Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination
During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the...
Gespeichert in:
| Veröffentlicht in: | Nucleic acids research 2016-07, Vol.44 (13), p.6242-6251 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6251 |
|---|---|
| container_issue | 13 |
| container_start_page | 6242 |
| container_title | Nucleic acids research |
| container_volume | 44 |
| creator | Su, Guan-Chin Yeh, Hsin-Yi Lin, Sheng-Wei Chung, Chan-I Huang, Yu-Shan Liu, Yi-Chung Lyu, Ping-Chiang Chi, Peter |
| description | During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the SWI5-SFR1 complex in RAD51-mediated DNA strand exchange, namely, by stabilizing the presynaptic filament and maintaining the catalytically active ATP-bound state of the filament via enhancement of ADP release. In this study, we have strived to determine the basis for physical and functional interactions between Mus musculus SWI5-SFR1 and RAD51. We found that SWI5-SFR1 preferentially associates with the oligomeric form of RAD51. Specifically, a C-terminal domain within SWI5 contributes to RAD51 interaction. With specific RAD51 interaction defective mutants of SWI5-SFR1 that we have isolated, we show that the physical interaction is indispensable for the stimulation of the recombinase activity of RAD51. Our results thus help establish the functional relevance of the trimeric RAD51-SWI5-SFR1 complex and provide insights into the mechanistic underpinnings of homology-directed DNA repair in mammalian cells. |
| doi_str_mv | 10.1093/nar/gkw375 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5291256</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1807890691</sourcerecordid><originalsourceid>FETCH-LOGICAL-c514t-cd8a79159b4182712ce03d20db7894f019148dd2ca3c11396b8b3b9888f367bc3</originalsourceid><addsrcrecordid>eNpVkNFKwzAUhoMobk5vfADppQh1OU3TJjfCmJsOBGFTvAxJmm7VNtGkU3wbn8Uns7IpenUuzsf_n_MhdAz4HDAnQyv9cPn0RnK6g_pAsiROeZbsoj4mmMaAU9ZDByE8Ygwp0HQf9ZIcCOQc99Fo7mrz-eHKqF2ZaD66pBAvHmY0XkznEE1sMI2qTVTZaOUaV7ulW4fIG-0aVVnZVs4eor1S1sEcbecA3U8nd-Pr-Ob2ajYe3cSaQtrGumAy50C5SoF1_Yk2mBQJLlTOeFpi4JCyoki0JBqA8EwxRRRnjJUky5UmA3SxyX1eq8YU2tjWy1o8-6qR_l04WYn_G1utxNK9CppwSGjWBZxuA7x7WZvQiqYK2tS1tKb7SgDD3Sk449ChZxtUexeCN-VvDWDx7Vx0zsXGeQef_D3sF_2RTL4AS399WQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1807890691</pqid></control><display><type>article</type><title>Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Oxford Journals Open Access Collection</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Su, Guan-Chin ; Yeh, Hsin-Yi ; Lin, Sheng-Wei ; Chung, Chan-I ; Huang, Yu-Shan ; Liu, Yi-Chung ; Lyu, Ping-Chiang ; Chi, Peter</creator><creatorcontrib>Su, Guan-Chin ; Yeh, Hsin-Yi ; Lin, Sheng-Wei ; Chung, Chan-I ; Huang, Yu-Shan ; Liu, Yi-Chung ; Lyu, Ping-Chiang ; Chi, Peter</creatorcontrib><description>During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the SWI5-SFR1 complex in RAD51-mediated DNA strand exchange, namely, by stabilizing the presynaptic filament and maintaining the catalytically active ATP-bound state of the filament via enhancement of ADP release. In this study, we have strived to determine the basis for physical and functional interactions between Mus musculus SWI5-SFR1 and RAD51. We found that SWI5-SFR1 preferentially associates with the oligomeric form of RAD51. Specifically, a C-terminal domain within SWI5 contributes to RAD51 interaction. With specific RAD51 interaction defective mutants of SWI5-SFR1 that we have isolated, we show that the physical interaction is indispensable for the stimulation of the recombinase activity of RAD51. Our results thus help establish the functional relevance of the trimeric RAD51-SWI5-SFR1 complex and provide insights into the mechanistic underpinnings of homology-directed DNA repair in mammalian cells.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkw375</identifier><identifier>PMID: 27131790</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; DNA Breaks, Double-Stranded ; DNA Repair - genetics ; DNA Replication - genetics ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Genome Integrity, Repair and ; Homologous Recombination - genetics ; Mice ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - metabolism ; Nuclear Proteins - chemistry ; Nuclear Proteins - metabolism ; Rad51 Recombinase - chemistry ; Rad51 Recombinase - metabolism</subject><ispartof>Nucleic acids research, 2016-07, Vol.44 (13), p.6242-6251</ispartof><rights>The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.</rights><rights>The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-cd8a79159b4182712ce03d20db7894f019148dd2ca3c11396b8b3b9888f367bc3</citedby><cites>FETCH-LOGICAL-c514t-cd8a79159b4182712ce03d20db7894f019148dd2ca3c11396b8b3b9888f367bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291256/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291256/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27131790$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Su, Guan-Chin</creatorcontrib><creatorcontrib>Yeh, Hsin-Yi</creatorcontrib><creatorcontrib>Lin, Sheng-Wei</creatorcontrib><creatorcontrib>Chung, Chan-I</creatorcontrib><creatorcontrib>Huang, Yu-Shan</creatorcontrib><creatorcontrib>Liu, Yi-Chung</creatorcontrib><creatorcontrib>Lyu, Ping-Chiang</creatorcontrib><creatorcontrib>Chi, Peter</creatorcontrib><title>Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the SWI5-SFR1 complex in RAD51-mediated DNA strand exchange, namely, by stabilizing the presynaptic filament and maintaining the catalytically active ATP-bound state of the filament via enhancement of ADP release. In this study, we have strived to determine the basis for physical and functional interactions between Mus musculus SWI5-SFR1 and RAD51. We found that SWI5-SFR1 preferentially associates with the oligomeric form of RAD51. Specifically, a C-terminal domain within SWI5 contributes to RAD51 interaction. With specific RAD51 interaction defective mutants of SWI5-SFR1 that we have isolated, we show that the physical interaction is indispensable for the stimulation of the recombinase activity of RAD51. Our results thus help establish the functional relevance of the trimeric RAD51-SWI5-SFR1 complex and provide insights into the mechanistic underpinnings of homology-directed DNA repair in mammalian cells.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>DNA Breaks, Double-Stranded</subject><subject>DNA Repair - genetics</subject><subject>DNA Replication - genetics</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Genome Integrity, Repair and</subject><subject>Homologous Recombination - genetics</subject><subject>Mice</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - metabolism</subject><subject>Rad51 Recombinase - chemistry</subject><subject>Rad51 Recombinase - metabolism</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkNFKwzAUhoMobk5vfADppQh1OU3TJjfCmJsOBGFTvAxJmm7VNtGkU3wbn8Uns7IpenUuzsf_n_MhdAz4HDAnQyv9cPn0RnK6g_pAsiROeZbsoj4mmMaAU9ZDByE8Ygwp0HQf9ZIcCOQc99Fo7mrz-eHKqF2ZaD66pBAvHmY0XkznEE1sMI2qTVTZaOUaV7ulW4fIG-0aVVnZVs4eor1S1sEcbecA3U8nd-Pr-Ob2ajYe3cSaQtrGumAy50C5SoF1_Yk2mBQJLlTOeFpi4JCyoki0JBqA8EwxRRRnjJUky5UmA3SxyX1eq8YU2tjWy1o8-6qR_l04WYn_G1utxNK9CppwSGjWBZxuA7x7WZvQiqYK2tS1tKb7SgDD3Sk449ChZxtUexeCN-VvDWDx7Vx0zsXGeQef_D3sF_2RTL4AS399WQ</recordid><startdate>20160727</startdate><enddate>20160727</enddate><creator>Su, Guan-Chin</creator><creator>Yeh, Hsin-Yi</creator><creator>Lin, Sheng-Wei</creator><creator>Chung, Chan-I</creator><creator>Huang, Yu-Shan</creator><creator>Liu, Yi-Chung</creator><creator>Lyu, Ping-Chiang</creator><creator>Chi, Peter</creator><general>Oxford University Press</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>20160727</creationdate><title>Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination</title><author>Su, Guan-Chin ; Yeh, Hsin-Yi ; Lin, Sheng-Wei ; Chung, Chan-I ; Huang, Yu-Shan ; Liu, Yi-Chung ; Lyu, Ping-Chiang ; Chi, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-cd8a79159b4182712ce03d20db7894f019148dd2ca3c11396b8b3b9888f367bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>DNA Breaks, Double-Stranded</topic><topic>DNA Repair - genetics</topic><topic>DNA Replication - genetics</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Genome Integrity, Repair and</topic><topic>Homologous Recombination - genetics</topic><topic>Mice</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - metabolism</topic><topic>Rad51 Recombinase - chemistry</topic><topic>Rad51 Recombinase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Su, Guan-Chin</creatorcontrib><creatorcontrib>Yeh, Hsin-Yi</creatorcontrib><creatorcontrib>Lin, Sheng-Wei</creatorcontrib><creatorcontrib>Chung, Chan-I</creatorcontrib><creatorcontrib>Huang, Yu-Shan</creatorcontrib><creatorcontrib>Liu, Yi-Chung</creatorcontrib><creatorcontrib>Lyu, Ping-Chiang</creatorcontrib><creatorcontrib>Chi, Peter</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>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Su, Guan-Chin</au><au>Yeh, Hsin-Yi</au><au>Lin, Sheng-Wei</au><au>Chung, Chan-I</au><au>Huang, Yu-Shan</au><au>Liu, Yi-Chung</au><au>Lyu, Ping-Chiang</au><au>Chi, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2016-07-27</date><risdate>2016</risdate><volume>44</volume><issue>13</issue><spage>6242</spage><epage>6251</epage><pages>6242-6251</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the SWI5-SFR1 complex in RAD51-mediated DNA strand exchange, namely, by stabilizing the presynaptic filament and maintaining the catalytically active ATP-bound state of the filament via enhancement of ADP release. In this study, we have strived to determine the basis for physical and functional interactions between Mus musculus SWI5-SFR1 and RAD51. We found that SWI5-SFR1 preferentially associates with the oligomeric form of RAD51. Specifically, a C-terminal domain within SWI5 contributes to RAD51 interaction. With specific RAD51 interaction defective mutants of SWI5-SFR1 that we have isolated, we show that the physical interaction is indispensable for the stimulation of the recombinase activity of RAD51. Our results thus help establish the functional relevance of the trimeric RAD51-SWI5-SFR1 complex and provide insights into the mechanistic underpinnings of homology-directed DNA repair in mammalian cells.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>27131790</pmid><doi>10.1093/nar/gkw375</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0305-1048 |
| ispartof | Nucleic acids research, 2016-07, Vol.44 (13), p.6242-6251 |
| issn | 0305-1048 1362-4962 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5291256 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Oxford Journals Open Access Collection; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphate - metabolism Animals DNA Breaks, Double-Stranded DNA Repair - genetics DNA Replication - genetics DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Genome Integrity, Repair and Homologous Recombination - genetics Mice Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Nuclear Proteins - chemistry Nuclear Proteins - metabolism Rad51 Recombinase - chemistry Rad51 Recombinase - metabolism |
| title | Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T04%3A48%3A06IST&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=Role%C2%A0of%20the%20RAD51-SWI5-SFR1%20Ensemble%20in%20homologous%20recombination&rft.jtitle=Nucleic%20acids%20research&rft.au=Su,%20Guan-Chin&rft.date=2016-07-27&rft.volume=44&rft.issue=13&rft.spage=6242&rft.epage=6251&rft.pages=6242-6251&rft.issn=0305-1048&rft.eissn=1362-4962&rft_id=info:doi/10.1093/nar/gkw375&rft_dat=%3Cproquest_pubme%3E1807890691%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=1807890691&rft_id=info:pmid/27131790&rfr_iscdi=true |