Peroxidases are involved in biosynthesis and biodegradation of β-thujaplicin in fungal elicitor-treated Cupressus lusitanica cell cultures

被引:20
作者
Zhao, J
Sakai, K [1 ]
机构
[1] Kyushu Univ, Fac Agr, Lab Forest Chem & Biochem, Fukuoka 8128581, Japan
[2] Chinese Acad Med Sci, Inst Mat Med, Beijing 100050, Peoples R China
[3] Peking Union Med Coll, Beijing 100050, Peoples R China
关键词
Cupressus lusitanica; H2O2; superoxide anion synthase; peroxidase; beta-thujaplicin; elicitor;
D O I
10.1046/j.1469-8137.2003.00841.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Here, collaboration between peroxidases and H2O2 in biosynthesis and biodegredation of beta-thujaplicin in elicited Cupressus lusitanica was investigated. The accumulation of a phytoalexin, beta-thujaplicin, in C. lusitanica cell cultures can be stimulated by a yeast elicitor. A transient low peak was followed by a high level lasting for 2 d, and then a decrease, while peroxidases were activated to a high level just when amounts of beta-thujaplicin decreased. In vitro tests revealed that horseradish peroxidase can transform c. 80% of beta-thujaplicin in the presence of H2O2, and the culture medium was also able to transform beta-thujaplicin. A transient production of H-2 O-2 occured in the cell cultures immediately after elicitation, following a increase in NAD(P)H-oxidase activity. This H2O2 production may mediate the elicitor-induced accumulation of beta-thujaplicin, because inhibiting H2O2 production or removing H2O2 from the cell cultures suppressed elicitor-induced beta-thujaplicin accumulation, while exogenously applied H2O2 or H2O2 generation system can stimulate beta-thujaplicin accumulation. Both NAD(P)H oxidase inhibitors and peroxidase inhibitors partially inhibited NAD(P)H-dependent O-2(-) and H2O2 production. In-gel assay of peroxidase and superoxide anion synthase activity demonstrated that peroxidase isoforms have NAD(P)H-dependent superoxide anion synthase activity. These results suggest that peroxidases can act as superoxide anion synthases to contribute to genecation of H2O2 that promotes beta-thujaplicin production in elicited C. lusitanica cell cultures.
引用
收藏
页码:719 / 731
页数:13
相关论文
共 37 条
  • [21] A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene encodes a plasma membrane protein with Ca2+ binding motifs
    Keller, T
    Damude, HG
    Werner, D
    Doerner, P
    Dixon, RA
    Lamb, C
    [J]. PLANT CELL, 1998, 10 (02) : 255 - 266
  • [22] DIFFERENCES IN PEROXIDASE-ACTIVITY AND ISOENZYMES IN EMBRYOGENIC AND NON-EMBRYOGENIC SHAMOUTI ORANGE OVULAR CALLUS LINES
    KOCHBA, J
    LAVEE, S
    SPIEGELROY, P
    [J]. PLANT AND CELL PHYSIOLOGY, 1977, 18 (02) : 463 - 467
  • [23] Retinitis pigmentosa caused by a homozygous mutation in the Stargardt disease gene ABCR
    Martínez-Mir, A
    Paloma, E
    Allikmets, R
    Ayuso, C
    del Río, T
    Dean, M
    Vilageliu, L
    Gonzàlez-Duarte, R
    Balcells, S
    [J]. NATURE GENETICS, 1998, 18 (01) : 11 - 12
  • [24] Involvement of an NAD(P)H oxidase in the elicitor-inducible oxidative burst of soybean
    Mithofer, A
    Daxberger, A
    FromholdTreu, D
    Ebel, J
    [J]. PHYTOCHEMISTRY, 1997, 45 (06) : 1101 - 1107
  • [25] Miyamoto D, 1998, BIOL PHARM BULL, V21, P1258, DOI 10.1248/bpb.21.1258
  • [26] RETHINKING AUXIN BIOSYNTHESIS AND METABOLISM
    NORMANLY, J
    SLOVIN, JP
    COHEN, JD
    [J]. PLANT PHYSIOLOGY, 1995, 107 (02) : 323 - 329
  • [27] OKABE T, 1989, FRAGRANCE J, V17, P74
  • [28] The generation of active oxygen species differs in tobacco and grapevine mesophyll protoplasts
    Papadakis, AK
    Roubelakis-Angelakis, KA
    [J]. PLANT PHYSIOLOGY, 1999, 121 (01) : 197 - 205
  • [29] A tomato peroxidase involved in the synthesis of lignin and suberin
    Quiroga, M
    Guerrero, C
    Botella, MA
    Barceló, A
    Amaya, I
    Medina, MI
    Alonso, FJ
    de Forchetti, SM
    Tigier, H
    Valpuesta, V
    [J]. PLANT PHYSIOLOGY, 2000, 122 (04) : 1119 - 1127
  • [30] Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val-Tyr-Lys as putative intermolecular cross-link site
    Schnabelrauch, LS
    Kieliszewski, M
    Upham, BL
    Alizedeh, H
    Lamport, DTA
    [J]. PLANT JOURNAL, 1996, 9 (04) : 477 - 489