Expression of gonococcal protein II in Escherichia coli by translational fusion
Summary Aprotein II (P.II) gene from Neisseria gonorrhoeae was cloned in Escherichia coli and characterized by DNA sequence analysis. As with other reported P.II sequences, this gene contains an ATG initiation codon which is out of frame with respect to the remainder of the P.II amino acid sequence....
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| Veröffentlicht in: | Molecular microbiology 1989-05, Vol.3 (5), p.663-671 |
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| container_title | Molecular microbiology |
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| creator | Palmer, L. Brooks, G. F. Falkow, S. |
| description | Summary
Aprotein II (P.II) gene from Neisseria gonorrhoeae was cloned in Escherichia coli and characterized by DNA sequence analysis. As with other reported P.II sequences, this gene contains an ATG initiation codon which is out of frame with respect to the remainder of the P.II amino acid sequence. A translational fusion was constructed in E. coli which linked the P.II sequence to the signal peptide of β‐lactamase. This P.II fusion differs from the gonococcal protein only in the first seven residues at the N terminus. In E. coli, the P.II fusion product exhibits properties analogous to those of P.II in N. gonorrhoeae. The P.II fusion product is a major component of the E. coli outer membrane and it is exposed on the cell surface. The P.II fusion protein also exhibits the heat‐modifiable phenotype of gonococcal P.II. |
| doi_str_mv | 10.1111/j.1365-2958.1989.tb00214.x |
| format | Article |
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Aprotein II (P.II) gene from Neisseria gonorrhoeae was cloned in Escherichia coli and characterized by DNA sequence analysis. As with other reported P.II sequences, this gene contains an ATG initiation codon which is out of frame with respect to the remainder of the P.II amino acid sequence. A translational fusion was constructed in E. coli which linked the P.II sequence to the signal peptide of β‐lactamase. This P.II fusion differs from the gonococcal protein only in the first seven residues at the N terminus. In E. coli, the P.II fusion product exhibits properties analogous to those of P.II in N. gonorrhoeae. The P.II fusion product is a major component of the E. coli outer membrane and it is exposed on the cell surface. The P.II fusion protein also exhibits the heat‐modifiable phenotype of gonococcal P.II.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.1989.tb00214.x</identifier><identifier>PMID: 2503682</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Antigens, Bacterial - biosynthesis ; Antigens, Bacterial - genetics ; Autoradiography ; Bacterial Outer Membrane Proteins - biosynthesis ; Bacterial Outer Membrane Proteins - genetics ; Bacteriology ; Base Sequence ; beta-Lactamases - genetics ; Biological and medical sciences ; cloning ; Cloning, Molecular ; DNA, Bacterial ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; gene expression ; genes ; Genetics ; Hot Temperature ; Immunoblotting ; Microbiology ; Molecular Sequence Data ; Neisseria gonorrhoeae - genetics ; nucleotide sequence ; Plasmids ; protein II ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - genetics</subject><ispartof>Molecular microbiology, 1989-05, Vol.3 (5), p.663-671</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4293-5b7cb8adfd39c0fda82c18bc39cd60aa3569624812040a3f21d09e105bc9bb6e3</citedby><cites>FETCH-LOGICAL-c4293-5b7cb8adfd39c0fda82c18bc39cd60aa3569624812040a3f21d09e105bc9bb6e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.1989.tb00214.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.1989.tb00214.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7373599$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2503682$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Palmer, L.</creatorcontrib><creatorcontrib>Brooks, G. F.</creatorcontrib><creatorcontrib>Falkow, S.</creatorcontrib><title>Expression of gonococcal protein II in Escherichia coli by translational fusion</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Aprotein II (P.II) gene from Neisseria gonorrhoeae was cloned in Escherichia coli and characterized by DNA sequence analysis. As with other reported P.II sequences, this gene contains an ATG initiation codon which is out of frame with respect to the remainder of the P.II amino acid sequence. A translational fusion was constructed in E. coli which linked the P.II sequence to the signal peptide of β‐lactamase. This P.II fusion differs from the gonococcal protein only in the first seven residues at the N terminus. In E. coli, the P.II fusion product exhibits properties analogous to those of P.II in N. gonorrhoeae. The P.II fusion product is a major component of the E. coli outer membrane and it is exposed on the cell surface. The P.II fusion protein also exhibits the heat‐modifiable phenotype of gonococcal P.II.</description><subject>Amino Acid Sequence</subject><subject>Antigens, Bacterial - biosynthesis</subject><subject>Antigens, Bacterial - genetics</subject><subject>Autoradiography</subject><subject>Bacterial Outer Membrane Proteins - biosynthesis</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>beta-Lactamases - genetics</subject><subject>Biological and medical sciences</subject><subject>cloning</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>genes</subject><subject>Genetics</subject><subject>Hot Temperature</subject><subject>Immunoblotting</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Neisseria gonorrhoeae - genetics</subject><subject>nucleotide sequence</subject><subject>Plasmids</subject><subject>protein II</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - genetics</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE9LwzAYh4MoOqcfQSgi3lrzp0kTD4KMqQPFi4K3kKSpZnTNbFrcvr0pK7uKOSSE3_O-efMAcIlghuK6WWaIMJpiQXmGBBdZpyHEKM82B2Cyjw7BBAoKU8Lxxwk4DWEJISKQkWNwjCkkjOMJeJ1v1q0Nwfkm8VXy6RtvvDGqTtat76xrksUiifs8mC_bOvPlVGJ87RK9TbpWNaFWXayNfNUPTc7AUaXqYM_HcwreH-Zvs6f0-fVxMbt_Tk2OBUmpLozmqqxKIgysSsWxQVybeCsZVIpQJhjOOcIwh4pUGJVQWASpNkJrZskUXO_6xjG_exs6uXLB2LpWjfV9kIVAJOeM_AkiigkuchbB2x1oWh9Cayu5bt1KtVuJoBy0y6Uc3MrBrRy0y1G73MTii_GVXq9suS8dPcf8asxViHKraM64sMcKUhAqRMTudtiPq-32HwPIl5cFi7_9Bfxin4o</recordid><startdate>198905</startdate><enddate>198905</enddate><creator>Palmer, L.</creator><creator>Brooks, G. F.</creator><creator>Falkow, S.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell Science</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>7QL</scope><scope>7QO</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>198905</creationdate><title>Expression of gonococcal protein II in Escherichia coli by translational fusion</title><author>Palmer, L. ; Brooks, G. F. ; Falkow, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4293-5b7cb8adfd39c0fda82c18bc39cd60aa3569624812040a3f21d09e105bc9bb6e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Antigens, Bacterial - biosynthesis</topic><topic>Antigens, Bacterial - genetics</topic><topic>Autoradiography</topic><topic>Bacterial Outer Membrane Proteins - biosynthesis</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>beta-Lactamases - genetics</topic><topic>Biological and medical sciences</topic><topic>cloning</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>genes</topic><topic>Genetics</topic><topic>Hot Temperature</topic><topic>Immunoblotting</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Neisseria gonorrhoeae - genetics</topic><topic>nucleotide sequence</topic><topic>Plasmids</topic><topic>protein II</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Palmer, L.</creatorcontrib><creatorcontrib>Brooks, G. F.</creatorcontrib><creatorcontrib>Falkow, S.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Palmer, L.</au><au>Brooks, G. F.</au><au>Falkow, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of gonococcal protein II in Escherichia coli by translational fusion</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1989-05</date><risdate>1989</risdate><volume>3</volume><issue>5</issue><spage>663</spage><epage>671</epage><pages>663-671</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Aprotein II (P.II) gene from Neisseria gonorrhoeae was cloned in Escherichia coli and characterized by DNA sequence analysis. As with other reported P.II sequences, this gene contains an ATG initiation codon which is out of frame with respect to the remainder of the P.II amino acid sequence. A translational fusion was constructed in E. coli which linked the P.II sequence to the signal peptide of β‐lactamase. This P.II fusion differs from the gonococcal protein only in the first seven residues at the N terminus. In E. coli, the P.II fusion product exhibits properties analogous to those of P.II in N. gonorrhoeae. The P.II fusion product is a major component of the E. coli outer membrane and it is exposed on the cell surface. The P.II fusion protein also exhibits the heat‐modifiable phenotype of gonococcal P.II.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2503682</pmid><doi>10.1111/j.1365-2958.1989.tb00214.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Molecular microbiology, 1989-05, Vol.3 (5), p.663-671 |
| issn | 0950-382X 1365-2958 |
| language | eng |
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| source | Wiley-Blackwell Journals; MEDLINE |
| subjects | Amino Acid Sequence Antigens, Bacterial - biosynthesis Antigens, Bacterial - genetics Autoradiography Bacterial Outer Membrane Proteins - biosynthesis Bacterial Outer Membrane Proteins - genetics Bacteriology Base Sequence beta-Lactamases - genetics Biological and medical sciences cloning Cloning, Molecular DNA, Bacterial Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene expression genes Genetics Hot Temperature Immunoblotting Microbiology Molecular Sequence Data Neisseria gonorrhoeae - genetics nucleotide sequence Plasmids protein II Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - genetics |
| title | Expression of gonococcal protein II in Escherichia coli by translational fusion |
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