메뉴 건너뛰기




Volumn 49, Issue 8, 2011, Pages 809-815

Enhanced activity of galactono-1,4-lactone dehydrogenase and ascorbate-glutathione cycle in mitochondria from complex III deficient Arabidopsis

Author keywords

Ascorbate; Ascorbate biosynthesis; Foyer Halliwell Asada cycle; Glutathione; Mitochondria; Respiratory chain

Indexed keywords

ANTIOXIDANT; ARABIDOPSIS PROTEIN; ASCORBATE PEROXIDASE; ASCORBIC ACID; DEHYDROASCORBIC ACID; GALACTONOLACTONE DEHYDROGENASE; GLUTATHIONE; GLUTATHIONE REDUCTASE; MONODEHYDROASCORBATE REDUCTASE; OXIDOREDUCTASE; PENTATRICOPEPTIDE REPEAT PROTEIN, ARABIDOPSIS; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 79960602600     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2011.04.013     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 2001, 52:561-591.
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 2
    • 33845667960 scopus 로고    scopus 로고
    • Reactive oxygen species generation and antioxidant systems in plant mitochondria
    • Navrot N., Rouhier N., Gelhaye E., Jacquot J.P. Reactive oxygen species generation and antioxidant systems in plant mitochondria. Physiol. Plant. 2007, 129:185-195.
    • (2007) Physiol. Plant. , vol.129 , pp. 185-195
    • Navrot, N.1    Rouhier, N.2    Gelhaye, E.3    Jacquot, J.P.4
  • 3
    • 77952055233 scopus 로고    scopus 로고
    • Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems
    • Blokhina O., Fagerstedt K.V. Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems. Physiol. Plant. 2010, 138:447-462.
    • (2010) Physiol. Plant. , vol.138 , pp. 447-462
    • Blokhina, O.1    Fagerstedt, K.V.2
  • 4
    • 0034126442 scopus 로고    scopus 로고
    • Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV
    • Bartoli C.G., Pastori G.M., Foyer C.H. Ascorbate biosynthesis in mitochondria is linked to the electron transport chain between complexes III and IV. Plant Physiol. 2000, 123:335-344.
    • (2000) Plant Physiol. , vol.123 , pp. 335-344
    • Bartoli, C.G.1    Pastori, G.M.2    Foyer, C.H.3
  • 6
  • 7
    • 0023651311 scopus 로고
    • In vitro oxidation of ascorbic acid and its prevention by GSH
    • Winkler B.S. In vitro oxidation of ascorbic acid and its prevention by GSH. Biochim. Biophys. Acta 1987, 925:258-264.
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 258-264
    • Winkler, B.S.1
  • 8
    • 0003121376 scopus 로고
    • The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism
    • Foyer C.H., Halliwell B. The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta 1976, 133:21-25.
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 10
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jimenez A., Hernandez J.A., Del Rio L.A., Sevilla F. Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 1997, 114:275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jimenez, A.1    Hernandez, J.A.2    Del Rio, L.A.3    Sevilla, F.4
  • 11
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew O., Whelan J., Millar A.H. Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 2003, 278:46869-46877.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 12
    • 34547135690 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins and their emerging roles in plants
    • Saha D., Prasad A.M., Srinivasan R. Pentatricopeptide repeat proteins and their emerging roles in plants. Plant Physiol. Biochem. 2007, 45:521-534.
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 521-534
    • Saha, D.1    Prasad, A.M.2    Srinivasan, R.3
  • 15
    • 77952898429 scopus 로고    scopus 로고
    • Increased vitamin C content accompanied by an enhanced recycling pathway confers oxidative stress tolerance in Arabidopsis
    • Wang Z., Xiao Y., Chen W., Tang K., Zhang L. Increased vitamin C content accompanied by an enhanced recycling pathway confers oxidative stress tolerance in Arabidopsis. J. Integr. Plant Biol. 2010, 52:400-409.
    • (2010) J. Integr. Plant Biol. , vol.52 , pp. 400-409
    • Wang, Z.1    Xiao, Y.2    Chen, W.3    Tang, K.4    Zhang, L.5
  • 16
    • 1942469563 scopus 로고    scopus 로고
    • Dehydroascorbate influences the plant cell cycle through a glutathione-independent reduction mechanism
    • Potters G., Horemans N., Bellone S., Caubergs R.J., Trost P., Guisez Y., Asard H. Dehydroascorbate influences the plant cell cycle through a glutathione-independent reduction mechanism. Plant Physiol. 2004, 134:1479-1487.
    • (2004) Plant Physiol. , vol.134 , pp. 1479-1487
    • Potters, G.1    Horemans, N.2    Bellone, S.3    Caubergs, R.J.4    Trost, P.5    Guisez, Y.6    Asard, H.7
  • 17
    • 77955657974 scopus 로고    scopus 로고
    • Life-cycle chronic gamma exposure of Arabidopsis thaliana induces growth effects but no discernable effects on oxidative stress pathways
    • Vandenhove H., Vanhoudt N., Cuypers A., van Hees M., Wannijn J., Horemans N. Life-cycle chronic gamma exposure of Arabidopsis thaliana induces growth effects but no discernable effects on oxidative stress pathways. Plant Physiol. Biochem. 2010, 48:778-786.
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 778-786
    • Vandenhove, H.1    Vanhoudt, N.2    Cuypers, A.3    van Hees, M.4    Wannijn, J.5    Horemans, N.6
  • 19
    • 78650418297 scopus 로고    scopus 로고
    • Ascorbate-glutathione cycle of mitochondria in osmoprimed soybean cotyledons in response to imbibitional chilling injury
    • Sun H., Li L., Wang X., Wu S., Wang X. Ascorbate-glutathione cycle of mitochondria in osmoprimed soybean cotyledons in response to imbibitional chilling injury. J. Plant Physiol. 2011, 168:226-232.
    • (2011) J. Plant Physiol. , vol.168 , pp. 226-232
    • Sun, H.1    Li, L.2    Wang, X.3    Wu, S.4    Wang, X.5
  • 22
    • 17644419591 scopus 로고    scopus 로고
    • Alterations in tocopherol cyclase activity in transgenic and mutant plants of Arabidopsis affect tocopherol content, tocopherol composition, and oxidative stress
    • Kanwischer M., Porfirova S., Bergmüller E., Dörmann P. Alterations in tocopherol cyclase activity in transgenic and mutant plants of Arabidopsis affect tocopherol content, tocopherol composition, and oxidative stress. Plant Physiol. 2005, 137:713-723.
    • (2005) Plant Physiol. , vol.137 , pp. 713-723
    • Kanwischer, M.1    Porfirova, S.2    Bergmüller, E.3    Dörmann, P.4
  • 23
    • 84989046140 scopus 로고
    • The antioxidant effects of thylakoid vitamin E (α-tocopherol)
    • Fryer M.J. The antioxidant effects of thylakoid vitamin E (α-tocopherol). Plant Cell Environ. 1992, 15:381-392.
    • (1992) Plant Cell Environ. , vol.15 , pp. 381-392
    • Fryer, M.J.1
  • 24
    • 0038705126 scopus 로고    scopus 로고
    • Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation
    • Dutilleul C., Garmier M., Noctor G., Mathieu C., Chétrit P., Foyer C.H., de Paepe R. Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation. Plant Cell 2003, 15:1212-1226.
    • (2003) Plant Cell , vol.15 , pp. 1212-1226
    • Dutilleul, C.1    Garmier, M.2    Noctor, G.3    Mathieu, C.4    Chétrit, P.5    Foyer, C.H.6    de Paepe, R.7
  • 25
    • 0035983840 scopus 로고    scopus 로고
    • A mitochondrial complex I defect impairs cold-regulated nuclear gene expression
    • Lee B.H., Lee H., Xiong L., Zhu J.K. A mitochondrial complex I defect impairs cold-regulated nuclear gene expression. Plant Cell 2002, 14:1235-1251.
    • (2002) Plant Cell , vol.14 , pp. 1235-1251
    • Lee, B.H.1    Lee, H.2    Xiong, L.3    Zhu, J.K.4
  • 26
    • 0033748333 scopus 로고    scopus 로고
    • Complex I impairment, respiratory compensations, and photosynthetic decrease in nuclear and mitochondrial male sterile mutants of Nicotiana sylvestris
    • Sabar M., De Paepe R., de Kouchkovsky Y. Complex I impairment, respiratory compensations, and photosynthetic decrease in nuclear and mitochondrial male sterile mutants of Nicotiana sylvestris. Plant Physiol. 2000, 124:1239-1250.
    • (2000) Plant Physiol. , vol.124 , pp. 1239-1250
    • Sabar, M.1    De Paepe, R.2    de Kouchkovsky, Y.3
  • 27
    • 0347264745 scopus 로고    scopus 로고
    • Functional mitochondrial complex I is required by tobacco leaves for optimal photosynthetic performance in photorespiratory conditions and during transients
    • Dutilleul C., Driscoll S., Cornic G., De Paepe R., Foyer C.H., Noctor G. Functional mitochondrial complex I is required by tobacco leaves for optimal photosynthetic performance in photorespiratory conditions and during transients. Plant Physiol. 2003, 131:264-275.
    • (2003) Plant Physiol. , vol.131 , pp. 264-275
    • Dutilleul, C.1    Driscoll, S.2    Cornic, G.3    De Paepe, R.4    Foyer, C.H.5    Noctor, G.6
  • 28
    • 0035631635 scopus 로고    scopus 로고
    • An easy and reliable method for establishment and maintenance of leaf and root cell cultures of Arabidopsis thaliana
    • Encina C.L., Constantin M., Botella J. An easy and reliable method for establishment and maintenance of leaf and root cell cultures of Arabidopsis thaliana. Plant Mol. Biol. Rep. 2001, 19:245-248.
    • (2001) Plant Mol. Biol. Rep. , vol.19 , pp. 245-248
    • Encina, C.L.1    Constantin, M.2    Botella, J.3
  • 29
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM201
    • Werhahn W., Niemeyer A., Jänsch L., Kruft V., Schmitz U.K., Braun H.P. Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM201. Plant Physiol. 2001, 125:943-954.
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.P.6
  • 30
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft V., Eubel H., Jänsch L., Werhahn W., Braun H.P. Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 2001, 127:1694-1710.
    • (2001) Plant Physiol. , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jänsch, L.3    Werhahn, W.4    Braun, H.P.5
  • 31
    • 0024199997 scopus 로고
    • Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid)
    • Smith I.K., Vierheller T.L., Thorne C.A. Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid). Anal. Biochem. 1988, 175:408-413.
    • (1988) Anal. Biochem. , vol.175 , pp. 408-413
    • Smith, I.K.1    Vierheller, T.L.2    Thorne, C.A.3
  • 32
    • 0020626279 scopus 로고
    • A spectrophotometric assay for dehydroascorbate reductase
    • Stahl R.L., Liebes L.F., Farber C.M., Silber R. A spectrophotometric assay for dehydroascorbate reductase. Anal. Biochem. 1983, 131:341-344.
    • (1983) Anal. Biochem. , vol.131 , pp. 341-344
    • Stahl, R.L.1    Liebes, L.F.2    Farber, C.M.3    Silber, R.4
  • 33
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano Y., Asada K. Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol. 1981, 22:867-880.
    • (1981) Plant Cell Physiol. , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 34
    • 0028035982 scopus 로고
    • L-Galactono-γ-lactone dehydrogenase: partial characterization, induction of activity and role in the synthesis of ascorbic acid in wounded white potato tuber tissue
    • Ôba K., Fukui M., Imai Y., Iriyama S., Nogami K. l-Galactono-γ-lactone dehydrogenase: partial characterization, induction of activity and role in the synthesis of ascorbic acid in wounded white potato tuber tissue. Plant Cell Physiol. 1994, 35:473-478.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 473-478
    • Ôba, K.1    Fukui, M.2    Imai, Y.3    Iriyama, S.4    Nogami, K.5
  • 37
    • 0033751099 scopus 로고    scopus 로고
    • Potentiation of pathogen-specific defense mechanisms in Arabidopsis by β aminobutyric acid
    • Zimmerli L., Jakab G., Métraux J.P., Mauch-Mani B. Potentiation of pathogen-specific defense mechanisms in Arabidopsis by β aminobutyric acid. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:12920-12925.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12920-12925
    • Zimmerli, L.1    Jakab, G.2    Métraux, J.P.3    Mauch-Mani, B.4
  • 38
    • 32644481938 scopus 로고    scopus 로고
    • Genome-wide identification and testing of superior reference genes for transcript normalisation in Arabidopsis
    • Czechowski T., Stitt M., Altmann T., Udvardi M.K., Scheible W.R. Genome-wide identification and testing of superior reference genes for transcript normalisation in Arabidopsis. Plant Physiol. 2005, 139:5-17.
    • (2005) Plant Physiol. , vol.139 , pp. 5-17
    • Czechowski, T.1    Stitt, M.2    Altmann, T.3    Udvardi, M.K.4    Scheible, W.R.5
  • 39
    • 0028007003 scopus 로고
    • Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3 α-hydroxysteroid dehydrogenase
    • Del Bello B., Maellaro E., Sugherini L., Santucci A., Comporti M., Casini A.F. Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3 α-hydroxysteroid dehydrogenase. Biochem. J. 1994, 304:385-390.
    • (1994) Biochem. J. , vol.304 , pp. 385-390
    • Del Bello, B.1    Maellaro, E.2    Sugherini, L.3    Santucci, A.4    Comporti, M.5    Casini, A.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.