Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein
Site-specific and strand-specific nicking at the origin of transfer ( oriT) of the F sex factor is the initial step in conjugal DNA metabolism. Then, DNA helicase I, the product of the traI gene, processively unwinds the plasmid from the nick site to generate the single strand of DNA that is transfe...
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| Veröffentlicht in: | Journal of molecular biology 1988-11, Vol.204 (1), p.205-209 |
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| container_title | Journal of molecular biology |
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| creator | Traxler, Beth A. Minkley, Edwin G. |
| description | Site-specific and strand-specific nicking at the origin of transfer (
oriT) of the F sex factor is the initial step in conjugal DNA metabolism. Then, DNA helicase I, the product of the
traI gene, processively unwinds the plasmid from the nick site to generate the single strand of DNA that is transferred to the recipient. The nick at
oriT is produced by the combined action of two Tra proteins, TraY and TraZ. The
traZ gene was never precisely mapped, as no available point mutation uniquely affected TraZ-dependent
oriT nicking. With several new mutations, we have demonstrated that TraZ activity is dependent upon
traI DNA sequences. The simplest interpretation of this finding is that the F TraI protein is bifunctional, with DNA unwinding and site-specific DNA nicking activities. |
| doi_str_mv | 10.1016/0022-2836(88)90609-2 |
| format | Article |
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oriT) of the F sex factor is the initial step in conjugal DNA metabolism. Then, DNA helicase I, the product of the
traI gene, processively unwinds the plasmid from the nick site to generate the single strand of DNA that is transferred to the recipient. The nick at
oriT is produced by the combined action of two Tra proteins, TraY and TraZ. The
traZ gene was never precisely mapped, as no available point mutation uniquely affected TraZ-dependent
oriT nicking. With several new mutations, we have demonstrated that TraZ activity is dependent upon
traI DNA sequences. The simplest interpretation of this finding is that the F TraI protein is bifunctional, with DNA unwinding and site-specific DNA nicking activities.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(88)90609-2</identifier><identifier>PMID: 2851049</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Bacterial Proteins - genetics ; Binding Sites ; Biological and medical sciences ; Conjugation, Genetic ; DNA Helicases - genetics ; DNA, Bacterial - metabolism ; Escherichia coli Proteins ; F Factor ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Molecular and cellular biology ; Molecular genetics ; Mutation ; Plasmids ; Replication ; Transfection</subject><ispartof>Journal of molecular biology, 1988-11, Vol.204 (1), p.205-209</ispartof><rights>1988</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-d105036a7c65d790ab3efb77093a38669680ff0d3e257acc3f20a7862dad41083</citedby><cites>FETCH-LOGICAL-c386t-d105036a7c65d790ab3efb77093a38669680ff0d3e257acc3f20a7862dad41083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(88)90609-2$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7041318$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2851049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Traxler, Beth A.</creatorcontrib><creatorcontrib>Minkley, Edwin G.</creatorcontrib><title>Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Site-specific and strand-specific nicking at the origin of transfer (
oriT) of the F sex factor is the initial step in conjugal DNA metabolism. Then, DNA helicase I, the product of the
traI gene, processively unwinds the plasmid from the nick site to generate the single strand of DNA that is transferred to the recipient. The nick at
oriT is produced by the combined action of two Tra proteins, TraY and TraZ. The
traZ gene was never precisely mapped, as no available point mutation uniquely affected TraZ-dependent
oriT nicking. With several new mutations, we have demonstrated that TraZ activity is dependent upon
traI DNA sequences. The simplest interpretation of this finding is that the F TraI protein is bifunctional, with DNA unwinding and site-specific DNA nicking activities.</description><subject>Bacterial Proteins - genetics</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Conjugation, Genetic</subject><subject>DNA Helicases - genetics</subject><subject>DNA, Bacterial - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>F Factor</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Mutation</subject><subject>Plasmids</subject><subject>Replication</subject><subject>Transfection</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFOGzEQhq2qFQToG7SSD1UFh4Wxvev1XiohCjQSgkt6thx73JhuvKntIPXt2SVRjpzmMN_8M_5MyBcGlwyYvALgvOJKyHOlLjqQ0FX8A5kxUF2lpFAfyeyAHJOTnJ8BoBG1OiJHXDUM6m5G3O1LcBgt0rIyhf58vKYr7IM1GemcmujokMKC5lCwyhu0wQdLY7B_Q_xDTUK6HMqK-m20JQwx08GPQUjv6CKZOd2koWCIZ-STN33Gz_t6Sn7f3S5uflUPT_fzm-uHygolS-UYNCCkaa1sXNuBWQr0y7aFTpgRkJ1U4D04gbxpjbXCczCtktwZV4_PFqfk-y533Ptvi7nodcgW-95EHLZZT6yspRzBegfaNOSc0OtNCmuT_msGepKrJ3N6MqeV0m9yNR_Hvu7zt8s1usPQ3ubY_7bvm2xN75OJNuQD1kLNBJvO_LHDcHTxEjDpbMP0By4ktEW7Ibx_xyuID5Pn</recordid><startdate>19881105</startdate><enddate>19881105</enddate><creator>Traxler, Beth A.</creator><creator>Minkley, Edwin G.</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>19881105</creationdate><title>Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein</title><author>Traxler, Beth A. ; Minkley, Edwin G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-d105036a7c65d790ab3efb77093a38669680ff0d3e257acc3f20a7862dad41083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Bacterial Proteins - genetics</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Conjugation, Genetic</topic><topic>DNA Helicases - genetics</topic><topic>DNA, Bacterial - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>F Factor</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Mutation</topic><topic>Plasmids</topic><topic>Replication</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Traxler, Beth A.</creatorcontrib><creatorcontrib>Minkley, Edwin G.</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>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Traxler, Beth A.</au><au>Minkley, Edwin G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1988-11-05</date><risdate>1988</risdate><volume>204</volume><issue>1</issue><spage>205</spage><epage>209</epage><pages>205-209</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>Site-specific and strand-specific nicking at the origin of transfer (
oriT) of the F sex factor is the initial step in conjugal DNA metabolism. Then, DNA helicase I, the product of the
traI gene, processively unwinds the plasmid from the nick site to generate the single strand of DNA that is transferred to the recipient. The nick at
oriT is produced by the combined action of two Tra proteins, TraY and TraZ. The
traZ gene was never precisely mapped, as no available point mutation uniquely affected TraZ-dependent
oriT nicking. With several new mutations, we have demonstrated that TraZ activity is dependent upon
traI DNA sequences. The simplest interpretation of this finding is that the F TraI protein is bifunctional, with DNA unwinding and site-specific DNA nicking activities.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>2851049</pmid><doi>10.1016/0022-2836(88)90609-2</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1988-11, Vol.204 (1), p.205-209 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78626466 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Bacterial Proteins - genetics Binding Sites Biological and medical sciences Conjugation, Genetic DNA Helicases - genetics DNA, Bacterial - metabolism Escherichia coli Proteins F Factor Fundamental and applied biological sciences. Psychology Genes, Bacterial Molecular and cellular biology Molecular genetics Mutation Plasmids Replication Transfection |
| title | Evidence that DNA helicase I and oriT site-specific nicking are both functions of the F TraI protein |
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