RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA
Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[gamma-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this bi...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-10, Vol.92 (22), p.10393-10397 |
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creator | Baliga, R Singleton, J W Dervan, P B |
description | Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[gamma-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA.Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nucleoprotein filament binds in the minor groove of an extended Watson-Crick duplex. |
doi_str_mv | 10.1073/pnas.92.22.10393 |
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The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA.Fe (T*) into the oligonucleotide part of the filament. 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The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA.Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nucleoprotein filament binds in the minor groove of an extended Watson-Crick duplex.</description><subject>Adenosine Triphosphate - analogs & derivatives</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Base Sequence</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - metabolism</subject><subject>Models, Genetic</subject><subject>Models, Structural</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Oligodeoxyribonucleotides</subject><subject>Plasmids - chemistry</subject><subject>Plasmids - metabolism</subject><subject>Rec A Recombinases - chemistry</subject><subject>Rec A Recombinases - metabolism</subject><subject>Restriction Mapping</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1v1DAQxS1EVZbCnQvCp4pLFn8ljiUuq0JLpapICM6WY4-3Ro692EkF_32zdKnKpSdr9N5vPDMPoTeUrCmR_MMumbpWbM3YUnPFn6EVJYo2nVDkOVoRwmTTCyZeoJe1_iSEqLYnx-hYCqmkoit0_Q3sZp1j2OY02wh5Cg6wD9GMkKaKh5AcDglPN4DHkHLB25LzLeDsscvzEKGpUzHJgcOfrjev0JE3scLrw3uCfpx__n72pbn6enF5trlqLFOcNwJI27FetkQYB62lTvqu8-2yQ8-par3jzPXGC8okhYFbP7SsExSkEZ3tPT9BH-_77uZhBGeXWYuJelfCaMofnU3Q_ysp3OhtvtWC9IQv-OkBL_nXDHXSY6gWYjQJ8ly1lK2ipJOLkdwbbcm1FvAPX1Ci9wnofQJaMc2Y_pvAgrx9PNoDcDj5or8_6Hvyn_qog_ZzjBP8nhbru6et_A52M5s8</recordid><startdate>19951024</startdate><enddate>19951024</enddate><creator>Baliga, R</creator><creator>Singleton, J W</creator><creator>Dervan, P B</creator><general>National Acad Sciences</general><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>19951024</creationdate><title>RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA</title><author>Baliga, R ; Singleton, J W ; Dervan, P B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2933-4e056287504ade5c1d7f66f510383195fd32d8af41271eb3cfb52641e7a46c8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine Triphosphate - analogs & derivatives</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Base Sequence</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - metabolism</topic><topic>Models, Genetic</topic><topic>Models, Structural</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Oligodeoxyribonucleotides</topic><topic>Plasmids - chemistry</topic><topic>Plasmids - metabolism</topic><topic>Rec A Recombinases - chemistry</topic><topic>Rec A Recombinases - metabolism</topic><topic>Restriction Mapping</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baliga, R</creatorcontrib><creatorcontrib>Singleton, J W</creatorcontrib><creatorcontrib>Dervan, P B</creatorcontrib><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>Baliga, R</au><au>Singleton, J W</au><au>Dervan, P B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-10-24</date><risdate>1995</risdate><volume>92</volume><issue>22</issue><spage>10393</spage><epage>10397</epage><pages>10393-10397</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[gamma-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA.Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nucleoprotein filament binds in the minor groove of an extended Watson-Crick duplex.</abstract><cop>United States</cop><pub>National Acad Sciences</pub><pmid>7479791</pmid><doi>10.1073/pnas.92.22.10393</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Base Sequence DNA - chemistry DNA - metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Models, Genetic Models, Structural Molecular Sequence Data Nucleic Acid Conformation Oligodeoxyribonucleotides Plasmids - chemistry Plasmids - metabolism Rec A Recombinases - chemistry Rec A Recombinases - metabolism Restriction Mapping |
title | RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA |
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