Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3
Using the M13 dideoxy sequencing technique, we have established the DNA sequences of colicins E2 and E3 which encompass the receptor-binding and the catalytic domains of each of the nucleases, and their immunity (imm) genes. The imm gene of plasmid ColE2-P9 is 255 bp long and is separated from the e...
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Veröffentlicht in: | Nucleic acids research 1984-11, Vol.12 (22), p.8733-8745 |
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creator | Lau, Peter C.K. Rowsome, R.Wally Zuker, Michael Visentin, Louis P. |
description | Using the M13 dideoxy sequencing technique, we have established the DNA sequences of colicins E2 and E3 which encompass the receptor-binding and the catalytic domains of each of the nucleases, and their immunity (imm) genes. The imm gene of plasmid ColE2-P9 is 255 bp long and is separated from the end of the col gene by a dinucleotide. This gene pair is arranged similarly in plasmid ColE3-CA38 except that the intergenic space is 9 bp and the E3 imm gene is one codon shorter than its E2 counterpart. Comparisons of the E2 and E3 imm sequences indicate considerable divergence whereas the receptor-binding domains of both colicins are highly conserved. The two nuclease domains appear to share some sequence homology. A possible evolutionary relationship between colicin E3 and other microbial extracellular ribonucleases is also suggested from the sequence alignment analysis. |
doi_str_mv | 10.1093/nar/12.22.8733 |
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The imm gene of plasmid ColE2-P9 is 255 bp long and is separated from the end of the col gene by a dinucleotide. This gene pair is arranged similarly in plasmid ColE3-CA38 except that the intergenic space is 9 bp and the E3 imm gene is one codon shorter than its E2 counterpart. Comparisons of the E2 and E3 imm sequences indicate considerable divergence whereas the receptor-binding domains of both colicins are highly conserved. The two nuclease domains appear to share some sequence homology. A possible evolutionary relationship between colicin E3 and other microbial extracellular ribonucleases is also suggested from the sequence alignment analysis.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/12.22.8733</identifier><identifier>PMID: 6095211</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - genetics ; Base Sequence ; Cloning, Molecular ; Colicins - genetics ; DNA Restriction Enzymes ; DNA, Bacterial - genetics ; Escherichia coli - genetics ; Escherichia coli - immunology ; Escherichia coli Proteins ; Genes ; Genes, Bacterial ; Plasmids</subject><ispartof>Nucleic acids research, 1984-11, Vol.12 (22), p.8733-8745</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4283-dba58ded9e203cebddf08a292934706beffdcae00530a4fa5780d637d81c22723</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC320411/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC320411/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6095211$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lau, Peter C.K.</creatorcontrib><creatorcontrib>Rowsome, R.Wally</creatorcontrib><creatorcontrib>Zuker, Michael</creatorcontrib><creatorcontrib>Visentin, Louis P.</creatorcontrib><title>Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Using the M13 dideoxy sequencing technique, we have established the DNA sequences of colicins E2 and E3 which encompass the receptor-binding and the catalytic domains of each of the nucleases, and their immunity (imm) genes. The imm gene of plasmid ColE2-P9 is 255 bp long and is separated from the end of the col gene by a dinucleotide. This gene pair is arranged similarly in plasmid ColE3-CA38 except that the intergenic space is 9 bp and the E3 imm gene is one codon shorter than its E2 counterpart. Comparisons of the E2 and E3 imm sequences indicate considerable divergence whereas the receptor-binding domains of both colicins are highly conserved. The two nuclease domains appear to share some sequence homology. A possible evolutionary relationship between colicin E3 and other microbial extracellular ribonucleases is also suggested from the sequence alignment analysis.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - genetics</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Colicins - genetics</subject><subject>DNA Restriction Enzymes</subject><subject>DNA, Bacterial - genetics</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - immunology</subject><subject>Escherichia coli Proteins</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Plasmids</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkTtv2zAURomiQeqkXbsV4NRNDnmp59ChMJxHYaRLWhRdCIq8SthKpEpKgf3vI8WG0UxZyOGc74KXHyEfOVtyVokLp8IFhyXAsiyEeEMWXOSQpFUOb8mCCZYlnKXlO3IW4x_GeMqz9JSc5qzKgPMF2a5816ugBvuI1I26RT9YgzTivxGdxkin0xvr7unwgNR23ejssKN98ANaF6ly5ploFWq_3bXJgKGzTrW0x34eFalvqPat1bO-hufEWrwnJ41qI3443Ofkx-X6bnWdbL5f3ay-bhKdQikSU6usNGgqBCY01sY0rFRQQSXSguU1No3RChnLBFNpo7KiZCYXhSm5BihAnJMv-7n9WHdoNLohqFb2wXYq7KRXVr4kzj7Ie_8oBbCU8yn_-ZAPfvqSOMjORo1tqxz6McoiKypeCnhV5JXIAEC8LqbzMnk5icu9qIOPMWBzfDVnci5fTuVLDhJAzuVPgU__73rUD21PPNlzGwfcHrEKf2VeiCKT179-y9vN3eb2208uuXgCt8K9RA</recordid><startdate>19841126</startdate><enddate>19841126</enddate><creator>Lau, Peter C.K.</creator><creator>Rowsome, R.Wally</creator><creator>Zuker, Michael</creator><creator>Visentin, Louis P.</creator><general>Oxford University Press</general><scope>BSCLL</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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19841126</creationdate><title>Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3</title><author>Lau, Peter C.K. ; Rowsome, R.Wally ; Zuker, Michael ; Visentin, Louis P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4283-dba58ded9e203cebddf08a292934706beffdcae00530a4fa5780d637d81c22723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - genetics</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>Colicins - genetics</topic><topic>DNA Restriction Enzymes</topic><topic>DNA, Bacterial - genetics</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - immunology</topic><topic>Escherichia coli Proteins</topic><topic>Genes</topic><topic>Genes, Bacterial</topic><topic>Plasmids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lau, Peter C.K.</creatorcontrib><creatorcontrib>Rowsome, R.Wally</creatorcontrib><creatorcontrib>Zuker, Michael</creatorcontrib><creatorcontrib>Visentin, Louis P.</creatorcontrib><collection>Istex</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>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>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lau, Peter C.K.</au><au>Rowsome, R.Wally</au><au>Zuker, Michael</au><au>Visentin, Louis P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1984-11-26</date><risdate>1984</risdate><volume>12</volume><issue>22</issue><spage>8733</spage><epage>8745</epage><pages>8733-8745</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Using the M13 dideoxy sequencing technique, we have established the DNA sequences of colicins E2 and E3 which encompass the receptor-binding and the catalytic domains of each of the nucleases, and their immunity (imm) genes. The imm gene of plasmid ColE2-P9 is 255 bp long and is separated from the end of the col gene by a dinucleotide. This gene pair is arranged similarly in plasmid ColE3-CA38 except that the intergenic space is 9 bp and the E3 imm gene is one codon shorter than its E2 counterpart. Comparisons of the E2 and E3 imm sequences indicate considerable divergence whereas the receptor-binding domains of both colicins are highly conserved. The two nuclease domains appear to share some sequence homology. A possible evolutionary relationship between colicin E3 and other microbial extracellular ribonucleases is also suggested from the sequence alignment analysis.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>6095211</pmid><doi>10.1093/nar/12.22.8733</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Bacterial Proteins - genetics Base Sequence Cloning, Molecular Colicins - genetics DNA Restriction Enzymes DNA, Bacterial - genetics Escherichia coli - genetics Escherichia coli - immunology Escherichia coli Proteins Genes Genes, Bacterial Plasmids |
title | Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3 |
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