Cloning and characterization of a theta class glutathione transferase from the potato pathogen Phytophthora infestans

被引：11

作者：

Bryant, David ^{[1
]}

Cummins, Ian ^{[1
]}

Dixon, David P. ^{[1
]}

Edwards, Robert ^{[1
]}

机构：

[1] Univ Durham, Sch Biol & Biomed Sci, Crop Protect Grp, Durham DH1 3LE, England

来源：

PHYTOCHEMISTRY | 2006年 / 67卷 / 14期

基金：

英国生物技术与生命科学研究理事会;

关键词：

detoxification; glutathione peroxidase; oxylipin; phytoalexin; phytopathogenic fungi; Phytophthora infestans; potato; Solanum tuberosum;

D O I：

10.1016/j.phytochem.2006.05.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A glutathione transferase (GST) related to the theta (T) class of enzymes found in plants and animals has been cloned from the potato pathogen Phytophthora infestans. The cDNA encoded a 25 kDa polypeptide termed PiGSTT1 which was expressed in E coli as the native protein. The purified recombinant enzyme behaved as a dimer (PiGSTT1-1) and while being unable to catalyse the glutathione conjugation of 1-chloro-2,4-dintrobenzene, was highly active as a glutathione peroxidase with organic hydroperoxide substrates. In addition to reducing the synthetic substrate cumene hydroperoxide, PiGSTT1-1 was shown to be highly active toward 9(S)-hydroperoxy-(10E, 12Z, 15Z)-octadecatrienoic acid = 9(S)-HPOT, which is formed in potato plants during infection by P. infestans as a precursor of the antifungal oxylipin colnelenic acid. An antiserum was raised to PiGSTT1-1 and used to demonstrate that the respective enzyme was abundantly expressed in P. infestans both cultured on pea agar and during the infection of potato plants. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：1427 / 1434

页数：8

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