Cd(II) and As(III) bioaccumulation by recombinant Escherichia coli expressing oligomeric human metallothioneins
Metallothioneins (MTs) are a family of metal binding proteins. Recombinant Escherichia coli expressing the human MT (hMT-1A) gene was constructed for bioaccumulation of heavy metals. In order to increase protein stability, the glutathione S-transferase (GST) gene was fused with the hMT-1A gene and c...
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| Veröffentlicht in: | Journal of hazardous materials 2011-01, Vol.185 (2), p.1605-1608 |
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| creator | Ma, Yao Lin, Jianqun Zhang, Chengjia Ren, Yilin Lin, Jianqiang |
| description | Metallothioneins (MTs) are a family of metal binding proteins. Recombinant
Escherichia coli expressing the human MT (hMT-1A) gene was constructed for bioaccumulation of heavy metals. In order to increase protein stability, the glutathione S-transferase (GST) gene was fused with the hMT-1A gene and coexpressed. In order to increase MT expression efficiency and metal binding capacity, two, three or four hMT-1A genes were integrated in series and overexpressed in
E. coli. The recombinant
E. coli expressing the GST fused trimeric hMT-1A protein exhibited the highest Cd(II) and As(III) bioaccumulation ability, 6.36
mg
Cd/g dry cells and 7.59
mg
As/g dry cells, respectively. |
| doi_str_mv | 10.1016/j.jhazmat.2010.10.051 |
| format | Article |
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Escherichia coli expressing the human MT (hMT-1A) gene was constructed for bioaccumulation of heavy metals. In order to increase protein stability, the glutathione S-transferase (GST) gene was fused with the hMT-1A gene and coexpressed. In order to increase MT expression efficiency and metal binding capacity, two, three or four hMT-1A genes were integrated in series and overexpressed in
E. coli. The recombinant
E. coli expressing the GST fused trimeric hMT-1A protein exhibited the highest Cd(II) and As(III) bioaccumulation ability, 6.36
mg
Cd/g dry cells and 7.59
mg
As/g dry cells, respectively.</description><identifier>ISSN: 0304-3894</identifier><identifier>EISSN: 1873-3336</identifier><identifier>DOI: 10.1016/j.jhazmat.2010.10.051</identifier><identifier>PMID: 21074318</identifier><identifier>CODEN: JHMAD9</identifier><language>eng</language><publisher>Kidlington: Elsevier B.V</publisher><subject>Applied sciences ; Arsenic ; Arsenic - metabolism ; Base Sequence ; Binding ; binding capacity ; binding proteins ; Bioaccumulation ; Biopolymers - genetics ; Biopolymers - metabolism ; Cadmium ; Cadmium - metabolism ; DNA Primers ; Dry cells ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Exact sciences and technology ; gene overexpression ; Genes ; glutathione transferase ; Heavy metal ; heavy metals ; Human ; Humans ; Metallothionein ; Metallothionein - genetics ; Metallothionein - metabolism ; Pollution ; Proteins ; Recombinant ; Recombination, Genetic ; Stability</subject><ispartof>Journal of hazardous materials, 2011-01, Vol.185 (2), p.1605-1608</ispartof><rights>2010 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-766b7575f664d3bdaddf9202efd034694791c93ff7918595e5b56287bebbe9763</citedby><cites>FETCH-LOGICAL-c549t-766b7575f664d3bdaddf9202efd034694791c93ff7918595e5b56287bebbe9763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jhazmat.2010.10.051$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23848991$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21074318$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ma, Yao</creatorcontrib><creatorcontrib>Lin, Jianqun</creatorcontrib><creatorcontrib>Zhang, Chengjia</creatorcontrib><creatorcontrib>Ren, Yilin</creatorcontrib><creatorcontrib>Lin, Jianqiang</creatorcontrib><title>Cd(II) and As(III) bioaccumulation by recombinant Escherichia coli expressing oligomeric human metallothioneins</title><title>Journal of hazardous materials</title><addtitle>J Hazard Mater</addtitle><description>Metallothioneins (MTs) are a family of metal binding proteins. Recombinant
Escherichia coli expressing the human MT (hMT-1A) gene was constructed for bioaccumulation of heavy metals. In order to increase protein stability, the glutathione S-transferase (GST) gene was fused with the hMT-1A gene and coexpressed. In order to increase MT expression efficiency and metal binding capacity, two, three or four hMT-1A genes were integrated in series and overexpressed in
E. coli. The recombinant
E. coli expressing the GST fused trimeric hMT-1A protein exhibited the highest Cd(II) and As(III) bioaccumulation ability, 6.36
mg
Cd/g dry cells and 7.59
mg
As/g dry cells, respectively.</description><subject>Applied sciences</subject><subject>Arsenic</subject><subject>Arsenic - metabolism</subject><subject>Base Sequence</subject><subject>Binding</subject><subject>binding capacity</subject><subject>binding proteins</subject><subject>Bioaccumulation</subject><subject>Biopolymers - genetics</subject><subject>Biopolymers - metabolism</subject><subject>Cadmium</subject><subject>Cadmium - metabolism</subject><subject>DNA Primers</subject><subject>Dry cells</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Exact sciences and technology</subject><subject>gene overexpression</subject><subject>Genes</subject><subject>glutathione transferase</subject><subject>Heavy metal</subject><subject>heavy metals</subject><subject>Human</subject><subject>Humans</subject><subject>Metallothionein</subject><subject>Metallothionein - genetics</subject><subject>Metallothionein - metabolism</subject><subject>Pollution</subject><subject>Proteins</subject><subject>Recombinant</subject><subject>Recombination, Genetic</subject><subject>Stability</subject><issn>0304-3894</issn><issn>1873-3336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkktv1DAURi0EokPhJwDeoJZFBjuO7XiFqlGBkSqxgK4tvzLxKLEHO6kov74OM8COrq4f537X0jEArzFaY4TZh_1636tfo5rWNfp9tkYUPwEr3HJSEULYU7BCBDUVaUVzBl7kvEcIYU6b5-Csxog3BLcrEDf2crt9D1Ww8CqXZVlrH5Ux8zgPavIxQH0PkzNx1D6oMMHrbHqXvOm9giYOHrqfh-Ry9mEHy3YXx-UW9vOoAhzdpIYhTn0Jcj7kl-BZp4bsXp3qObj9dP1986W6-fp5u7m6qQxtxFRxxjSnnHaMNZZoq6ztRI1q11lEGiYaLrARpOtKbamgjmrK6pZrp7UTnJFzcHHMPaT4Y3Z5kqPPxg2DCi7OWbaUcc4JR4-TNcYCs2bJvPwviTlHtWAEL6H0iJoUc06uk4fkR5XuJUZy8Sf38uRPLv6W4-Kv9L05jZj16Ozfrj_CCvDuBKhs1NAlFYzP_zjSNq0QS9DbI9epKNUuFeb2W5lEyx8QqEQV4uORcEXDnXdJZuNdMM76YnuSNvpHHvsAAdrEIg</recordid><startdate>20110130</startdate><enddate>20110130</enddate><creator>Ma, Yao</creator><creator>Lin, Jianqun</creator><creator>Zhang, Chengjia</creator><creator>Ren, Yilin</creator><creator>Lin, Jianqiang</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QQ</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>FR3</scope><scope>JG9</scope><scope>KR7</scope><scope>7X8</scope><scope>7QL</scope><scope>7U7</scope><scope>C1K</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20110130</creationdate><title>Cd(II) and As(III) bioaccumulation by recombinant Escherichia coli expressing oligomeric human metallothioneins</title><author>Ma, Yao ; Lin, Jianqun ; Zhang, Chengjia ; Ren, Yilin ; Lin, Jianqiang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-766b7575f664d3bdaddf9202efd034694791c93ff7918595e5b56287bebbe9763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Applied sciences</topic><topic>Arsenic</topic><topic>Arsenic - metabolism</topic><topic>Base Sequence</topic><topic>Binding</topic><topic>binding capacity</topic><topic>binding proteins</topic><topic>Bioaccumulation</topic><topic>Biopolymers - genetics</topic><topic>Biopolymers - metabolism</topic><topic>Cadmium</topic><topic>Cadmium - metabolism</topic><topic>DNA Primers</topic><topic>Dry cells</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Exact sciences and technology</topic><topic>gene overexpression</topic><topic>Genes</topic><topic>glutathione transferase</topic><topic>Heavy metal</topic><topic>heavy metals</topic><topic>Human</topic><topic>Humans</topic><topic>Metallothionein</topic><topic>Metallothionein - genetics</topic><topic>Metallothionein - metabolism</topic><topic>Pollution</topic><topic>Proteins</topic><topic>Recombinant</topic><topic>Recombination, Genetic</topic><topic>Stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ma, Yao</creatorcontrib><creatorcontrib>Lin, Jianqun</creatorcontrib><creatorcontrib>Zhang, Chengjia</creatorcontrib><creatorcontrib>Ren, Yilin</creatorcontrib><creatorcontrib>Lin, Jianqiang</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Ceramic Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Materials Research Database</collection><collection>Civil Engineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of hazardous materials</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ma, Yao</au><au>Lin, Jianqun</au><au>Zhang, Chengjia</au><au>Ren, Yilin</au><au>Lin, Jianqiang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cd(II) and As(III) bioaccumulation by recombinant Escherichia coli expressing oligomeric human metallothioneins</atitle><jtitle>Journal of hazardous materials</jtitle><addtitle>J Hazard Mater</addtitle><date>2011-01-30</date><risdate>2011</risdate><volume>185</volume><issue>2</issue><spage>1605</spage><epage>1608</epage><pages>1605-1608</pages><issn>0304-3894</issn><eissn>1873-3336</eissn><coden>JHMAD9</coden><abstract>Metallothioneins (MTs) are a family of metal binding proteins. Recombinant
Escherichia coli expressing the human MT (hMT-1A) gene was constructed for bioaccumulation of heavy metals. In order to increase protein stability, the glutathione S-transferase (GST) gene was fused with the hMT-1A gene and coexpressed. In order to increase MT expression efficiency and metal binding capacity, two, three or four hMT-1A genes were integrated in series and overexpressed in
E. coli. The recombinant
E. coli expressing the GST fused trimeric hMT-1A protein exhibited the highest Cd(II) and As(III) bioaccumulation ability, 6.36
mg
Cd/g dry cells and 7.59
mg
As/g dry cells, respectively.</abstract><cop>Kidlington</cop><pub>Elsevier B.V</pub><pmid>21074318</pmid><doi>10.1016/j.jhazmat.2010.10.051</doi><tpages>4</tpages></addata></record> |
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| subjects | Applied sciences Arsenic Arsenic - metabolism Base Sequence Binding binding capacity binding proteins Bioaccumulation Biopolymers - genetics Biopolymers - metabolism Cadmium Cadmium - metabolism DNA Primers Dry cells Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Exact sciences and technology gene overexpression Genes glutathione transferase Heavy metal heavy metals Human Humans Metallothionein Metallothionein - genetics Metallothionein - metabolism Pollution Proteins Recombinant Recombination, Genetic Stability |
| title | Cd(II) and As(III) bioaccumulation by recombinant Escherichia coli expressing oligomeric human metallothioneins |
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