Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli
We describe the construction and use of two sets of vectors for the over-expression and purification of protein from Escherichia coli. The set of pTEV plasmids (pTEV3, 4, 5) directs the synthesis of a recombinant protein with a N-terminal hexahistidine (His 6) tag that is removable by the tobacco et...
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| Veröffentlicht in: | Plasmid 2008-05, Vol.59 (3), p.231-237 |
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| creator | Rocco, C.J. Dennison, K.L. Klenchin, Vadim A. Rayment, I. Escalante-Semerena, J.C. |
| description | We describe the construction and use of two sets of vectors for the over-expression and purification of protein from
Escherichia coli. The set of pTEV plasmids (pTEV3, 4, 5) directs the synthesis of a recombinant protein with a N-terminal hexahistidine (His
6) tag that is removable by the tobacco etch virus (TEV) protease. The set of pKLD plasmids (pKLD66, 116) directs the synthesis of a recombinant protein that contains a N-terminal His
6 and maltose-binding protein tag in tandem, which can also be removed with TEV protease. The usefulness of these plasmids is illustrated by the rapid, high-yield purification of the 2-methylcitrate dehydratase (PrpD) protein of
Salmonella enterica, and the 2-methylaconitate isomerase (PrpF) protein of
Shewanella oneidensis, two enzymes involved in the catabolism of propionate to pyruvate via the 2-methylcitric acid cycle. |
| doi_str_mv | 10.1016/j.plasmid.2008.01.001 |
| format | Article |
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Escherichia coli. The set of pTEV plasmids (pTEV3, 4, 5) directs the synthesis of a recombinant protein with a N-terminal hexahistidine (His
6) tag that is removable by the tobacco etch virus (TEV) protease. The set of pKLD plasmids (pKLD66, 116) directs the synthesis of a recombinant protein that contains a N-terminal His
6 and maltose-binding protein tag in tandem, which can also be removed with TEV protease. The usefulness of these plasmids is illustrated by the rapid, high-yield purification of the 2-methylcitrate dehydratase (PrpD) protein of
Salmonella enterica, and the 2-methylaconitate isomerase (PrpF) protein of
Shewanella oneidensis, two enzymes involved in the catabolism of propionate to pyruvate via the 2-methylcitric acid cycle.</description><identifier>ISSN: 0147-619X</identifier><identifier>EISSN: 1095-9890</identifier><identifier>DOI: 10.1016/j.plasmid.2008.01.001</identifier><identifier>PMID: 18295882</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>2-Methylaconitate isomerase ; 2-Methylcitrate dehydratase ; 2-Methylcitric acid cycle enzymes ; Bacterial Proteins - chemistry ; Citrates - chemistry ; Cloning, Molecular ; Endopeptidases - metabolism ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Genetic Techniques ; Genetic Vectors ; Histidine - chemistry ; Hydro-Lyases - genetics ; Models, Genetic ; Oligopeptides - chemistry ; Plasmids - metabolism ; Propionate catabolism ; Rapid protein purification ; Recombinant Fusion Proteins - chemistry ; Recombinant Proteins - chemistry ; Salmonella enterica ; Salmonella enterica - enzymology ; Shewanella - metabolism ; Shewanella oneidensis ; TEV protease-cleavable tags ; Tobacco etch virus</subject><ispartof>Plasmid, 2008-05, Vol.59 (3), p.231-237</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c496t-3cc6132bfb03f0c0c3197ed4b7b73c9ca6bbaa3ed602e9b7592176c024abb4fc3</citedby><cites>FETCH-LOGICAL-c496t-3cc6132bfb03f0c0c3197ed4b7b73c9ca6bbaa3ed602e9b7592176c024abb4fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.plasmid.2008.01.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18295882$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rocco, C.J.</creatorcontrib><creatorcontrib>Dennison, K.L.</creatorcontrib><creatorcontrib>Klenchin, Vadim A.</creatorcontrib><creatorcontrib>Rayment, I.</creatorcontrib><creatorcontrib>Escalante-Semerena, J.C.</creatorcontrib><title>Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli</title><title>Plasmid</title><addtitle>Plasmid</addtitle><description>We describe the construction and use of two sets of vectors for the over-expression and purification of protein from
Escherichia coli. The set of pTEV plasmids (pTEV3, 4, 5) directs the synthesis of a recombinant protein with a N-terminal hexahistidine (His
6) tag that is removable by the tobacco etch virus (TEV) protease. The set of pKLD plasmids (pKLD66, 116) directs the synthesis of a recombinant protein that contains a N-terminal His
6 and maltose-binding protein tag in tandem, which can also be removed with TEV protease. The usefulness of these plasmids is illustrated by the rapid, high-yield purification of the 2-methylcitrate dehydratase (PrpD) protein of
Salmonella enterica, and the 2-methylaconitate isomerase (PrpF) protein of
Shewanella oneidensis, two enzymes involved in the catabolism of propionate to pyruvate via the 2-methylcitric acid cycle.</description><subject>2-Methylaconitate isomerase</subject><subject>2-Methylcitrate dehydratase</subject><subject>2-Methylcitric acid cycle enzymes</subject><subject>Bacterial Proteins - chemistry</subject><subject>Citrates - chemistry</subject><subject>Cloning, Molecular</subject><subject>Endopeptidases - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Genetic Techniques</subject><subject>Genetic Vectors</subject><subject>Histidine - chemistry</subject><subject>Hydro-Lyases - genetics</subject><subject>Models, Genetic</subject><subject>Oligopeptides - chemistry</subject><subject>Plasmids - metabolism</subject><subject>Propionate catabolism</subject><subject>Rapid protein purification</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Salmonella enterica</subject><subject>Salmonella enterica - enzymology</subject><subject>Shewanella - metabolism</subject><subject>Shewanella oneidensis</subject><subject>TEV protease-cleavable tags</subject><subject>Tobacco etch virus</subject><issn>0147-619X</issn><issn>1095-9890</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EotvCTwD5xC1h7CROfAGhVaFIlbiAxM2yJ5OuV4m9tZNF_HtSdsXHqScf5nnfsf0w9kpAKUCot_vyMNo8-b6UAF0JogQQT9hGgG4K3Wl4yjYg6rZQQn-_YJc57wFASaGeswvRSd10ndyw-20MeU4Lzj4GbkPPl0w8DjzQD45jDD7c8SPhHFPmQ0x83hFP9uB77nMc7e_YiifCODkfbJj5IcWZfFj5FCd-nXFHyePOW45x9C_Ys8GOmV6ezyv27eP11-1Ncfvl0-fth9sCa63mokJUopJucFANgICV0C31tWtdW6FGq5yztqJegSTt2kZL0SoEWVvn6gGrK_bu1HtY3EQ9UpiTHc0h-cmmnyZab_6fBL8zd_FoZNUp2cq14M25IMX7hfJsJp-RxtEGiks2LdRadtA-Cgrd1JXqmhVsTiCmmHOi4c9tBJgHq2ZvzlbNg1UDwqxW19zrf5_yN3XWuALvTwCtH3r0lExGTwGp96uY2fTRP7LiFwRzumw</recordid><startdate>20080501</startdate><enddate>20080501</enddate><creator>Rocco, C.J.</creator><creator>Dennison, K.L.</creator><creator>Klenchin, Vadim A.</creator><creator>Rayment, I.</creator><creator>Escalante-Semerena, J.C.</creator><general>Elsevier Inc</general><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>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080501</creationdate><title>Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli</title><author>Rocco, C.J. ; Dennison, K.L. ; Klenchin, Vadim A. ; Rayment, I. ; Escalante-Semerena, J.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c496t-3cc6132bfb03f0c0c3197ed4b7b73c9ca6bbaa3ed602e9b7592176c024abb4fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>2-Methylaconitate isomerase</topic><topic>2-Methylcitrate dehydratase</topic><topic>2-Methylcitric acid cycle enzymes</topic><topic>Bacterial Proteins - chemistry</topic><topic>Citrates - chemistry</topic><topic>Cloning, Molecular</topic><topic>Endopeptidases - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Genetic Techniques</topic><topic>Genetic Vectors</topic><topic>Histidine - chemistry</topic><topic>Hydro-Lyases - genetics</topic><topic>Models, Genetic</topic><topic>Oligopeptides - chemistry</topic><topic>Plasmids - metabolism</topic><topic>Propionate catabolism</topic><topic>Rapid protein purification</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Proteins - chemistry</topic><topic>Salmonella enterica</topic><topic>Salmonella enterica - enzymology</topic><topic>Shewanella - metabolism</topic><topic>Shewanella oneidensis</topic><topic>TEV protease-cleavable tags</topic><topic>Tobacco etch virus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rocco, C.J.</creatorcontrib><creatorcontrib>Dennison, K.L.</creatorcontrib><creatorcontrib>Klenchin, Vadim A.</creatorcontrib><creatorcontrib>Rayment, I.</creatorcontrib><creatorcontrib>Escalante-Semerena, J.C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plasmid</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rocco, C.J.</au><au>Dennison, K.L.</au><au>Klenchin, Vadim A.</au><au>Rayment, I.</au><au>Escalante-Semerena, J.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli</atitle><jtitle>Plasmid</jtitle><addtitle>Plasmid</addtitle><date>2008-05-01</date><risdate>2008</risdate><volume>59</volume><issue>3</issue><spage>231</spage><epage>237</epage><pages>231-237</pages><issn>0147-619X</issn><eissn>1095-9890</eissn><abstract>We describe the construction and use of two sets of vectors for the over-expression and purification of protein from
Escherichia coli. The set of pTEV plasmids (pTEV3, 4, 5) directs the synthesis of a recombinant protein with a N-terminal hexahistidine (His
6) tag that is removable by the tobacco etch virus (TEV) protease. The set of pKLD plasmids (pKLD66, 116) directs the synthesis of a recombinant protein that contains a N-terminal His
6 and maltose-binding protein tag in tandem, which can also be removed with TEV protease. The usefulness of these plasmids is illustrated by the rapid, high-yield purification of the 2-methylcitrate dehydratase (PrpD) protein of
Salmonella enterica, and the 2-methylaconitate isomerase (PrpF) protein of
Shewanella oneidensis, two enzymes involved in the catabolism of propionate to pyruvate via the 2-methylcitric acid cycle.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18295882</pmid><doi>10.1016/j.plasmid.2008.01.001</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 2-Methylaconitate isomerase 2-Methylcitrate dehydratase 2-Methylcitric acid cycle enzymes Bacterial Proteins - chemistry Citrates - chemistry Cloning, Molecular Endopeptidases - metabolism Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - genetics Genetic Techniques Genetic Vectors Histidine - chemistry Hydro-Lyases - genetics Models, Genetic Oligopeptides - chemistry Plasmids - metabolism Propionate catabolism Rapid protein purification Recombinant Fusion Proteins - chemistry Recombinant Proteins - chemistry Salmonella enterica Salmonella enterica - enzymology Shewanella - metabolism Shewanella oneidensis TEV protease-cleavable tags Tobacco etch virus |
| title | Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli |
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