Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase
We have developed a system for expressing human interleukin 6 into the periplasmic space of Escherichia coli. The method is based on the expression of the hIL6 gene under the control of the regulatory signals of plasmid pINIII-OMPA3, i.e., lpp-lac promoter and the E. coli OMPA ribosome binding site...
Gespeichert in:
| Veröffentlicht in: | Journal of biotechnology 1993, Vol.27 (3), p.307-316 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 316 |
|---|---|
| container_issue | 3 |
| container_start_page | 307 |
| container_title | Journal of biotechnology |
| container_volume | 27 |
| creator | Barthelemy, I. González de Buitrago, G. Carreiro, C. Roncal, F. Pérez-Aranda, A. Márquez, G. Barbero, J.L. |
| description | We have developed a system for expressing human interleukin 6 into the periplasmic space of
Escherichia coli. The method is based on the expression of the hIL6 gene under the control of the regulatory signals of plasmid pINIII-OMPA3, i.e., lpp-lac promoter and the
E. coli OMPA ribosome binding site and leader sequence. Since microheterogeneity is known to occur in the amino end of the cytokine, we tested different ‘natural’ versions of the protein, and we found that the secretion process was only efficient when the N-terminal amino acid was not proline. In flask experiments this procedure yields about 8–10 mg of biologically active hIL6 per liter. |
| doi_str_mv | 10.1016/0168-1656(93)90093-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16540659</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0168165693900933</els_id><sourcerecordid>16540659</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4143-e7a6a062339b9a758f7586fd753dcba65508268603f10a7b8a122aec53e2ae163</originalsourceid><addsrcrecordid>eNp9kcGO1DAMhiO0aBkW3gCkHFYIDl2Spk1bDkhoNcBKI-AA58hN3Z1Am3bjdqR9Jl6StDOaIwfLsvz5t-WfsVdS3Egh9fsYZSJ1rt9W6l0lRKUS9YRtZFmoJCu1umCbM_KMPSf6LYTIqlxessui0CrT1Yb9_RGGZraTGzwH33BCG3Cthpbv5x48d37C0OH8x3mul2rg0x75iMGNHVC_kFuy-1jbvQNuh8594Ni2zjr0Ex_DYJHI-fuF_JZEtd556PgBggM_0brqbqd5_bgqb29WDU7ufsFGHCfXAOEL9rSFjvDlKV-xX5-3P2-_JrvvX-5uP-0Sm8lMJViABqFTpaq6giIv2xi6bYpcNbYGneeiTHWphWqlgKIuQaYpoM0VxiS1umJvjrrx8ocZaTK9I4tdBx6HmUx8aCZ0XkUwO4I2DEQBWzMG10N4NFKYxSOzGLDw2lTKrB4ZFcden_TnusfmPHQyJfavT30gC10bwFtHZywiMpVpxD4eMYy_ODgMhpaHW2xcQDuZZnD_v-MfSu2u2w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16540659</pqid></control><display><type>article</type><title>Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Barthelemy, I. ; González de Buitrago, G. ; Carreiro, C. ; Roncal, F. ; Pérez-Aranda, A. ; Márquez, G. ; Barbero, J.L.</creator><creatorcontrib>Barthelemy, I. ; González de Buitrago, G. ; Carreiro, C. ; Roncal, F. ; Pérez-Aranda, A. ; Márquez, G. ; Barbero, J.L.</creatorcontrib><description>We have developed a system for expressing human interleukin 6 into the periplasmic space of
Escherichia coli. The method is based on the expression of the hIL6 gene under the control of the regulatory signals of plasmid pINIII-OMPA3, i.e., lpp-lac promoter and the
E. coli OMPA ribosome binding site and leader sequence. Since microheterogeneity is known to occur in the amino end of the cytokine, we tested different ‘natural’ versions of the protein, and we found that the secretion process was only efficient when the N-terminal amino acid was not proline. In flask experiments this procedure yields about 8–10 mg of biologically active hIL6 per liter.</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/0168-1656(93)90093-3</identifier><identifier>PMID: 7763469</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Antineoplastic drugs. Cytokines ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Cloning, Molecular - methods ; DNA - genetics ; DNA - isolation & purification ; Endopeptidases - metabolism ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Genetic Variation ; Health. Pharmaceutical industry ; Humans ; IL6 signal peptide ; Industrial applications and implications. Economical aspects ; Interleukin-6 - biosynthesis ; Interleukin-6 - genetics ; Interleukin-6 - isolation & purification ; Membrane Proteins ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Oligonucleotide site-directed mutagenesis ; Organophosphorus Compounds ; Periplasm ; Plasmids ; Production of active biomolecules ; Promoter Regions, Genetic ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; Ribosomes - metabolism ; Serine Endopeptidases</subject><ispartof>Journal of biotechnology, 1993, Vol.27 (3), p.307-316</ispartof><rights>1993</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4143-e7a6a062339b9a758f7586fd753dcba65508268603f10a7b8a122aec53e2ae163</citedby><cites>FETCH-LOGICAL-c4143-e7a6a062339b9a758f7586fd753dcba65508268603f10a7b8a122aec53e2ae163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0168165693900933$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4691212$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7763469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barthelemy, I.</creatorcontrib><creatorcontrib>González de Buitrago, G.</creatorcontrib><creatorcontrib>Carreiro, C.</creatorcontrib><creatorcontrib>Roncal, F.</creatorcontrib><creatorcontrib>Pérez-Aranda, A.</creatorcontrib><creatorcontrib>Márquez, G.</creatorcontrib><creatorcontrib>Barbero, J.L.</creatorcontrib><title>Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase</title><title>Journal of biotechnology</title><addtitle>J Biotechnol</addtitle><description>We have developed a system for expressing human interleukin 6 into the periplasmic space of
Escherichia coli. The method is based on the expression of the hIL6 gene under the control of the regulatory signals of plasmid pINIII-OMPA3, i.e., lpp-lac promoter and the
E. coli OMPA ribosome binding site and leader sequence. Since microheterogeneity is known to occur in the amino end of the cytokine, we tested different ‘natural’ versions of the protein, and we found that the secretion process was only efficient when the N-terminal amino acid was not proline. In flask experiments this procedure yields about 8–10 mg of biologically active hIL6 per liter.</description><subject>Antineoplastic drugs. Cytokines</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cloning, Molecular - methods</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Endopeptidases - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Variation</subject><subject>Health. Pharmaceutical industry</subject><subject>Humans</subject><subject>IL6 signal peptide</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Interleukin-6 - biosynthesis</subject><subject>Interleukin-6 - genetics</subject><subject>Interleukin-6 - isolation & purification</subject><subject>Membrane Proteins</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Oligodeoxyribonucleotides</subject><subject>Oligonucleotide site-directed mutagenesis</subject><subject>Organophosphorus Compounds</subject><subject>Periplasm</subject><subject>Plasmids</subject><subject>Production of active biomolecules</subject><subject>Promoter Regions, Genetic</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Ribosomes - metabolism</subject><subject>Serine Endopeptidases</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcGO1DAMhiO0aBkW3gCkHFYIDl2Spk1bDkhoNcBKI-AA58hN3Z1Am3bjdqR9Jl6StDOaIwfLsvz5t-WfsVdS3Egh9fsYZSJ1rt9W6l0lRKUS9YRtZFmoJCu1umCbM_KMPSf6LYTIqlxessui0CrT1Yb9_RGGZraTGzwH33BCG3Cthpbv5x48d37C0OH8x3mul2rg0x75iMGNHVC_kFuy-1jbvQNuh8594Ni2zjr0Ex_DYJHI-fuF_JZEtd556PgBggM_0brqbqd5_bgqb29WDU7ufsFGHCfXAOEL9rSFjvDlKV-xX5-3P2-_JrvvX-5uP-0Sm8lMJViABqFTpaq6giIv2xi6bYpcNbYGneeiTHWphWqlgKIuQaYpoM0VxiS1umJvjrrx8ocZaTK9I4tdBx6HmUx8aCZ0XkUwO4I2DEQBWzMG10N4NFKYxSOzGLDw2lTKrB4ZFcden_TnusfmPHQyJfavT30gC10bwFtHZywiMpVpxD4eMYy_ODgMhpaHW2xcQDuZZnD_v-MfSu2u2w</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Barthelemy, I.</creator><creator>González de Buitrago, G.</creator><creator>Carreiro, C.</creator><creator>Roncal, F.</creator><creator>Pérez-Aranda, A.</creator><creator>Márquez, G.</creator><creator>Barbero, J.L.</creator><general>Elsevier B.V</general><general>Elsevier</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>1993</creationdate><title>Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase</title><author>Barthelemy, I. ; González de Buitrago, G. ; Carreiro, C. ; Roncal, F. ; Pérez-Aranda, A. ; Márquez, G. ; Barbero, J.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4143-e7a6a062339b9a758f7586fd753dcba65508268603f10a7b8a122aec53e2ae163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Antineoplastic drugs. Cytokines</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cloning, Molecular - methods</topic><topic>DNA - genetics</topic><topic>DNA - isolation & purification</topic><topic>Endopeptidases - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Variation</topic><topic>Health. Pharmaceutical industry</topic><topic>Humans</topic><topic>IL6 signal peptide</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Interleukin-6 - biosynthesis</topic><topic>Interleukin-6 - genetics</topic><topic>Interleukin-6 - isolation & purification</topic><topic>Membrane Proteins</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Oligodeoxyribonucleotides</topic><topic>Oligonucleotide site-directed mutagenesis</topic><topic>Organophosphorus Compounds</topic><topic>Periplasm</topic><topic>Plasmids</topic><topic>Production of active biomolecules</topic><topic>Promoter Regions, Genetic</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Ribosomes - metabolism</topic><topic>Serine Endopeptidases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barthelemy, I.</creatorcontrib><creatorcontrib>González de Buitrago, G.</creatorcontrib><creatorcontrib>Carreiro, C.</creatorcontrib><creatorcontrib>Roncal, F.</creatorcontrib><creatorcontrib>Pérez-Aranda, A.</creatorcontrib><creatorcontrib>Márquez, G.</creatorcontrib><creatorcontrib>Barbero, J.L.</creatorcontrib><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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barthelemy, I.</au><au>González de Buitrago, G.</au><au>Carreiro, C.</au><au>Roncal, F.</au><au>Pérez-Aranda, A.</au><au>Márquez, G.</au><au>Barbero, J.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase</atitle><jtitle>Journal of biotechnology</jtitle><addtitle>J Biotechnol</addtitle><date>1993</date><risdate>1993</risdate><volume>27</volume><issue>3</issue><spage>307</spage><epage>316</epage><pages>307-316</pages><issn>0168-1656</issn><eissn>1873-4863</eissn><coden>JBITD4</coden><abstract>We have developed a system for expressing human interleukin 6 into the periplasmic space of
Escherichia coli. The method is based on the expression of the hIL6 gene under the control of the regulatory signals of plasmid pINIII-OMPA3, i.e., lpp-lac promoter and the
E. coli OMPA ribosome binding site and leader sequence. Since microheterogeneity is known to occur in the amino end of the cytokine, we tested different ‘natural’ versions of the protein, and we found that the secretion process was only efficient when the N-terminal amino acid was not proline. In flask experiments this procedure yields about 8–10 mg of biologically active hIL6 per liter.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>7763469</pmid><doi>10.1016/0168-1656(93)90093-3</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0168-1656 |
| ispartof | Journal of biotechnology, 1993, Vol.27 (3), p.307-316 |
| issn | 0168-1656 1873-4863 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16540659 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Antineoplastic drugs. Cytokines Base Sequence Biological and medical sciences Biotechnology Cloning, Molecular - methods DNA - genetics DNA - isolation & purification Endopeptidases - metabolism Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic Variation Health. Pharmaceutical industry Humans IL6 signal peptide Industrial applications and implications. Economical aspects Interleukin-6 - biosynthesis Interleukin-6 - genetics Interleukin-6 - isolation & purification Membrane Proteins Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Oligonucleotide site-directed mutagenesis Organophosphorus Compounds Periplasm Plasmids Production of active biomolecules Promoter Regions, Genetic Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Ribosomes - metabolism Serine Endopeptidases |
| title | Production and secretion of human interleukin 6 into the periplasm of Escherichia coli: efficient processing of N-terminal variants of hIL6 by the E. coli signal peptidase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T05%3A23%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Production%20and%20secretion%20of%20human%20interleukin%206%20into%20the%20periplasm%20of%20Escherichia%20coli:%20efficient%20processing%20of%20N-terminal%20variants%20of%20hIL6%20by%20the%20E.%20coli%20signal%20peptidase&rft.jtitle=Journal%20of%20biotechnology&rft.au=Barthelemy,%20I.&rft.date=1993&rft.volume=27&rft.issue=3&rft.spage=307&rft.epage=316&rft.pages=307-316&rft.issn=0168-1656&rft.eissn=1873-4863&rft.coden=JBITD4&rft_id=info:doi/10.1016/0168-1656(93)90093-3&rft_dat=%3Cproquest_cross%3E16540659%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16540659&rft_id=info:pmid/7763469&rft_els_id=0168165693900933&rfr_iscdi=true |