
    • Expression of spinach ascorbate peroxidase isoenzymes in response to oxidative stresses.
    • Yoshimura K, Yabuta Y, Ishikawa T, Shigeoka S (2000) Expression of spinach ascorbate peroxidase isoenzymes in response to oxidative stresses. Plant Physiol 123: 223-234
    • (2000) Plant Physiol , vol.123 , pp. 223-234
    • Yoshimura, K.1    Yabuta, Y.2    Ishikawa, T.3    Shigeoka, S.4
  • 44
    • 10344224052 scopus 로고    scopus 로고
    • NaCl enhances thylakoid-bound SOD activity in the leaves of C3 halophyte Suaeda salsa L.
    • Zhang QF, Li YY, Pang CH, Lu CM, Wang BS (2005) NaCl enhances thylakoid-bound SOD activity in the leaves of C3 halophyte Suaeda salsa L. Plant Sci 168: 423-430
    • (2005) Plant Sci , vol.168 , pp. 423-430
    • Zhang, Q.F.1    Li, Y.Y.2    Pang, C.H.3    Lu, C.M.4    Wang, B.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.