A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+
Zhang, Weiwei1; Yin, Kun1,2; Li, Bowei1; Chen, Lingxin1
发表期刊JOURNAL OF HAZARDOUS MATERIALS
ISSN0304-3894
2013-10-15
卷号261页码:646-652
关键词Glutathione S-transferase Proteus Mirabilis Heavy Metal Surface Display Adsorption
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
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
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.; 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.
文章类型Article
资助机构Chinese Academy of Sciences [KZCX2-EW-206]; National Natural Science Foundation of China (NSFC) [31200041]
收录类别SCI
语种英语
关键词[WOS]YEAST SACCHAROMYCES-CEREVISIAE ; TETRACHLOROHYDROQUINONE DEHALOGENASE ; MOLECULAR APPLICATION ; ESCHERICHIA-COLI ; MERCURY ; B1-1 ; STRAIN ; BACTERIA ; REGION ; PURIFICATION
研究领域[WOS]Engineering ; Environmental Sciences & Ecology
WOS记录号WOS:000328177300073
引用统计
被引频次:44[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.yic.ac.cn/handle/133337/6943
专题中国科学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.
条目包含的文件 下载所有文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
A glutathione S-tran(1357KB) 开放获取CC BY-NC-SA浏览 下载
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Zhang, Weiwei]的文章
[Yin, Kun]的文章
[Li, Bowei]的文章
百度学术
百度学术中相似的文章
[Zhang, Weiwei]的文章
[Yin, Kun]的文章
[Li, Bowei]的文章
必应学术
必应学术中相似的文章
[Zhang, Weiwei]的文章
[Yin, Kun]的文章
[Li, Bowei]的文章
相关权益政策
暂无数据
收藏/分享
文件名: A glutathione S-transferase from Proteus mirabilis involved in heavy metal Hg2+.pdf
格式: Adobe PDF
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。