Defense mechanism of the rice plant against rice blast disease

Kato, Tadahiro; Yamaguchi, Yoshihiro; Uyehara, Tadao; Yokoyama, Toshiro; Namai, Tsuneo; Yamanaka, Susumu

doi:10.1007/bf01047565

Cited by 58 publications

(32 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Epoxy, monohydroxy, dihydroxy, epoxy-hydroxy, and trihydroxy derivatives of linoleic and a-linolenic acids have been implicated as defensive substances in plants against attack by pathogens (Kato et al, 1983;Masui et al, 1989;Namai et al, 1993). Although a number of these oxylipins, such as fatty acid epoxides and certain hydroxy acids, can be formed by Cyt P450-catalyzed monooxygenation (Croteau and Kolattukudy, 1975;Salaiin et al, 1993), it appears that a pathway involving lipoxygenase and peroxygenase is the most important one for production of plant defensive substances.…”

Section: Discussionmentioning

confidence: 99%

Peroxygenase-Catalyzed Fatty Acid Epoxidation in Cereal Seeds (Sequential Oxidation of Linoleic Acid into 9(S),12(S),13(S)-Trihydroxy-10(E)-Octadecenoic Acid)

Hámberg

Hamberg

1996

Plant Physiol.

View full text Add to dashboard Cite

Peroxygenase-catalyzed epoxidation of oleic acid in preparations of cereal seeds was investigated. The 105,OOOg particle fraction of oat (Avena safiva) seed homogenate showed high peroxygenase activity, i.e. 3034 2 288 and 2441 f 168 nmol (10 min)-' mg-' protein in two cultivars, whereas the corresponding fraction obtained from barley (Hordeum vulgare and Hordeum distichum), rye (Secale cereale), and wheat (Trificum aesfivum) showed only weak activity, i.e. dihydroxy-9(Z)-octadecenoic acid, and 12(R),13(S)-epoxy-9(S)-hy-droxy-1 O(€)-octadecenoic acid. lncubation of linoleic acid with the 105,OOOg particle fraction gave a similar, but not identical, pattern of metabolites. Conversion of linoleic acid into 9(S),12(S),13(S)-trihydroxy-1 O(€)-octadecenoic acid, a naturally occurring oxylipin with antifungal properties, took place by a pathway involving sequential catalysis by lipoxygenase, peroxygenase, and epoxide hydrolase.Formation of hydroxyoctadecadienoic acids and epoxyhydroxyoctadecenoic acids upon incubation of linoleic acid with wheat (Triticum aestivum) flour-water suspensions was described by Graveland (1970). In the same year, the presence of a "lipoperoxidase" activity in oat (Avena sntiva) seed was postulated to explain reduction of linoleic acid 9-and 13-hydroperoxides (9-HPOD and 13-HPOD) into the corresponding alcohols (9-and 13-HOD) (Heimann and Schreier, 1970). In a further study, oat seed was reported to '

show abstract

Section: Discussionmentioning

confidence: 99%

Peroxygenase-Catalyzed Fatty Acid Epoxidation in Cereal Seeds (Sequential Oxidation of Linoleic Acid into 9(S),12(S),13(S)-Trihydroxy-10(E)-Octadecenoic Acid)

Hámberg

Hamberg

1996

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…However, these enzymes are believed to play central roles in the biosynthesis of essential cuticular components (Bl~e and Schuber, 1993;Croteau and Kolattukudy, 1975;Hamberg and Fahlstadius;1992, Kolattukudy, 1980Pinot et aL, 1992) and a variety of antifungal compounds (Kato et al, 1983(Kato et al, , 1985Masui etaL, 1989) in plants.…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of soluble epoxide hydrolase from potato

et al. 1994

View full text Add to dashboard Cite

SummaryFive cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used dlagnostic substrata for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.

show abstract

“…Thirdly, oxidized forms of linoleic acid and linolenic acid produced in rice infected with Pyricularia oryzae (i.e. M. grisea) and tomato plants infected with Phytophthora infestans display fungitoxic activities (Kato et a/., 1983;Verninghi et a/., 1985).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of elicitor‐induced lipoxygenase in tobacco cells

et al. 1993

View full text Add to dashboard Cite

SummaryLipoxygenase activity was induced in a tobacco cell suspension culture by treatment with glycopeptide elicitors prepared from the cell walls of Phytophthora parasitica var, nicotianae, and in tobacco seedlings infected by this fungal pathogen. Upon purification and characterization, the enzyme appeared to have a molecular weight of 96000, a pl of 5.1 and a Km of 20.9 μM with linoleic acid as substrate. According to its acidic optimum pH, it belongs to type‐2 lipoxygenases. Using linoleic, linolenic and arachidonic acids as substrates, the products formed in vitro by lipoxygenase were characterized. 9‐ and 5‐hydroperoxides were the main products obtained from the C18 and C20 fatty acids, respectively, thereby indicating that a 5‐lipoxygenase accounts for most of the elicitor‐induced activity, since the main site of insertion of molecular oxygen is on C‐5 of arachidonic acid. Small amounts of 13‐hydroperoxides were also formed from the C18 fatty acids. In vitro, the strongest inhibitors of tobacco lipoxygenase were n‐propylgallate and nordihydroguaiaretic acid. The possible involvement of this enzyme in signaling phenomena leading to defense induction in plants via jasmonic acid and other fatty acid‐derived products is discussed.

show abstract

Defense mechanism of the rice plant against rice blast disease

Cited by 58 publications

References 3 publications

Peroxygenase-Catalyzed Fatty Acid Epoxidation in Cereal Seeds (Sequential Oxidation of Linoleic Acid into 9(S),12(S),13(S)-Trihydroxy-10(E)-Octadecenoic Acid)

Peroxygenase-Catalyzed Fatty Acid Epoxidation in Cereal Seeds (Sequential Oxidation of Linoleic Acid into 9(S),12(S),13(S)-Trihydroxy-10(E)-Octadecenoic Acid)

Cloning and expression of soluble epoxide hydrolase from potato

Purification and characterization of elicitor‐induced lipoxygenase in tobacco cells

Contact Info

Product

Resources

About