Single-molecule imaging brings Rad51 nucleoprotein filaments into focus

The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro , Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innova...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Trends in cell biology 2010-05, Vol.20 (5), p.269-276
Hauptverfasser: Forget, Anthony L, Kowalczykowski, Stephen C
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 276
container_issue 5
container_start_page 269
container_title Trends in cell biology
container_volume 20
creator Forget, Anthony L
Kowalczykowski, Stephen C
description The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro , Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynamic nature of this filament and its cellular function. The assembly and disassembly of Rad51 nucleoprotein filaments is seen to be regulated by recombination accessory proteins. In this regard, the BRC repeats of the BRCA2 protein were shown to modulate the DNA binding selectivity of Rad51. Furthermore, single-molecule studies explained the need for a DNA translocase, Rad54 protein, in the disassembly of Rad51 double-stranded DNA filaments.
doi_str_mv 10.1016/j.tcb.2010.02.004
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2862779</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>1_s2_0_S0962892410000371</els_id><sourcerecordid>746005678</sourcerecordid><originalsourceid>FETCH-LOGICAL-c537t-296b0bfa7b8a2c23fac97b53e7cf9f593b3080598ae59770f7ec6839a26db0003</originalsourceid><addsrcrecordid>eNqFUl1rFDEUDWKxa_UH-CLz5tNsb5KdyQShIKXWQkHox3NIMnfWrJlkTWYK_fdm2FrUB33JJbnnHE7uuYS8o7CmQNvT3XqyZs2g3IGtATYvyIp2QtYcuu4lWYFsWd1Jtjkmr3PeAYBglL8ixwyYlIzRFbm8dWHrsR6jRzt7rNyot-WpMqmcubrRfUOrMFuPcZ_ihC5Ug_N6xDDlyoUpVkO0c35DjgbtM759qifk_vPF3fmX-vrr5dX5p-vaNlxMNZOtATNoYTrNLOODtlKYhqOwgxwayU2xDo3sNDZSCBgE2rbjUrO2N8U_PyFnB939bEbsbbGRtFf7VHynRxW1U392gvumtvFBsa5lQsgi8OFJIMUfM-ZJjS5b9F4HjHNWYtMCNK3o_o_kXHLJmsUUPSBtijknHJ79UFBLUmqnSlJqSUoBUyWpwnn_-0eeGb-iKYCPBwCWcT44TCpbh8Fi7xLaSfXR_VP-7C-29S44q_13fMS8i3MKJSdFVS4EdbusyrIpFJYpC8p_ArMWuWs</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733939250</pqid></control><display><type>article</type><title>Single-molecule imaging brings Rad51 nucleoprotein filaments into focus</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Forget, Anthony L ; Kowalczykowski, Stephen C</creator><creatorcontrib>Forget, Anthony L ; Kowalczykowski, Stephen C</creatorcontrib><description>The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro , Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynamic nature of this filament and its cellular function. The assembly and disassembly of Rad51 nucleoprotein filaments is seen to be regulated by recombination accessory proteins. In this regard, the BRC repeats of the BRCA2 protein were shown to modulate the DNA binding selectivity of Rad51. Furthermore, single-molecule studies explained the need for a DNA translocase, Rad54 protein, in the disassembly of Rad51 double-stranded DNA filaments.</description><identifier>ISSN: 0962-8924</identifier><identifier>EISSN: 1879-3088</identifier><identifier>DOI: 10.1016/j.tcb.2010.02.004</identifier><identifier>PMID: 20299221</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; DNA - genetics ; DNA - metabolism ; DNA Repair ; DNA, Single-Stranded - genetics ; DNA, Single-Stranded - metabolism ; Humans ; Nucleoproteins - metabolism ; Optical Tweezers ; Pathology ; Protein Binding ; Rad51 Recombinase - metabolism ; Recombination, Genetic</subject><ispartof>Trends in cell biology, 2010-05, Vol.20 (5), p.269-276</ispartof><rights>Elsevier Ltd</rights><rights>2010 Elsevier Ltd</rights><rights>Copyright 2010 Elsevier Ltd. All rights reserved.</rights><rights>2010 Elsevier Ltd. All rights reserved. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c537t-296b0bfa7b8a2c23fac97b53e7cf9f593b3080598ae59770f7ec6839a26db0003</citedby><cites>FETCH-LOGICAL-c537t-296b0bfa7b8a2c23fac97b53e7cf9f593b3080598ae59770f7ec6839a26db0003</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0962892410000371$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20299221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Forget, Anthony L</creatorcontrib><creatorcontrib>Kowalczykowski, Stephen C</creatorcontrib><title>Single-molecule imaging brings Rad51 nucleoprotein filaments into focus</title><title>Trends in cell biology</title><addtitle>Trends Cell Biol</addtitle><description>The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro , Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynamic nature of this filament and its cellular function. The assembly and disassembly of Rad51 nucleoprotein filaments is seen to be regulated by recombination accessory proteins. In this regard, the BRC repeats of the BRCA2 protein were shown to modulate the DNA binding selectivity of Rad51. Furthermore, single-molecule studies explained the need for a DNA translocase, Rad54 protein, in the disassembly of Rad51 double-stranded DNA filaments.</description><subject>Animals</subject><subject>DNA - genetics</subject><subject>DNA - metabolism</subject><subject>DNA Repair</subject><subject>DNA, Single-Stranded - genetics</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>Humans</subject><subject>Nucleoproteins - metabolism</subject><subject>Optical Tweezers</subject><subject>Pathology</subject><subject>Protein Binding</subject><subject>Rad51 Recombinase - metabolism</subject><subject>Recombination, Genetic</subject><issn>0962-8924</issn><issn>1879-3088</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUl1rFDEUDWKxa_UH-CLz5tNsb5KdyQShIKXWQkHox3NIMnfWrJlkTWYK_fdm2FrUB33JJbnnHE7uuYS8o7CmQNvT3XqyZs2g3IGtATYvyIp2QtYcuu4lWYFsWd1Jtjkmr3PeAYBglL8ixwyYlIzRFbm8dWHrsR6jRzt7rNyot-WpMqmcubrRfUOrMFuPcZ_ihC5Ug_N6xDDlyoUpVkO0c35DjgbtM759qifk_vPF3fmX-vrr5dX5p-vaNlxMNZOtATNoYTrNLOODtlKYhqOwgxwayU2xDo3sNDZSCBgE2rbjUrO2N8U_PyFnB939bEbsbbGRtFf7VHynRxW1U392gvumtvFBsa5lQsgi8OFJIMUfM-ZJjS5b9F4HjHNWYtMCNK3o_o_kXHLJmsUUPSBtijknHJ79UFBLUmqnSlJqSUoBUyWpwnn_-0eeGb-iKYCPBwCWcT44TCpbh8Fi7xLaSfXR_VP-7C-29S44q_13fMS8i3MKJSdFVS4EdbusyrIpFJYpC8p_ArMWuWs</recordid><startdate>20100501</startdate><enddate>20100501</enddate><creator>Forget, Anthony L</creator><creator>Kowalczykowski, Stephen C</creator><general>Elsevier Ltd</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>7TM</scope><scope>5PM</scope></search><sort><creationdate>20100501</creationdate><title>Single-molecule imaging brings Rad51 nucleoprotein filaments into focus</title><author>Forget, Anthony L ; Kowalczykowski, Stephen C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-296b0bfa7b8a2c23fac97b53e7cf9f593b3080598ae59770f7ec6839a26db0003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>DNA - genetics</topic><topic>DNA - metabolism</topic><topic>DNA Repair</topic><topic>DNA, Single-Stranded - genetics</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>Humans</topic><topic>Nucleoproteins - metabolism</topic><topic>Optical Tweezers</topic><topic>Pathology</topic><topic>Protein Binding</topic><topic>Rad51 Recombinase - metabolism</topic><topic>Recombination, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Forget, Anthony L</creatorcontrib><creatorcontrib>Kowalczykowski, Stephen C</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>Nucleic Acids Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Trends in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Forget, Anthony L</au><au>Kowalczykowski, Stephen C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Single-molecule imaging brings Rad51 nucleoprotein filaments into focus</atitle><jtitle>Trends in cell biology</jtitle><addtitle>Trends Cell Biol</addtitle><date>2010-05-01</date><risdate>2010</risdate><volume>20</volume><issue>5</issue><spage>269</spage><epage>276</epage><pages>269-276</pages><issn>0962-8924</issn><eissn>1879-3088</eissn><abstract>The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro , Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynamic nature of this filament and its cellular function. The assembly and disassembly of Rad51 nucleoprotein filaments is seen to be regulated by recombination accessory proteins. In this regard, the BRC repeats of the BRCA2 protein were shown to modulate the DNA binding selectivity of Rad51. Furthermore, single-molecule studies explained the need for a DNA translocase, Rad54 protein, in the disassembly of Rad51 double-stranded DNA filaments.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>20299221</pmid><doi>10.1016/j.tcb.2010.02.004</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0962-8924
ispartof Trends in cell biology, 2010-05, Vol.20 (5), p.269-276
issn 0962-8924
1879-3088
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2862779
source MEDLINE; Elsevier ScienceDirect Journals Complete
subjects Animals
DNA - genetics
DNA - metabolism
DNA Repair
DNA, Single-Stranded - genetics
DNA, Single-Stranded - metabolism
Humans
Nucleoproteins - metabolism
Optical Tweezers
Pathology
Protein Binding
Rad51 Recombinase - metabolism
Recombination, Genetic
title Single-molecule imaging brings Rad51 nucleoprotein filaments into focus
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T17%3A12%3A58IST&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=Single-molecule%20imaging%20brings%20Rad51%20nucleoprotein%20filaments%20into%20focus&rft.jtitle=Trends%20in%20cell%20biology&rft.au=Forget,%20Anthony%20L&rft.date=2010-05-01&rft.volume=20&rft.issue=5&rft.spage=269&rft.epage=276&rft.pages=269-276&rft.issn=0962-8924&rft.eissn=1879-3088&rft_id=info:doi/10.1016/j.tcb.2010.02.004&rft_dat=%3Cproquest_pubme%3E746005678%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=733939250&rft_id=info:pmid/20299221&rft_els_id=1_s2_0_S0962892410000371&rfr_iscdi=true