Disulfide isomerase-like protein AtPDIL1-2 is a good candidate for trichlorophenol phytodetoxification
文献类型： 外文期刊
作者： Peng, Ri-He 1 ; Qiu, Jin 1 ; Tian, Yong-Sheng 1 ; Gao, Jian-jie 1 ; Han, Hong-juan 1 ; Fu, Xiao-Yan 1 ; Zhu, Bo 1 ; Xu, J 1 ;
作者机构： 1.Shanghai Acad Agr Sci, Agrobiotechnol Res Inst, 2901 Beidi Rd, Shanghai, Peoples R China; Shanghai Key Lab Agr Genet & Breeding, 2901 Beidi Rd, Shanghai, Peoples R China
期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）
ISSN： 2045-2322
年卷期： 2017 年 7 卷
页码：
收录情况： SCI
摘要： Trichlorophenol (TCP) is a widely used and persistent environmentally toxic compound that poses a carcinogenic risk to humans. Phytoremediation is a proficient cleanup technology for organic pollutants. In this study, we found that the disulfide isomerase-like protein AtPDIL1-2 in plants is a good candidate for enhancing 2,4,6-TCP phytoremediation. The expression of AtPDIL1-2 in Arabidopsis was induced by 2,4,6-TCP. The heterologously expressed AtPDIL1-2 in Escherichia coli exhibited both oxidase and isomerase activities as protein disulfide isomerase and improved bacteria tolerance to 2,4,6-TCP. Further research revealed that transgenic tobacco overexpressing AtPDIL1-2 was more tolerant to high concentrations of 2,4,6-TCP and removed the toxic compound at far greater rates than the control plants. To elucidate the mechanism of action of AtPDIL1-2, we investigated the chemical interaction of AtPDIL1-2 with 2,4,6-TCP for the first time. HPLC analysis implied that AtPDIL1-2 exerts a TCP-binding activity. A suitable configuration of AtPDIL1-2-TCP binding was obtained by molecular docking studies using the AutoDock program. It predicted that the TCP binding site is located in the b-b' domain of AtPDIL1-2 and that His254 of the protein is critical for the binding interaction. These findings imply that AtPDIL1-2 can be used for TCP detoxification by the way of overexpression in plants.
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