Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells
Homologous recombinational repair of DNA double-strand breaks and crosslinks in human cells is likely to require Rad51 and the five Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3), as has been shown in chicken and rodent cells. Previously, we reported on the interact...
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| Veröffentlicht in: | Nucleic acids research 2002-02, Vol.30 (4), p.1001-1008 |
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| creator | Wiese, Claudia Collins, David W. Albala, Joanna S. Thompson, Larry H. Kronenberg, Amy Schild, David Chatterjee, A. |
| description | Homologous recombinational repair of DNA double-strand breaks and crosslinks in human cells is likely to require Rad51 and the five Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3), as has been shown in chicken and rodent cells. Previously, we reported on the interactions among these proteins using baculovirus and two- and three-hybrid yeast systems. To test for interactions involving XRCC3 and Rad51C, stable human cell lines have been isolated that express (His)6-tagged versions of XRCC3 or Rad51C. Ni2+-binding experiments demonstrate that XRCC3 and Rad51C interact in human cells. In addition, we find that Rad51C, but not XRCC3, interacts directly or indirectly with Rad51B, Rad51D and XRCC2. These results argue that there are at least two complexes of Rad51 paralogs in human cells (Rad51C-XRCC3 and Rad51B-Rad51C-Rad51D-XRCC2), both containing Rad51C. Moreover, Rad51 is not found in these complexes. X-ray treatment did not alter either the level of any Rad51 paralog or the observed interactions between paralogs. However, the endogenous level of Rad51C is moderately elevated in the XRCC3-overexpressing cell line, suggesting that dimerization between these proteins might help stabilize Rad51C. |
| doi_str_mv | 10.1093/nar/30.4.1001 |
| format | Article |
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Previously, we reported on the interactions among these proteins using baculovirus and two- and three-hybrid yeast systems. To test for interactions involving XRCC3 and Rad51C, stable human cell lines have been isolated that express (His)6-tagged versions of XRCC3 or Rad51C. Ni2+-binding experiments demonstrate that XRCC3 and Rad51C interact in human cells. In addition, we find that Rad51C, but not XRCC3, interacts directly or indirectly with Rad51B, Rad51D and XRCC2. These results argue that there are at least two complexes of Rad51 paralogs in human cells (Rad51C-XRCC3 and Rad51B-Rad51C-Rad51D-XRCC2), both containing Rad51C. Moreover, Rad51 is not found in these complexes. X-ray treatment did not alter either the level of any Rad51 paralog or the observed interactions between paralogs. However, the endogenous level of Rad51C is moderately elevated in the XRCC3-overexpressing cell line, suggesting that dimerization between these proteins might help stabilize Rad51C.</description><identifier>ISSN: 0305-1048</identifier><identifier>ISSN: 1362-4962</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/30.4.1001</identifier><identifier>PMID: 11842112</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>Legacy CDMS: Oxford Publishing Limited (England)</publisher><subject>Avian Proteins ; Cell Death ; Cell Line ; DNA Damage ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; DNA-Binding Proteins - physiology ; Humans ; Kinetics ; Life Sciences (General) ; Lymphocytes - metabolism ; Lymphocytes - radiation effects ; Macromolecular Substances ; Models, Biological ; Precipitin Tests ; Rad51 protein ; Rad51 Recombinase ; Rad51B protein ; Rad51C protein ; Rad51D protein ; Recombinant Fusion Proteins - metabolism ; Space life sciences ; Transfection ; X-Rays ; XRCC3 protein</subject><ispartof>Nucleic acids research, 2002-02, Vol.30 (4), p.1001-1008</ispartof><rights>Copyright Oxford University Press(England) Feb 15, 2002</rights><rights>Copyright © 2002 Oxford University Press 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c527t-eda88a7904fcb55cc702ebfa540b43c68b84729f01415d73f36bdbb82f63ffdb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC100332/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC100332/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11842112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wiese, Claudia</creatorcontrib><creatorcontrib>Collins, David W.</creatorcontrib><creatorcontrib>Albala, Joanna S.</creatorcontrib><creatorcontrib>Thompson, Larry H.</creatorcontrib><creatorcontrib>Kronenberg, Amy</creatorcontrib><creatorcontrib>Schild, David</creatorcontrib><creatorcontrib>Chatterjee, A.</creatorcontrib><title>Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Homologous recombinational repair of DNA double-strand breaks and crosslinks in human cells is likely to require Rad51 and the five Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3), as has been shown in chicken and rodent cells. Previously, we reported on the interactions among these proteins using baculovirus and two- and three-hybrid yeast systems. To test for interactions involving XRCC3 and Rad51C, stable human cell lines have been isolated that express (His)6-tagged versions of XRCC3 or Rad51C. Ni2+-binding experiments demonstrate that XRCC3 and Rad51C interact in human cells. In addition, we find that Rad51C, but not XRCC3, interacts directly or indirectly with Rad51B, Rad51D and XRCC2. These results argue that there are at least two complexes of Rad51 paralogs in human cells (Rad51C-XRCC3 and Rad51B-Rad51C-Rad51D-XRCC2), both containing Rad51C. Moreover, Rad51 is not found in these complexes. X-ray treatment did not alter either the level of any Rad51 paralog or the observed interactions between paralogs. However, the endogenous level of Rad51C is moderately elevated in the XRCC3-overexpressing cell line, suggesting that dimerization between these proteins might help stabilize Rad51C.</description><subject>Avian Proteins</subject><subject>Cell Death</subject><subject>Cell Line</subject><subject>DNA Damage</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>DNA-Binding Proteins - physiology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Life Sciences (General)</subject><subject>Lymphocytes - metabolism</subject><subject>Lymphocytes - radiation effects</subject><subject>Macromolecular Substances</subject><subject>Models, Biological</subject><subject>Precipitin Tests</subject><subject>Rad51 protein</subject><subject>Rad51 Recombinase</subject><subject>Rad51B protein</subject><subject>Rad51C protein</subject><subject>Rad51D protein</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Space life sciences</subject><subject>Transfection</subject><subject>X-Rays</subject><subject>XRCC3 protein</subject><issn>0305-1048</issn><issn>1362-4962</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNqFkclr3DAUh0VJSSbLsbdSTA-5OXnabPmQQzBZBgKF0EBvQpKlGQePNJXsgf730Sw0bS89iYe-J_0WhD5huMLQ0Guv4jWFK5YnwB_QDNOKlKypyBGaAQVeYmDiBJ2m9JoBhjk7RicYC0YwJjM0n_vRRmXGPvhU9H4Thk3vF8W4tMWz6jgu1iqqISzSfmwL5bvix3Pb0kwXy2mlfGHsMKRz9NGpIdmLw3mGXu7vvreP5dO3h3l7-1QaTuqxtJ0SQtUNMGc058bUQKx2ijPQjJpKaMFq0rid1q6mjla601oQV1HnOk3P0M3-3fWkV7Yz1o9ZoFzHfqXiLxlUL_--8f1SLsJG5oAoJXn_8rAfw8_JplGu-rR1oLwNU5I1ZpxWUP0XxIIIWjdNBr_-A76GKfocgiQAXGRrPEPlHjIxpBSt-60Yg9w2KXOTkoJkW6E481_-tPlOH6rLwOc94FVSMlvd_cYARA4Q6Bsg3KEg</recordid><startdate>20020215</startdate><enddate>20020215</enddate><creator>Wiese, Claudia</creator><creator>Collins, David W.</creator><creator>Albala, Joanna S.</creator><creator>Thompson, Larry H.</creator><creator>Kronenberg, Amy</creator><creator>Schild, David</creator><creator>Chatterjee, A.</creator><general>Oxford Publishing Limited (England)</general><general>Oxford University Press</general><scope>CYE</scope><scope>CYI</scope><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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020215</creationdate><title>Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells</title><author>Wiese, Claudia ; Collins, David W. ; Albala, Joanna S. ; Thompson, Larry H. ; Kronenberg, Amy ; Schild, David ; Chatterjee, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c527t-eda88a7904fcb55cc702ebfa540b43c68b84729f01415d73f36bdbb82f63ffdb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Avian Proteins</topic><topic>Cell Death</topic><topic>Cell Line</topic><topic>DNA Damage</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>DNA-Binding Proteins - physiology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Life Sciences (General)</topic><topic>Lymphocytes - metabolism</topic><topic>Lymphocytes - radiation effects</topic><topic>Macromolecular Substances</topic><topic>Models, Biological</topic><topic>Precipitin Tests</topic><topic>Rad51 protein</topic><topic>Rad51 Recombinase</topic><topic>Rad51B protein</topic><topic>Rad51C protein</topic><topic>Rad51D protein</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Space life sciences</topic><topic>Transfection</topic><topic>X-Rays</topic><topic>XRCC3 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wiese, Claudia</creatorcontrib><creatorcontrib>Collins, David W.</creatorcontrib><creatorcontrib>Albala, Joanna S.</creatorcontrib><creatorcontrib>Thompson, Larry H.</creatorcontrib><creatorcontrib>Kronenberg, Amy</creatorcontrib><creatorcontrib>Schild, David</creatorcontrib><creatorcontrib>Chatterjee, A.</creatorcontrib><collection>NASA Scientific and Technical Information</collection><collection>NASA Technical Reports Server</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Wiese, Claudia</au><au>Collins, David W.</au><au>Albala, Joanna S.</au><au>Thompson, Larry H.</au><au>Kronenberg, Amy</au><au>Schild, David</au><au>Chatterjee, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2002-02-15</date><risdate>2002</risdate><volume>30</volume><issue>4</issue><spage>1001</spage><epage>1008</epage><pages>1001-1008</pages><issn>0305-1048</issn><issn>1362-4962</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>Homologous recombinational repair of DNA double-strand breaks and crosslinks in human cells is likely to require Rad51 and the five Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3), as has been shown in chicken and rodent cells. Previously, we reported on the interactions among these proteins using baculovirus and two- and three-hybrid yeast systems. To test for interactions involving XRCC3 and Rad51C, stable human cell lines have been isolated that express (His)6-tagged versions of XRCC3 or Rad51C. Ni2+-binding experiments demonstrate that XRCC3 and Rad51C interact in human cells. In addition, we find that Rad51C, but not XRCC3, interacts directly or indirectly with Rad51B, Rad51D and XRCC2. These results argue that there are at least two complexes of Rad51 paralogs in human cells (Rad51C-XRCC3 and Rad51B-Rad51C-Rad51D-XRCC2), both containing Rad51C. Moreover, Rad51 is not found in these complexes. X-ray treatment did not alter either the level of any Rad51 paralog or the observed interactions between paralogs. However, the endogenous level of Rad51C is moderately elevated in the XRCC3-overexpressing cell line, suggesting that dimerization between these proteins might help stabilize Rad51C.</abstract><cop>Legacy CDMS</cop><pub>Oxford Publishing Limited (England)</pub><pmid>11842112</pmid><doi>10.1093/nar/30.4.1001</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 2002-02, Vol.30 (4), p.1001-1008 |
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| source | MEDLINE; Oxford Journals Open Access Collection; NASA Technical Reports Server; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Avian Proteins Cell Death Cell Line DNA Damage DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology Humans Kinetics Life Sciences (General) Lymphocytes - metabolism Lymphocytes - radiation effects Macromolecular Substances Models, Biological Precipitin Tests Rad51 protein Rad51 Recombinase Rad51B protein Rad51C protein Rad51D protein Recombinant Fusion Proteins - metabolism Space life sciences Transfection X-Rays XRCC3 protein |
| title | Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells |
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