Action mechanism of the novel rice blast fungicide tolprocarb distinct from that of conventional melanin biosynthesis inhibitors

被引：22

作者：

Hamada, Takahiro ^{[1
]}

Asanagi, Mineko ^{[2
]}

Satozawa, Tomomi ^{[3
]}

Araki, Natsuko ^{[1
]}

Banba, Shinichi ^{[1
]}

Higashimura, Norikazu ^{[1
]}

Akase, Tomohisa ^{[1
]}

Hirase, Kangetsu ^{[1
]}

机构：

[1] Mitsui Chem Agro Inc, Agrochem Res Ctr, Mobara, Chiba 2970017, Japan

[2] Japan Sci & Technol Agcy, Dept Business Innovat Dev, Chiyoda Ku, Tokyo 1020076, Japan

[3] Mitsui Chem Inc, Purchasing Div, Minato Ku, Tokyo 1057117, Japan

来源：

JOURNAL OF PESTICIDE SCIENCE | 2014年 / 39卷 / 3-4期

关键词：

melanin biosynthesis inhibitors; polyketide synthase; tolprocarb; M; grisea; rice blast; APPRESSORIAL PENETRATION; VERTICILLIUM-DAHLIAE; ASPERGILLUS-ORYZAE; DEFICIENT; TETRACHLOROPHTHALIDE; TRICYCLAZOLE; PRECURSORS;

D O I：

10.1584/jpestics.D14-033

中图分类号：

Q96 [昆虫学];

学科分类号：

摘要：

The target site of tolprocarb, a novel systemic fungicide used for controlling rice blast, was investigated. Tolprocarb decolorized the mycelia of Magnaporthe grisea; the decolorization was reversed by adding scytalone or 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN). This result suggested that the target site of tolprocarb was polyketide synthase (PKS), which regulated polyketide synthesis and pentaketide cyclization in melanin biosynthesis. Further, we produced a transgenic Aspergillus oryzae, which possessed the PKS gene of M. grisea, and performed in vitro assays of PKS using membrane fractions from the transgenic A. oryzae. Compared with some conventional melanin biosynthesis inhibitors (cMBIs), tolprocarb only inhibited PKS activity in vitro. These results indicated that tolprocarb's target protein in M. grisea was PKS, which differentiates this fungicide from other cMBIs. Pesticide Science Society of Japan

引用

页码：152 / 158

页数：7

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