메뉴 건너뛰기




Volumn 132, Issue 4, 2003, Pages 2116-2125

Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity

Author keywords

[No Author keywords available]

Indexed keywords

BIOMASS; CROPS; ELECTRON TRANSPORT PROPERTIES; ENZYME KINETICS; GENETIC ENGINEERING; MUTAGENESIS; PHOTOSYNTHESIS;

EID: 0043011573     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.103.021717     Document Type: Article
Times cited : (84)

References (39)
  • 1
    • 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
  • 2
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • CH Foyer, PM Mullineaux, eds. CRC Press, Boca Raton, FL
    • Asada K (1994) Production and action of active oxygen species in photosynthetic tissues. In CH Foyer, PM Mullineaux, eds, Causes of Photooxidative Stress and Amelioration of Defenses Systems in Plants CRC Press, Boca Raton, FL, pp 77-104
    • (1994) Causes of Photooxidative Stress and Amelioration of Defenses Systems in Plants , pp. 77-104
    • Asada, K.1
  • 3
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada K (1999) The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu Rev Plant Physiol Plant Mol Biol 50: 601-639
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 601-639
    • Asada, K.1
  • 4
    • 0000682385 scopus 로고
    • Production and scavenging of active oxygen in photosynthesis
    • DJ Kyle, CB Osmond, CJ Arntzen, eds. Elsevier, Amsterdam
    • Asada K, Takahashi M (1987) Production and scavenging of active oxygen in photosynthesis. In DJ Kyle, CB Osmond, CJ Arntzen, eds, Photoinhibition. Elsevier, Amsterdam, pp 227-287
    • (1987) Photoinhibition , pp. 227-287
    • Asada, K.1    Takahashi, M.2
  • 5
    • 0033033416 scopus 로고    scopus 로고
    • Drought and watering-dependent oxidative stress: Effect on antioxidant content in Triticum aestivum L. leaves
    • Bartoli CG, Simontacchi M, Tambussi E, Beltrano J, Montaldi E, Puntarulo S (1999) Drought and watering-dependent oxidative stress: effect on antioxidant content in Triticum aestivum L. leaves. J Exp Bot 50: 375-383
    • (1999) J Exp Bot , vol.50 , pp. 375-383
    • Bartoli, C.G.1    Simontacchi, M.2    Tambussi, E.3    Beltrano, J.4    Montaldi, E.5    Puntarulo, S.6
  • 6
    • 0030087896 scopus 로고    scopus 로고
    • Ascorbate peroxidase: A prominent membrane protein in oilseed glyoxysomes
    • Bunkelmann JR, Trelease RN (1996) Ascorbate peroxidase: a prominent membrane protein in oilseed glyoxysomes. Plant Physiol 110: 589-598
    • (1996) Plant Physiol , vol.110 , pp. 589-598
    • Bunkelmann, J.R.1    Trelease, R.N.2
  • 8
    • 0347296409 scopus 로고    scopus 로고
    • Cloning and mapping of genes involved in wheat-leaf rust interaction through gene-expression analysis using chromosome-deleted near-isogenic wheat lines
    • Danna CH, Sacco F, Ingala LR, Saione HA, Ugalde RA (2002) Cloning and mapping of genes involved in wheat-leaf rust interaction through gene-expression analysis using chromosome-deleted near-isogenic wheat lines. Theor Appl Genet 105: 972-979
    • (2002) Theor Appl Genet , vol.105 , pp. 972-979
    • Danna, C.H.1    Sacco, F.2    Ingala, L.R.3    Saione, H.A.4    Ugalde, R.A.5
  • 9
    • 0034075142 scopus 로고    scopus 로고
    • Ascorbate-dependent hydrogen peroxide detoxification and ascorbate regeneration during germination of a highly productive maize hybrid: Evidence of an improved detoxification mechanism against reactive oxygen species
    • De Gara L, Paciolla C, De Tullio MC, Motto M, Arrigoni O (2000) Ascorbate-dependent hydrogen peroxide detoxification and ascorbate regeneration during germination of a highly productive maize hybrid: evidence of an improved detoxification mechanism against reactive oxygen species. Physiol Plant 109: 7-13
    • (2000) Physiol Plant , vol.109 , pp. 7-13
    • De Gara, L.1    Paciolla, C.2    De Tullio, M.C.3    Motto, M.4    Arrigoni, O.5
  • 11
    • 0036066340 scopus 로고    scopus 로고
    • Photoinhibition and loss of photosystem II reaction center proteins during senescence of soybean leaves: Enhancement of photoinhibition by the "stay-green" mutation cytG
    • Guiamét JJ, Tyystjärvi E, Tyystjärvi T, John I, Kairavuo M, Pichersky E, Noodén LD (2002) Photoinhibition and loss of photosystem II reaction center proteins during senescence of soybean leaves: enhancement of photoinhibition by the "stay-green" mutation cytG. Physiol Plant 115: 468-478
    • (2002) Physiol Plant , vol.115 , pp. 468-478
    • Guiamét, J.J.1    Tyystjärvi, E.2    Tyystjärvi, T.3    John, I.4    Kairavuo, M.5    Pichersky, E.6    Noodén, L.D.7
  • 12
    • 0031467704 scopus 로고    scopus 로고
    • Alternative mRNA splicing of 3′-terminal exons generates ascorbate peroxidase isoenzymes in spinach (Spinacia oleracea) chloroplasts
    • Ishikawa T, Yoshimura K, Tamoi M, Takeda T, Shigeoka S (1997) Alternative mRNA splicing of 3′-terminal exons generates ascorbate peroxidase isoenzymes in spinach (Spinacia oleracea) chloroplasts. Biochem J 328: 795-800
    • (1997) Biochem J , vol.328 , pp. 795-800
    • Ishikawa, T.1    Yoshimura, K.2    Tamoi, M.3    Takeda, T.4    Shigeoka, S.5
  • 13
    • 0026687906 scopus 로고
    • Determination of ascorbic acid in elemental diet by high-performance liquid chromatography with electrochemical detection
    • Iwase H (1992) Determination of ascorbic acid in elemental diet by high-performance liquid chromatography with electrochemical detection. J Chromatogr 606: 277-280
    • (1992) J Chromatogr , vol.606 , pp. 277-280
    • Iwase, H.1
  • 14
    • 0033959934 scopus 로고    scopus 로고
    • Bundle sheath proteins are more sensitive to oxidative damage than those of the mesophyll in maize leaves exposed to paraquat or low temperatures
    • Kingston-Smith AH, Foyer CH (2000) Bundle sheath proteins are more sensitive to oxidative damage than those of the mesophyll in maize leaves exposed to paraquat or low temperatures. J Exp Bot 51: 123-130
    • (2000) J Exp Bot , vol.51 , pp. 123-130
    • Kingston-Smith, A.H.1    Foyer, C.H.2
  • 15
    • 0035795162 scopus 로고    scopus 로고
    • Chloroplastic ascorbate peroxidase is the primary target of methylviologen-induced photooxidative stress in spinach leaves: Its relevance to monodehydroascorbate radical detected with in vivo ESR
    • Mano J, Ohno C, Domae Y, Asada K (2001) Chloroplastic ascorbate peroxidase is the primary target of methylviologen-induced photooxidative stress in spinach leaves: its relevance to monodehydroascorbate radical detected with in vivo ESR. Biochim Biophys Acta 1504: 273-287
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 273-287
    • Mano, J.1    Ohno, C.2    Domae, Y.3    Asada, K.4
  • 16
    • 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
  • 17
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence: A practical guide
    • Maxwell K, Johnson GN (2000) Chlorophyll fluorescence: a practical guide. J Exp Bot 51: 659-668
    • (2000) J Exp Bot , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 18
    • 0032029095 scopus 로고    scopus 로고
    • Post-transcriptional suppression of cytosolic ascorbate peroxidase expression during pathogen-induced programmed cell death in tobacco
    • Mittler R, Feng X, Cohen M (1998) Post-transcriptional suppression of cytosolic ascorbate peroxidase expression during pathogen-induced programmed cell death in tobacco. Plant Cell 10: 461-473
    • (1998) Plant Cell , vol.10 , pp. 461-473
    • Mittler, R.1    Feng, X.2    Cohen, M.3
  • 19
    • 0026793997 scopus 로고
    • Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase
    • Mittler R, Zilinkas BA (1992) Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase. J Biol Chem 267: 21802-21807
    • (1992) J Biol Chem , vol.267 , pp. 21802-21807
    • Mittler, R.1    Zilinkas, B.A.2
  • 20
    • 0034089277 scopus 로고    scopus 로고
    • Evaluation of the defense system in chloroplast to oxidative stress caused by paraquat using transgenic tobacco plants expressing catalase from Escherichia coli
    • Miyagawa Y, Tamoi M, Shigeoka S (2000) Evaluation of the defense system in chloroplast to oxidative stress caused by paraquat using transgenic tobacco plants expressing catalase from Escherichia coli. Plant Cell Physiol 33: 311-320
    • (2000) Plant Cell Physiol , vol.33 , pp. 311-320
    • Miyagawa, Y.1    Tamoi, M.2    Shigeoka, S.3
  • 21
    • 77957181306 scopus 로고
    • Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radical in thylakoids
    • Miyake C, Asada K (1992) Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radical in thylakoids. Plant Cell Physiol 33: 541-553
    • (1992) Plant Cell Physiol , vol.33 , pp. 541-553
    • Miyake, C.1    Asada, K.2
  • 22
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate peroxidase in spinach chloroplasts
    • Nakano Y, Asada K (1981) Hydrogen peroxide is scavenged by ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol 22: 867-880
    • (1981) Plant Cell Physiol , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 23
    • 77957183372 scopus 로고
    • Purification of peroxidase in spinach chloroplasts: Its inactivation in ascorbate-depleted medium and re-activation by monoedhydroascorbate radical
    • Nakano Y, Asada K (1987) Purification of peroxidase in spinach chloroplasts: its inactivation in ascorbate-depleted medium and re-activation by monoedhydroascorbate radical. Plant Cell Physiol 28: 131-140
    • (1987) Plant Cell Physiol , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 24
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor G, Foyer CH (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49: 246-279
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 246-279
    • Noctor, G.1    Foyer, C.H.2
  • 25
    • 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 AS (2001) Protecting cotton photosynthesis during moderate chilling at high light intensity by increasing chloroplastic antioxidant enzyme activity. J Exp Bot 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
  • 26
    • 0036845048 scopus 로고    scopus 로고
    • Double antisense plants lacking ascorbate peroxidase and catalase are less sensitive to oxidative stress than single antisense plants lacking ascorbate peroxidase or catalase
    • Rizhsky L, Hallak-Herr E, Van Breusegem F, Rachmilevitch S, Barr JE, Rodermel S, Inzé D, Mittler R (2002) Double antisense plants lacking ascorbate peroxidase and catalase are less sensitive to oxidative stress than single antisense plants lacking ascorbate peroxidase or catalase. Plant J 32: 329-332
    • (2002) Plant J , vol.32 , pp. 329-332
    • Rizhsky, L.1    Hallak-Herr, E.2    Van Breusegem, F.3    Rachmilevitch, S.4    Barr, J.E.5    Rodermel, S.6    Inzé, D.7    Mittler, R.8
  • 28
    • 0344718457 scopus 로고    scopus 로고
    • Mapping of the leaf rust resistance gene Lr3 on the chromosome 6B of Sinvalocho MA wheat
    • Sacco F, Suárez EY, Naranjo T (1998) Mapping of the leaf rust resistance gene Lr3 on the chromosome 6B of Sinvalocho MA wheat. Genome 41: 686-690
    • (1998) Genome , vol.41 , pp. 686-690
    • Sacco, F.1    Suárez, E.Y.2    Naranjo, T.3
  • 29
    • 0028407352 scopus 로고
    • cDNA cloning of monodehydroascorbate radical reductase from cucumber: A high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes
    • Sano S, Asada K (1994) cDNA cloning of monodehydroascorbate radical reductase from cucumber: a high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes. Plant Cell Physiol 35: 425-437
    • (1994) Plant Cell Physiol , vol.35 , pp. 425-437
    • Sano, S.1    Asada, K.2
  • 30
    • 0029089221 scopus 로고
    • Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli
    • Sano S, Miyake C, Mikami B, Asada K (1995) Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli. J Biol Chem 270: 21354-21361
    • (1995) J Biol Chem , vol.270 , pp. 21354-21361
    • Sano, S.1    Miyake, C.2    Mikami, B.3    Asada, K.4
  • 31
    • 0031421317 scopus 로고    scopus 로고
    • The HAK1 gene of barley is a member of a large gene family and encodes a high-affinity potassium transport
    • Santa-María GE, Rubio F, Dubcovsky J, Rodríguez-Navarro A (1997) The HAK1 gene of barley is a member of a large gene family and encodes a high-affinity potassium transport. Plant Cell 9: 2281-2289
    • (1997) Plant Cell , vol.9 , pp. 2281-2289
    • Santa-María, G.E.1    Rubio, F.2    Dubcovsky, J.3    Rodríguez-Navarro, A.4
  • 32
    • 0027511499 scopus 로고
    • Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase
    • Sen Gupta A, Heinen JL, Holaday AS, Allen RD (1993a) Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc Natl Acad Sci USA 90: 1629-1633
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1629-1633
    • Sen Gupta, A.1    Heinen, J.L.2    Holaday, A.S.3    Allen, R.D.4
  • 33
    • 0027141553 scopus 로고
    • Overexpression of superoxide dismutase protects plants from oxidative stress
    • Sen Gupta A, Webb RP, Holaday AS, Allen RD (1993b) Overexpression of superoxide dismutase protects plants from oxidative stress. Plant Physiol 103: 1067-1073
    • (1993) Plant Physiol , vol.103 , pp. 1067-1073
    • Sen Gupta, A.1    Webb, R.P.2    Holaday, A.S.3    Allen, R.D.4
  • 34
    • 0032557638 scopus 로고    scopus 로고
    • Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts
    • Shikanai T, Takeda T, Yamauchi Y, Sano S, Tomizawa K, Yokota A, Shigeoka S (1998) Inhibition of ascorbate peroxidase under oxidative stress in tobacco having bacterial catalase in chloroplasts. FEBS Lett 428: 47-51
    • (1998) FEBS Lett , vol.428 , pp. 47-51
    • Shikanai, T.1    Takeda, T.2    Yamauchi, Y.3    Sano, S.4    Tomizawa, K.5    Yokota, A.6    Shigeoka, S.7
  • 35
    • 0035029939 scopus 로고    scopus 로고
    • Active oxygen produced during selective excitation of photosystem I is damaging not only to photosystem I, but also to photosystem II
    • Tjus SE, Scheller HV, Andersson B, Møller BL (2001) Active oxygen produced during selective excitation of photosystem I is damaging not only to photosystem I, but also to photosystem II. Plant Physiol 125: 2007-2015
    • (2001) Plant Physiol , vol.125 , pp. 2007-2015
    • Tjus, S.E.1    Scheller, H.V.2    Andersson, B.3    Møller, B.L.4
  • 37
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder KG (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struct Biol 2: 388-393
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 38
    • 0036954219 scopus 로고    scopus 로고
    • Thylakoid membrane-bound ascorbate peroxidase is a limiting factor of antioxidative systems trader 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 trader 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
  • 39
    • 0034033939 scopus 로고    scopus 로고
    • Expression of ascorbate peroxidase isoenzymes in response to oxidative stress
    • Yoshimura K, Yabuta Y, Ishikawa T, Shigeoka S (2000) Expression of ascorbate peroxidase isoenzymes in response to oxidative stress. Plant Physiol 123: 223-233
    • (2000) Plant Physiol , vol.123 , pp. 223-233
    • Yoshimura, K.1    Yabuta, Y.2    Ishikawa, T.3    Shigeoka, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.