Xrs2 facilitates crossovers during DNA double-strand gap repair in yeast
Xrs2 is a member of the MRX complex (Mre11/Rad50/Xrs2) in Saccharomyces cerevisiae. In this study we demonstrate the important role of the MRX complex and in more detail of Xrs2 for the repair of radiation-induced chromosomal double-strand breaks by pulsed field gel electrophoresis. By using a newly...
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| Veröffentlicht in: | DNA repair 2008-09, Vol.7 (9), p.1563-1577 |
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| creator | Steininger, Sylvia Gomez-Paramio, Idoia Braselmann, Herbert Fellerhoff, Barbara Dittberner, Daniela Eckardt-Schupp, Friederike Moertl, Simone |
| description | Xrs2 is a member of the MRX complex (Mre11/Rad50/Xrs2) in
Saccharomyces cerevisiae. In this study we demonstrate the important role of the MRX complex and in more detail of Xrs2 for the repair of radiation-induced chromosomal double-strand breaks by pulsed field gel electrophoresis. By using a newly designed
in vivo plasmid–chromosome recombination system, we could show that gap repair efficiency and the association with crossovers were reduced in the MRX null mutants, but repair accuracy was unaffected. For these processes, an intact Mre11-binding domain of Xrs2 is crucial, whereas the FHA- and BRCT-domains as well as the Tel1-binding domain of Xrs2 are dispensable. Obviously, the Mre11-binding domain of the Xrs2 protein is crucial for the analysed functions and our results suggest a new role of the MRX complex for the formation of crossovers. Analysis of double mutants showed that the phenotype of the
Δxrs2 null mutant concerning the crossover frequency is dominant over the phenotypes of
Δsrs2 and
Δsgs1 null mutants. Thus, the complex seems to be involved in early steps of double-strand break and gap repair, and we propose that it has a regulatory role for the selection of homologous recombination pathways. |
| doi_str_mv | 10.1016/j.dnarep.2008.06.004 |
| format | Article |
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Saccharomyces cerevisiae. In this study we demonstrate the important role of the MRX complex and in more detail of Xrs2 for the repair of radiation-induced chromosomal double-strand breaks by pulsed field gel electrophoresis. By using a newly designed
in vivo plasmid–chromosome recombination system, we could show that gap repair efficiency and the association with crossovers were reduced in the MRX null mutants, but repair accuracy was unaffected. For these processes, an intact Mre11-binding domain of Xrs2 is crucial, whereas the FHA- and BRCT-domains as well as the Tel1-binding domain of Xrs2 are dispensable. Obviously, the Mre11-binding domain of the Xrs2 protein is crucial for the analysed functions and our results suggest a new role of the MRX complex for the formation of crossovers. Analysis of double mutants showed that the phenotype of the
Δxrs2 null mutant concerning the crossover frequency is dominant over the phenotypes of
Δsrs2 and
Δsgs1 null mutants. Thus, the complex seems to be involved in early steps of double-strand break and gap repair, and we propose that it has a regulatory role for the selection of homologous recombination pathways.</description><identifier>ISSN: 1568-7864</identifier><identifier>EISSN: 1568-7856</identifier><identifier>DOI: 10.1016/j.dnarep.2008.06.004</identifier><identifier>PMID: 18599383</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Bacteriology ; Biological and medical sciences ; Crossing Over, Genetic ; DNA Breaks, Double-Stranded ; DNA double-strand break repair ; DNA Repair ; Fundamental and applied biological sciences. Psychology ; Growth, nutrition, cell differenciation ; Microbiology ; Mitotic crossover ; Molecular and cellular biology ; Molecular genetics ; MRX complex ; Mutagenesis. Repair ; Plasmids ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - physiology ; XRS2</subject><ispartof>DNA repair, 2008-09, Vol.7 (9), p.1563-1577</ispartof><rights>2008 Elsevier B.V.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-804444a4098179f7cdcab1daa49151409be293978dc54ed749427a97154621113</citedby><cites>FETCH-LOGICAL-c421t-804444a4098179f7cdcab1daa49151409be293978dc54ed749427a97154621113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1568786408002206$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20598713$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18599383$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Steininger, Sylvia</creatorcontrib><creatorcontrib>Gomez-Paramio, Idoia</creatorcontrib><creatorcontrib>Braselmann, Herbert</creatorcontrib><creatorcontrib>Fellerhoff, Barbara</creatorcontrib><creatorcontrib>Dittberner, Daniela</creatorcontrib><creatorcontrib>Eckardt-Schupp, Friederike</creatorcontrib><creatorcontrib>Moertl, Simone</creatorcontrib><title>Xrs2 facilitates crossovers during DNA double-strand gap repair in yeast</title><title>DNA repair</title><addtitle>DNA Repair (Amst)</addtitle><description>Xrs2 is a member of the MRX complex (Mre11/Rad50/Xrs2) in
Saccharomyces cerevisiae. In this study we demonstrate the important role of the MRX complex and in more detail of Xrs2 for the repair of radiation-induced chromosomal double-strand breaks by pulsed field gel electrophoresis. By using a newly designed
in vivo plasmid–chromosome recombination system, we could show that gap repair efficiency and the association with crossovers were reduced in the MRX null mutants, but repair accuracy was unaffected. For these processes, an intact Mre11-binding domain of Xrs2 is crucial, whereas the FHA- and BRCT-domains as well as the Tel1-binding domain of Xrs2 are dispensable. Obviously, the Mre11-binding domain of the Xrs2 protein is crucial for the analysed functions and our results suggest a new role of the MRX complex for the formation of crossovers. Analysis of double mutants showed that the phenotype of the
Δxrs2 null mutant concerning the crossover frequency is dominant over the phenotypes of
Δsrs2 and
Δsgs1 null mutants. Thus, the complex seems to be involved in early steps of double-strand break and gap repair, and we propose that it has a regulatory role for the selection of homologous recombination pathways.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Crossing Over, Genetic</subject><subject>DNA Breaks, Double-Stranded</subject><subject>DNA double-strand break repair</subject><subject>DNA Repair</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Growth, nutrition, cell differenciation</subject><subject>Microbiology</subject><subject>Mitotic crossover</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>MRX complex</subject><subject>Mutagenesis. Repair</subject><subject>Plasmids</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>XRS2</subject><issn>1568-7864</issn><issn>1568-7856</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi0EoqXwDxDyBW4JnsSfF6SqBYpUwQUkbtasPam8yiaLnVTqv8fLrsoNfLE1et6Z8cPYaxAtCNDvt22cMNO-7YSwrdCtEPIJOwelbWOs0k8f31qesRelbIUAZbR-zs7AKud625-zm5-5dHzAkMa04EKFhzyXMt9TLjyuOU13_PrrJY_zuhmpKUvGKfI73PM6GlPmaeIPhGV5yZ4NOBZ6dbov2I9PH79f3TS33z5_ubq8bYLsYGmskPWgFM6CcYMJMeAGIqJ0oKCWN9S53hkbg5IUjXSyM-gMKKk7AOgv2Ltj332ef61UFr9LJdA44kTzWrx2vdFG6f-C4KRV1okKyiP45-eZBr_PaYf5wYPwB9V-64-q_UG1F9pX1TX25tR_3ewo_g2d3Fbg7QnAEnAcqrmQyiPXCeWsgQP34chR1XafKPsSEk2BYsoUFh_n9O9NfgPiG5yE</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Steininger, Sylvia</creator><creator>Gomez-Paramio, Idoia</creator><creator>Braselmann, Herbert</creator><creator>Fellerhoff, Barbara</creator><creator>Dittberner, Daniela</creator><creator>Eckardt-Schupp, Friederike</creator><creator>Moertl, Simone</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>Xrs2 facilitates crossovers during DNA double-strand gap repair in yeast</title><author>Steininger, Sylvia ; Gomez-Paramio, Idoia ; Braselmann, Herbert ; Fellerhoff, Barbara ; Dittberner, Daniela ; Eckardt-Schupp, Friederike ; Moertl, Simone</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-804444a4098179f7cdcab1daa49151409be293978dc54ed749427a97154621113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Crossing Over, Genetic</topic><topic>DNA Breaks, Double-Stranded</topic><topic>DNA double-strand break repair</topic><topic>DNA Repair</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Growth, nutrition, cell differenciation</topic><topic>Microbiology</topic><topic>Mitotic crossover</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>MRX complex</topic><topic>Mutagenesis. Repair</topic><topic>Plasmids</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>XRS2</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steininger, Sylvia</creatorcontrib><creatorcontrib>Gomez-Paramio, Idoia</creatorcontrib><creatorcontrib>Braselmann, Herbert</creatorcontrib><creatorcontrib>Fellerhoff, Barbara</creatorcontrib><creatorcontrib>Dittberner, Daniela</creatorcontrib><creatorcontrib>Eckardt-Schupp, Friederike</creatorcontrib><creatorcontrib>Moertl, Simone</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>DNA repair</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Steininger, Sylvia</au><au>Gomez-Paramio, Idoia</au><au>Braselmann, Herbert</au><au>Fellerhoff, Barbara</au><au>Dittberner, Daniela</au><au>Eckardt-Schupp, Friederike</au><au>Moertl, Simone</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Xrs2 facilitates crossovers during DNA double-strand gap repair in yeast</atitle><jtitle>DNA repair</jtitle><addtitle>DNA Repair (Amst)</addtitle><date>2008-09-01</date><risdate>2008</risdate><volume>7</volume><issue>9</issue><spage>1563</spage><epage>1577</epage><pages>1563-1577</pages><issn>1568-7864</issn><eissn>1568-7856</eissn><abstract>Xrs2 is a member of the MRX complex (Mre11/Rad50/Xrs2) in
Saccharomyces cerevisiae. In this study we demonstrate the important role of the MRX complex and in more detail of Xrs2 for the repair of radiation-induced chromosomal double-strand breaks by pulsed field gel electrophoresis. By using a newly designed
in vivo plasmid–chromosome recombination system, we could show that gap repair efficiency and the association with crossovers were reduced in the MRX null mutants, but repair accuracy was unaffected. For these processes, an intact Mre11-binding domain of Xrs2 is crucial, whereas the FHA- and BRCT-domains as well as the Tel1-binding domain of Xrs2 are dispensable. Obviously, the Mre11-binding domain of the Xrs2 protein is crucial for the analysed functions and our results suggest a new role of the MRX complex for the formation of crossovers. Analysis of double mutants showed that the phenotype of the
Δxrs2 null mutant concerning the crossover frequency is dominant over the phenotypes of
Δsrs2 and
Δsgs1 null mutants. Thus, the complex seems to be involved in early steps of double-strand break and gap repair, and we propose that it has a regulatory role for the selection of homologous recombination pathways.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>18599383</pmid><doi>10.1016/j.dnarep.2008.06.004</doi><tpages>15</tpages></addata></record> |
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| subjects | Bacteriology Biological and medical sciences Crossing Over, Genetic DNA Breaks, Double-Stranded DNA double-strand break repair DNA Repair Fundamental and applied biological sciences. Psychology Growth, nutrition, cell differenciation Microbiology Mitotic crossover Molecular and cellular biology Molecular genetics MRX complex Mutagenesis. Repair Plasmids Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - physiology XRS2 |
| title | Xrs2 facilitates crossovers during DNA double-strand gap repair in yeast |
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