The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F‐like plasmids
Summary The effects of defined mutations In the lipopolysaccharide (LPS) and the outer membrane protein OmpA of the recipient cell on mating‐pair formation in liquid media by the transfer systems of the F‐Iike plasmids pOX38 (F), ColB2 and R100‐1 were investigated. Transfer of all three plasmids was...
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Veröffentlicht in: | Molecular microbiology 1994-09, Vol.13 (6), p.939-953 |
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The effects of defined mutations In the lipopolysaccharide (LPS) and the outer membrane protein OmpA of the recipient cell on mating‐pair formation in liquid media by the transfer systems of the F‐Iike plasmids pOX38 (F), ColB2 and R100‐1 were investigated. Transfer of all three plasmids was affected differently by mutations in the rfa (LPS) locus of the recipient cell, the F plasmid being most sensitive to mutations that affected rfaP gene expression which is responslbie for the addition of pyrophosphorylethanolamine (PPEA) to heptose I of the inner core of the LPS. CoIB2 transfer was more strongly affected by mutations in the heptose II‐heptose III region of the LPS (rfaF) whereas R100‐1 was not strongly affected by any of the rfa mutations tested. ompA but not rfa mutations further decreased the mating efficiency of an F plasmid carrying a mutation in the mating‐pair stabilization protein TraN. An F derivative with a chloramphenicol acetyltransferase (CAT) cassette interrupting the traA pilin gene was constructed and pilin genes from F‐like plasmids (F, ColB2, R100‐1) were used to complement this mutation. Unexpectediy, the results suggested that the differences in the pilin sequences were not responsible for recognizing specific groups in the LPS, OmpA or the TraT surface exclusion protein. Other corroborating evidence is presented suggesting the presence of an adhesin at the F pilus tip. |
doi_str_mv | 10.1111/j.1365-2958.1994.tb00486.x |
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The effects of defined mutations In the lipopolysaccharide (LPS) and the outer membrane protein OmpA of the recipient cell on mating‐pair formation in liquid media by the transfer systems of the F‐Iike plasmids pOX38 (F), ColB2 and R100‐1 were investigated. Transfer of all three plasmids was affected differently by mutations in the rfa (LPS) locus of the recipient cell, the F plasmid being most sensitive to mutations that affected rfaP gene expression which is responslbie for the addition of pyrophosphorylethanolamine (PPEA) to heptose I of the inner core of the LPS. CoIB2 transfer was more strongly affected by mutations in the heptose II‐heptose III region of the LPS (rfaF) whereas R100‐1 was not strongly affected by any of the rfa mutations tested. ompA but not rfa mutations further decreased the mating efficiency of an F plasmid carrying a mutation in the mating‐pair stabilization protein TraN. An F derivative with a chloramphenicol acetyltransferase (CAT) cassette interrupting the traA pilin gene was constructed and pilin genes from F‐like plasmids (F, ColB2, R100‐1) were used to complement this mutation. Unexpectediy, the results suggested that the differences in the pilin sequences were not responsible for recognizing specific groups in the LPS, OmpA or the TraT surface exclusion protein. Other corroborating evidence is presented suggesting the presence of an adhesin at the F pilus tip.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.1994.tb00486.x</identifier><identifier>PMID: 7854127</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Bacterial Adhesion ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Outer Membrane Proteins - physiology ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Carbohydrate Sequence ; Conjugation, Genetic - physiology ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - physiology ; Escherichia coli Proteins ; Ethanolamines - metabolism ; F Factor - physiology ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genetics ; Lipopolysaccharides - metabolism ; Microbiology ; Molecular Sequence Data ; Pili, Sex - physiology ; Plasmids - physiology ; Salmonella typhimurium - genetics ; Salmonella typhimurium - physiology</subject><ispartof>Molecular microbiology, 1994-09, Vol.13 (6), p.939-953</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4299-f3cb16d06646628a2532bba9b2205f1b3284d983a821b55c1cf61271fc78e6a33</citedby><cites>FETCH-LOGICAL-c4299-f3cb16d06646628a2532bba9b2205f1b3284d983a821b55c1cf61271fc78e6a33</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.1365-2958.1994.tb00486.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.1994.tb00486.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4228594$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7854127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Anthony, Karen G.</creatorcontrib><creatorcontrib>Sherburne, Craig</creatorcontrib><creatorcontrib>Sherburne, Richard</creatorcontrib><creatorcontrib>Frost, Laura S.</creatorcontrib><title>The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F‐like plasmids</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
The effects of defined mutations In the lipopolysaccharide (LPS) and the outer membrane protein OmpA of the recipient cell on mating‐pair formation in liquid media by the transfer systems of the F‐Iike plasmids pOX38 (F), ColB2 and R100‐1 were investigated. Transfer of all three plasmids was affected differently by mutations in the rfa (LPS) locus of the recipient cell, the F plasmid being most sensitive to mutations that affected rfaP gene expression which is responslbie for the addition of pyrophosphorylethanolamine (PPEA) to heptose I of the inner core of the LPS. CoIB2 transfer was more strongly affected by mutations in the heptose II‐heptose III region of the LPS (rfaF) whereas R100‐1 was not strongly affected by any of the rfa mutations tested. ompA but not rfa mutations further decreased the mating efficiency of an F plasmid carrying a mutation in the mating‐pair stabilization protein TraN. An F derivative with a chloramphenicol acetyltransferase (CAT) cassette interrupting the traA pilin gene was constructed and pilin genes from F‐like plasmids (F, ColB2, R100‐1) were used to complement this mutation. Unexpectediy, the results suggested that the differences in the pilin sequences were not responsible for recognizing specific groups in the LPS, OmpA or the TraT surface exclusion protein. Other corroborating evidence is presented suggesting the presence of an adhesin at the F pilus tip.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Adhesion</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Outer Membrane Proteins - physiology</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Sequence</subject><subject>Conjugation, Genetic - physiology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - physiology</subject><subject>Escherichia coli Proteins</subject><subject>Ethanolamines - metabolism</subject><subject>F Factor - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes, Bacterial</subject><subject>Genetics</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Pili, Sex - physiology</subject><subject>Plasmids - physiology</subject><subject>Salmonella typhimurium - genetics</subject><subject>Salmonella typhimurium - physiology</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS1EVYbCIyBZCLFL8H9sFkhVRaFSq26KxM6yHWfw4HEGOxGdHY_AM_IkTTrRbFG9sa3z3WvfcwB4i1GNp_VhU2MqeEUUlzVWitWDRYhJUd8_A6uj9ByskOKoopJ8fwFelrJBCFMk6Ck4bSRnmDQrkO5-eJj76GHfwWE670IcCwwJZu_CLvg0QOdjnK_9OoUh9Am2Yw5pDa1xg8_BROj6tBnX5lHc-jaYwbfQ7uHlvz9_Y_g5dY2mbENbXoGTzsTiXy_7Gfh2-fnu4mt1ffvl6uL8unKMKFV11FksWiQEE4JIQzgl1hplCUG8w5YSyVolqZEEW84ddp2YxsGda6QXhtIz8P7Qd5f7X6Mvg96GMs9hku_Hopum4RJh_F8QC4EEewQ_HkCX-1Ky7_Quh63Je42RnlPRGz1br2fr9ZyKXlLR91Pxm-WV0U7-HEuXGCb93aKb4kzsskkulCPGCJFcsQn7dMB-h-j3T_iAvrm5UlTRB31WqvA</recordid><startdate>199409</startdate><enddate>199409</enddate><creator>Anthony, Karen G.</creator><creator>Sherburne, Craig</creator><creator>Sherburne, Richard</creator><creator>Frost, Laura 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>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>199409</creationdate><title>The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F‐like plasmids</title><author>Anthony, Karen G. ; Sherburne, Craig ; Sherburne, Richard ; Frost, Laura S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4299-f3cb16d06646628a2532bba9b2205f1b3284d983a821b55c1cf61271fc78e6a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Adhesion</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Outer Membrane Proteins - physiology</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Sequence</topic><topic>Conjugation, Genetic - physiology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - physiology</topic><topic>Escherichia coli Proteins</topic><topic>Ethanolamines - metabolism</topic><topic>F Factor - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes, Bacterial</topic><topic>Genetics</topic><topic>Lipopolysaccharides - metabolism</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Pili, Sex - physiology</topic><topic>Plasmids - physiology</topic><topic>Salmonella typhimurium - genetics</topic><topic>Salmonella typhimurium - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anthony, Karen G.</creatorcontrib><creatorcontrib>Sherburne, Craig</creatorcontrib><creatorcontrib>Sherburne, Richard</creatorcontrib><creatorcontrib>Frost, Laura 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>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anthony, Karen G.</au><au>Sherburne, Craig</au><au>Sherburne, Richard</au><au>Frost, Laura S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F‐like plasmids</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1994-09</date><risdate>1994</risdate><volume>13</volume><issue>6</issue><spage>939</spage><epage>953</epage><pages>939-953</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
The effects of defined mutations In the lipopolysaccharide (LPS) and the outer membrane protein OmpA of the recipient cell on mating‐pair formation in liquid media by the transfer systems of the F‐Iike plasmids pOX38 (F), ColB2 and R100‐1 were investigated. Transfer of all three plasmids was affected differently by mutations in the rfa (LPS) locus of the recipient cell, the F plasmid being most sensitive to mutations that affected rfaP gene expression which is responslbie for the addition of pyrophosphorylethanolamine (PPEA) to heptose I of the inner core of the LPS. CoIB2 transfer was more strongly affected by mutations in the heptose II‐heptose III region of the LPS (rfaF) whereas R100‐1 was not strongly affected by any of the rfa mutations tested. ompA but not rfa mutations further decreased the mating efficiency of an F plasmid carrying a mutation in the mating‐pair stabilization protein TraN. An F derivative with a chloramphenicol acetyltransferase (CAT) cassette interrupting the traA pilin gene was constructed and pilin genes from F‐like plasmids (F, ColB2, R100‐1) were used to complement this mutation. Unexpectediy, the results suggested that the differences in the pilin sequences were not responsible for recognizing specific groups in the LPS, OmpA or the TraT surface exclusion protein. Other corroborating evidence is presented suggesting the presence of an adhesin at the F pilus tip.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7854127</pmid><doi>10.1111/j.1365-2958.1994.tb00486.x</doi><tpages>15</tpages></addata></record> |
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subjects | Amino Acid Sequence Bacterial Adhesion Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Outer Membrane Proteins - physiology Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Carbohydrate Sequence Conjugation, Genetic - physiology Escherichia coli Escherichia coli - genetics Escherichia coli - physiology Escherichia coli Proteins Ethanolamines - metabolism F Factor - physiology Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Genes, Bacterial Genetics Lipopolysaccharides - metabolism Microbiology Molecular Sequence Data Pili, Sex - physiology Plasmids - physiology Salmonella typhimurium - genetics Salmonella typhimurium - physiology |
title | The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F‐like plasmids |
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