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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1995-10, Vol.92 (22), p.10393-10397
Hauptverfasser: Baliga, R, Singleton, J W, Dervan, P B
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 10397
container_issue 22
container_start_page 10393
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 92
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
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_40803</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77591067</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2933-4e056287504ade5c1d7f66f510383195fd32d8af41271eb3cfb52641e7a46c8f3</originalsourceid><addsrcrecordid>eNp9kc1v1DAQxS1EVZbCnQvCp4pLFn8ljiUuq0JLpapICM6WY4-3Ro692EkF_32zdKnKpSdr9N5vPDMPoTeUrCmR_MMumbpWbM3YUnPFn6EVJYo2nVDkOVoRwmTTCyZeoJe1_iSEqLYnx-hYCqmkoit0_Q3sZp1j2OY02wh5Cg6wD9GMkKaKh5AcDglPN4DHkHLB25LzLeDsscvzEKGpUzHJgcOfrjev0JE3scLrw3uCfpx__n72pbn6enF5trlqLFOcNwJI27FetkQYB62lTvqu8-2yQ8-par3jzPXGC8okhYFbP7SsExSkEZ3tPT9BH-_77uZhBGeXWYuJelfCaMofnU3Q_ysp3OhtvtWC9IQv-OkBL_nXDHXSY6gWYjQJ8ly1lK2ipJOLkdwbbcm1FvAPX1Ci9wnofQJaMc2Y_pvAgrx9PNoDcDj5or8_6Hvyn_qog_ZzjBP8nhbru6et_A52M5s8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77591067</pqid></control><display><type>article</type><title>RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Baliga, R ; Singleton, J W ; Dervan, P B</creator><creatorcontrib>Baliga, R ; Singleton, J W ; Dervan, P B</creatorcontrib><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.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.22.10393</identifier><identifier>PMID: 7479791</identifier><language>eng</language><publisher>United States: National Acad Sciences</publisher><subject>Adenosine Triphosphate - analogs &amp; 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</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-10, Vol.92 (22), p.10393-10397</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2933-4e056287504ade5c1d7f66f510383195fd32d8af41271eb3cfb52641e7a46c8f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/22.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC40803/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC40803/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7479791$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baliga, R</creatorcontrib><creatorcontrib>Singleton, J W</creatorcontrib><creatorcontrib>Dervan, P B</creatorcontrib><title>RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><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.</description><subject>Adenosine Triphosphate - analogs &amp; 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 &amp; 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>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 1995-10, Vol.92 (22), p.10393-10397
issn 0027-8424
1091-6490
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_40803
source MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T15%3A43%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=RecA.oligonucleotide%20filaments%20bind%20in%20the%20minor%20groove%20of%20double-stranded%20DNA&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Baliga,%20R&rft.date=1995-10-24&rft.volume=92&rft.issue=22&rft.spage=10393&rft.epage=10397&rft.pages=10393-10397&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.92.22.10393&rft_dat=%3Cproquest_pubme%3E77591067%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77591067&rft_id=info:pmid/7479791&rfr_iscdi=true