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Isolation and Characterization of Intermediates in Site-Specific Recombination
Cre, the site-specific recombinase from bacteriophage P1, catalyzes a recombination reaction between specific DNA sequences designated as lox sites. The breakage and rejoining of partners during this recombination process must be highly concerted because it has not been possible to detect intermedia...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS 1987-10, Vol.84 (19), p.6840-6844 |
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| container_end_page | 6844 |
| container_issue | 19 |
| container_start_page | 6840 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 84 |
| creator | Hoess, Ronald Wierzbicki, Anna Abremski, Kenneth |
| description | Cre, the site-specific recombinase from bacteriophage P1, catalyzes a recombination reaction between specific DNA sequences designated as lox sites. The breakage and rejoining of partners during this recombination process must be highly concerted because it has not been possible to detect intermediates of the reaction with wild-type Cre. Several mutant Cre proteins have been isolated that produce significant amounts of a possible intermediate product of the recombination reaction. The product has been identified as a Holliday structure in which one set of the DNA strands of the recombining partners has been exchanged. Wild-type Cre protein is capable of acting on this structure to form recombinant products, which is consistent with this being an intermediate in the recombination reaction. Characterization of the Holliday structure indicated that one set of strands in the recombining partners was always exchanged preferentially before the other set. In addition, it has been found that certain Cre mutants that are unable to carry out recombination in vitro are able to resolve the intermediate. This suggests that these mutants are defective in a step in the reaction that precedes the formation of the Holliday intermediate. |
| doi_str_mv | 10.1073/pnas.84.19.6840 |
| format | article |
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The breakage and rejoining of partners during this recombination process must be highly concerted because it has not been possible to detect intermediates of the reaction with wild-type Cre. Several mutant Cre proteins have been isolated that produce significant amounts of a possible intermediate product of the recombination reaction. The product has been identified as a Holliday structure in which one set of the DNA strands of the recombining partners has been exchanged. Wild-type Cre protein is capable of acting on this structure to form recombinant products, which is consistent with this being an intermediate in the recombination reaction. Characterization of the Holliday structure indicated that one set of strands in the recombining partners was always exchanged preferentially before the other set. In addition, it has been found that certain Cre mutants that are unable to carry out recombination in vitro are able to resolve the intermediate. This suggests that these mutants are defective in a step in the reaction that precedes the formation of the Holliday intermediate.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.19.6840</identifier><identifier>PMID: 2821547</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Bacteriophages ; Biological and medical sciences ; Coliphages - genetics ; Cruciform DNA ; DNA ; DNA Nucleotidyltransferases - genetics ; DNA Nucleotidyltransferases - metabolism ; DNA Restriction Enzymes ; DNA, Viral - genetics ; DNA, Viral - ultrastructure ; Electron microscopy ; Enzymes ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gels ; Genic rearrangement. Recombination. Transposable element ; Integrases ; Molecular and cellular biology ; Molecular genetics ; Molecules ; Mutation ; Plasmids ; Recombination reactions ; Recombination, Genetic ; Topology ; Viral Proteins</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1987-10, Vol.84 (19), p.6840-6844</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-850af16a61351d150d423ab4f4205cafdae848a4d22b22f4c6381594199bf1ae3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/19.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30676$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30676$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7390834$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2821547$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hoess, Ronald</creatorcontrib><creatorcontrib>Wierzbicki, Anna</creatorcontrib><creatorcontrib>Abremski, Kenneth</creatorcontrib><title>Isolation and Characterization of Intermediates in Site-Specific Recombination</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Cre, the site-specific recombinase from bacteriophage P1, catalyzes a recombination reaction between specific DNA sequences designated as lox sites. The breakage and rejoining of partners during this recombination process must be highly concerted because it has not been possible to detect intermediates of the reaction with wild-type Cre. Several mutant Cre proteins have been isolated that produce significant amounts of a possible intermediate product of the recombination reaction. The product has been identified as a Holliday structure in which one set of the DNA strands of the recombining partners has been exchanged. Wild-type Cre protein is capable of acting on this structure to form recombinant products, which is consistent with this being an intermediate in the recombination reaction. Characterization of the Holliday structure indicated that one set of strands in the recombining partners was always exchanged preferentially before the other set. In addition, it has been found that certain Cre mutants that are unable to carry out recombination in vitro are able to resolve the intermediate. This suggests that these mutants are defective in a step in the reaction that precedes the formation of the Holliday intermediate.</description><subject>Bacteriophages</subject><subject>Biological and medical sciences</subject><subject>Coliphages - genetics</subject><subject>Cruciform DNA</subject><subject>DNA</subject><subject>DNA Nucleotidyltransferases - genetics</subject><subject>DNA Nucleotidyltransferases - metabolism</subject><subject>DNA Restriction Enzymes</subject><subject>DNA, Viral - genetics</subject><subject>DNA, Viral - ultrastructure</subject><subject>Electron microscopy</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Genic rearrangement. Recombination. Transposable element</subject><subject>Integrases</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecules</subject><subject>Mutation</subject><subject>Plasmids</subject><subject>Recombination reactions</subject><subject>Recombination, Genetic</subject><subject>Topology</subject><subject>Viral Proteins</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNp9kc1v1DAQxS1EVZbCGQkJlAOip2zHH0nsAwe0ArpSBRKFszVxbOoqay-2FwF_fbNsWNELp5Hn_d7MyI-QZxSWFDp-sQ2Yl1IsqVq2UsADsqCgaN0KBQ_JAoB1tRRMPCKPc74FANVIOCWnTDLaiG5BPq5zHLH4GCoMQ7W6wYSm2OR_H5rRVeswvTd28Fhsrnyorn2x9fXWGu-8qT5bEze9D3_4J-TE4Zjt07meka_v331ZXdZXnz6sV2-vatM0ballA-hoiy3lDR1oA4NgHHvhBIPGoBvQSiFRDIz1jDlhWi5powRVqncULT8jbw5zt7t-Os3YUBKOepv8BtMvHdHr-0rwN_pb_KGZUlTC5H89-1P8vrO56I3Pxo4jBht3WUsKgtOOTuDFATQp5pysO-6goPcJ6H0CWgpNld4nMDle_HvakZ-_fNJfzTpmg6NLGIzPR6zjCiQXE_Zyxvbz_6r39pz_F9BuN47F_iwT-fxA3uYS0xHl0HYtvwN85bEq</recordid><startdate>19871001</startdate><enddate>19871001</enddate><creator>Hoess, Ronald</creator><creator>Wierzbicki, Anna</creator><creator>Abremski, Kenneth</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>5PM</scope></search><sort><creationdate>19871001</creationdate><title>Isolation and Characterization of Intermediates in Site-Specific Recombination</title><author>Hoess, Ronald ; Wierzbicki, Anna ; Abremski, Kenneth</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-850af16a61351d150d423ab4f4205cafdae848a4d22b22f4c6381594199bf1ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Bacteriophages</topic><topic>Biological and medical sciences</topic><topic>Coliphages - genetics</topic><topic>Cruciform DNA</topic><topic>DNA</topic><topic>DNA Nucleotidyltransferases - genetics</topic><topic>DNA Nucleotidyltransferases - metabolism</topic><topic>DNA Restriction Enzymes</topic><topic>DNA, Viral - genetics</topic><topic>DNA, Viral - ultrastructure</topic><topic>Electron microscopy</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Genic rearrangement. Recombination. Transposable element</topic><topic>Integrases</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecules</topic><topic>Mutation</topic><topic>Plasmids</topic><topic>Recombination reactions</topic><topic>Recombination, Genetic</topic><topic>Topology</topic><topic>Viral Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hoess, Ronald</creatorcontrib><creatorcontrib>Wierzbicki, Anna</creatorcontrib><creatorcontrib>Abremski, Kenneth</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hoess, Ronald</au><au>Wierzbicki, Anna</au><au>Abremski, Kenneth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Characterization of Intermediates in Site-Specific Recombination</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-10-01</date><risdate>1987</risdate><volume>84</volume><issue>19</issue><spage>6840</spage><epage>6844</epage><pages>6840-6844</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Cre, the site-specific recombinase from bacteriophage P1, catalyzes a recombination reaction between specific DNA sequences designated as lox sites. The breakage and rejoining of partners during this recombination process must be highly concerted because it has not been possible to detect intermediates of the reaction with wild-type Cre. Several mutant Cre proteins have been isolated that produce significant amounts of a possible intermediate product of the recombination reaction. The product has been identified as a Holliday structure in which one set of the DNA strands of the recombining partners has been exchanged. Wild-type Cre protein is capable of acting on this structure to form recombinant products, which is consistent with this being an intermediate in the recombination reaction. Characterization of the Holliday structure indicated that one set of strands in the recombining partners was always exchanged preferentially before the other set. In addition, it has been found that certain Cre mutants that are unable to carry out recombination in vitro are able to resolve the intermediate. This suggests that these mutants are defective in a step in the reaction that precedes the formation of the Holliday intermediate.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2821547</pmid><doi>10.1073/pnas.84.19.6840</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1987-10, Vol.84 (19), p.6840-6844 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | PubMed Central(OpenAccess); JSTOR Archival Journals and Primary Sources Collection |
| subjects | Bacteriophages Biological and medical sciences Coliphages - genetics Cruciform DNA DNA DNA Nucleotidyltransferases - genetics DNA Nucleotidyltransferases - metabolism DNA Restriction Enzymes DNA, Viral - genetics DNA, Viral - ultrastructure Electron microscopy Enzymes Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gels Genic rearrangement. Recombination. Transposable element Integrases Molecular and cellular biology Molecular genetics Molecules Mutation Plasmids Recombination reactions Recombination, Genetic Topology Viral Proteins |
| title | Isolation and Characterization of Intermediates in Site-Specific Recombination |
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