Protein-protein interactions in a higher-order structure direct lambda site-specific recombination
The highly directional site-specific recombination of bacteriophage lambda is tightly regulated by the binding of three different proteins to a complex array of sites. The manner in which these reactions are both stimulated and inhibited by co-operative binding of proteins to specific sites on the P...
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| Veröffentlicht in: | Journal of molecular biology 1987-06, Vol.195 (3), p.481-493 |
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| container_end_page | 493 |
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| container_title | Journal of molecular biology |
| container_volume | 195 |
| creator | Thompson, John F. de Vargas, Lina Moitoso Skinner, Sarah E. Landy, Arthur |
| description | The highly directional site-specific recombination of bacteriophage lambda is tightly regulated by the binding of three different proteins to a complex array of sites. The manner in which these reactions are both stimulated and inhibited by co-operative binding of proteins to specific sites on the P arm of
attP and
attR has been elucidated by correlation of nuclease protection with recombination studies of both wild-type and mutant DNAs. In addition to co-operative forces, there is a specific competitive interaction that allows the protein-DNA complex to serve as a “biological switch”. This switch does not depend upon the simple occlusion of DNA binding sites by neighboring proteins; but, rather, the outcome of this competition is dependent on long-range interactions that vary between the higher-order structures of
attP and
attR. These higher-order structures are dependent on co-operative interactions involving three proteins binding to five or more sites. |
| doi_str_mv | 10.1016/0022-2836(87)90177-X |
| format | Article |
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attP and
attR has been elucidated by correlation of nuclease protection with recombination studies of both wild-type and mutant DNAs. In addition to co-operative forces, there is a specific competitive interaction that allows the protein-DNA complex to serve as a “biological switch”. This switch does not depend upon the simple occlusion of DNA binding sites by neighboring proteins; but, rather, the outcome of this competition is dependent on long-range interactions that vary between the higher-order structures of
attP and
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attP and
attR has been elucidated by correlation of nuclease protection with recombination studies of both wild-type and mutant DNAs. In addition to co-operative forces, there is a specific competitive interaction that allows the protein-DNA complex to serve as a “biological switch”. This switch does not depend upon the simple occlusion of DNA binding sites by neighboring proteins; but, rather, the outcome of this competition is dependent on long-range interactions that vary between the higher-order structures of
attP and
attR. These higher-order structures are dependent on co-operative interactions involving three proteins binding to five or more sites.</description><subject>Allosteric Site</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriophage lambda - genetics</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>DNA, Recombinant - metabolism</subject><subject>DNA, Viral - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>Integration Host Factors</subject><subject>Microbiology</subject><subject>Mutation</subject><subject>Viral Core Proteins - metabolism</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rFTEUhoMo9bb6DxRmIaKLaD4mH7MRpFgrFOpCobuQOXNiI_NxTTIF_725zuUuuzqE9zkvOQ8hrzj7wBnXHxkTggor9Ttr3neMG0PvnpAdZ7ajVkv7lOxOyHNynvNvxpiSrT0jZ6JTFZE70n9PS8E40_02mzgXTB5KXOZcH41v7uOve0x0SQOmJpe0QlkTNkNMCKUZ_dQPvsmxIM17hBgiNDVZpj7O_lDzgjwLfsz48jgvyM-rLz8ur-nN7ddvl59vKEirC-V2kK3EXurQBYReBQDmbae0McCUQTDMy05CEFbxVgWlpbG87bQVSnsmL8jbrbee8mfFXNwUM-A4-hmXNTvLmai8qGC7gZCWnBMGt09x8umv48wd1LqDN3fw5qxx_9W6u7r2-ti_9hMOp6Wjy5q_OeY-gx9D8jPEfMKssJ0QXcU-bRhWFw8Rk8sQcQbchLphiY__4x-WNZYj</recordid><startdate>19870605</startdate><enddate>19870605</enddate><creator>Thompson, John F.</creator><creator>de Vargas, Lina Moitoso</creator><creator>Skinner, Sarah E.</creator><creator>Landy, Arthur</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>19870605</creationdate><title>Protein-protein interactions in a higher-order structure direct lambda site-specific recombination</title><author>Thompson, John F. ; de Vargas, Lina Moitoso ; Skinner, Sarah E. ; Landy, Arthur</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-18d343eb36f9fecb5fcc0a895677c057ec70a393cf285145f5637814968256a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Allosteric Site</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriophage lambda - genetics</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>DNA, Recombinant - metabolism</topic><topic>DNA, Viral - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics</topic><topic>Integration Host Factors</topic><topic>Microbiology</topic><topic>Mutation</topic><topic>Viral Core Proteins - metabolism</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thompson, John F.</creatorcontrib><creatorcontrib>de Vargas, Lina Moitoso</creatorcontrib><creatorcontrib>Skinner, Sarah E.</creatorcontrib><creatorcontrib>Landy, Arthur</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>Thompson, John F.</au><au>de Vargas, Lina Moitoso</au><au>Skinner, Sarah E.</au><au>Landy, Arthur</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein-protein interactions in a higher-order structure direct lambda site-specific recombination</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1987-06-05</date><risdate>1987</risdate><volume>195</volume><issue>3</issue><spage>481</spage><epage>493</epage><pages>481-493</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The highly directional site-specific recombination of bacteriophage lambda is tightly regulated by the binding of three different proteins to a complex array of sites. The manner in which these reactions are both stimulated and inhibited by co-operative binding of proteins to specific sites on the P arm of
attP and
attR has been elucidated by correlation of nuclease protection with recombination studies of both wild-type and mutant DNAs. In addition to co-operative forces, there is a specific competitive interaction that allows the protein-DNA complex to serve as a “biological switch”. This switch does not depend upon the simple occlusion of DNA binding sites by neighboring proteins; but, rather, the outcome of this competition is dependent on long-range interactions that vary between the higher-order structures of
attP and
attR. These higher-order structures are dependent on co-operative interactions involving three proteins binding to five or more sites.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>2958633</pmid><doi>10.1016/0022-2836(87)90177-X</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1987-06, Vol.195 (3), p.481-493 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81028142 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Allosteric Site Bacterial Proteins - metabolism Bacteriophage lambda - genetics Binding Sites Biological and medical sciences DNA, Recombinant - metabolism DNA, Viral - metabolism DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Genetics Integration Host Factors Microbiology Mutation Viral Core Proteins - metabolism Viral Proteins - metabolism Virology |
| title | Protein-protein interactions in a higher-order structure direct lambda site-specific recombination |
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