A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+
文献类型：期刊论文
| 作者 | Zhang, Weiwei1; Yin, Kun1,2; Li, Bowei1 ; Chen, Lingxin1
|
| 刊名 | JOURNAL OF HAZARDOUS MATERIALS
 |
| 出版日期 | 2013-10-15 |
| 卷号 | 261页码:646-652 |
| ISSN号 | 0304-3894 |
| 关键词 | Glutathione S-transferase Proteus mirabilis Heavy metal Surface display Adsorption |
| 通讯作者 | Chen, LX (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res, 17 Chunhui Rd, Yantai 264003, Peoples R China. lxchen@yic.ac.cn |
| 产权排序 | [Zhang, Weiwei; Yin, Kun; Li, Bowei; Chen, Lingxin] Chinese Acad Sci, Key Lab Coastal Zone Environm Proc & Ecol Remedia, Shandong Prov Key Lab Coastal Zone Environm Proc, Yantai Inst Coastal Zone Res YIC,YICCAS, Yantai 264003, Shandong, Peoples R China; [Yin, Kun] Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 中文摘要 | Glutathione S-transferases (GSTs) are a family of multifunctional proteins playing important roles in detoxification of harmful physiological and xenobiotic compounds in organisms. In our study, a gene encoding a GST from Proteus mirabilis strain V7, gst(Pm)-4, was cloned and conditionally expressed in Escherichia coli strain BL21(DE3). The purified Gst(Pm)-4 protein, with an estimated molecular mass of approximately 23 kDa, was able to conjugate 1-chloro-2,4-dinitrobenzene and bind to the GSH-affinity matrix. Real-time reverse transcriptase PCR suggested that mRNA level of gst(Pm)-4 was increased in the presence of CdCl2, CuCl2, HgCl2 and PbCl2, respectively. Correspondingly, overexpression of gst(Pm)-4 in the genetically engineered bacterium Top10/pLacpGst exhibited higher heavy metal resistance compared to the control Top10/pLacP3. Another genetically engineered bacterium Top10/pBATGst, in which the DNA encoding Gst(Pm)-4 protein was fused with the DNA encoding Pfa1-based auto surface display system, was built. Top10/pBATGst could constitutively express the chimeric Gst(Pm)-4 and anchor it onto the cell surface subsequently. Almost 100% of the Hg2+ within the range of 0.1-100 nM was adsorbed by Top10/pBATGst, and 80% of the bounded Hg2+ could be desorbed from bacterial cells when pH was adjusted to 6.0. Thus, Top10/pBATGst can be potentially used for efficient treatment of Hg2+-contaminated aquatic environment. (C) 2013 Elsevier B.V. All rights reserved. |
| 英文摘要 | Glutathione S-transferases (GSTs) are a family of multifunctional proteins playing important roles in detoxification of harmful physiological and xenobiotic compounds in organisms. In our study, a gene encoding a GST from Proteus mirabilis strain V7, gst(Pm)-4, was cloned and conditionally expressed in Escherichia coli strain BL21(DE3). The purified Gst(Pm)-4 protein, with an estimated molecular mass of approximately 23 kDa, was able to conjugate 1-chloro-2,4-dinitrobenzene and bind to the GSH-affinity matrix. Real-time reverse transcriptase PCR suggested that mRNA level of gst(Pm)-4 was increased in the presence of CdCl2, CuCl2, HgCl2 and PbCl2, respectively. Correspondingly, overexpression of gst(Pm)-4 in the genetically engineered bacterium Top10/pLacpGst exhibited higher heavy metal resistance compared to the control Top10/pLacP3. Another genetically engineered bacterium Top10/pBATGst, in which the DNA encoding Gst(Pm)-4 protein was fused with the DNA encoding Pfa1-based auto surface display system, was built. Top10/pBATGst could constitutively express the chimeric Gst(Pm)-4 and anchor it onto the cell surface subsequently. Almost 100% of the Hg2+ within the range of 0.1-100 nM was adsorbed by Top10/pBATGst, and 80% of the bounded Hg2+ could be desorbed from bacterial cells when pH was adjusted to 6.0. Thus, Top10/pBATGst can be potentially used for efficient treatment of Hg2+-contaminated aquatic environment. (C) 2013 Elsevier B.V. All rights reserved. |
| 学科主题 | Engineering, Environmental ; Engineering, Civil ; Environmental Sciences |
| 研究领域[WOS] | Engineering ; Environmental Sciences & Ecology |
| 关键词[WOS] | YEAST SACCHAROMYCES-CEREVISIAE ; TETRACHLOROHYDROQUINONE DEHALOGENASE ; MOLECULAR APPLICATION ; ESCHERICHIA-COLI ; MERCURY ; B1-1 ; STRAIN ; BACTERIA ; REGION ; PURIFICATION |
| 资助信息 | Chinese Academy of Sciences [KZCX2-EW-206]; National Natural Science Foundation of China (NSFC) [31200041] |
| 收录类别 | SCI |
| 原文出处 | http://dx.doi.org/10.1016/j.jhazmat.2013.08.023 |
| 语种 | 英语 |
| WOS记录号 | WOS:000328177300073 |
| 公开日期 | 2014-07-08 |
| 源URL | [http://ir.yic.ac.cn/handle/133337/6943]  |
| 专题 | 烟台海岸带研究所_中科院海岸带环境过程与生态修复重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Key Lab Coastal Zone Environm Proc & Ecol Remedia, Shandong Prov Key Lab Coastal Zone Environm Proc, Yantai Inst Coastal Zone Res YIC,YICCAS, Yantai 264003, Shandong, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Weiwei,Yin, Kun,Li, Bowei,et al. A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+[J]. JOURNAL OF HAZARDOUS MATERIALS,2013,261:646-652. |
| APA | Zhang, Weiwei,Yin, Kun,Li, Bowei,&Chen, Lingxin.(2013).A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+.JOURNAL OF HAZARDOUS MATERIALS,261,646-652. |
| MLA | Zhang, Weiwei,et al."A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+".JOURNAL OF HAZARDOUS MATERIALS 261(2013):646-652. |
入库方式： OAI收割
来源：烟台海岸带研究所
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