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...
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Veröffentlicht in: | Trends in cell biology 2010-05, Vol.20 (5), p.269-276 |
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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 |
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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. 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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. 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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 |
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