TRF2 recruits the Werner syndrome (WRN) exonuclease for processing of telomeric DNA
The cancer-prone and premature aging disease Werner syndrome is due to loss of WRN gene function. Cells lacking WRN demonstrate genomic instability, including telomeric abnormalities and undergo premature senescence, suggesting defects in telomere metabolism. This notion is strongly supported by our...
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| Veröffentlicht in: | Oncogene 2004-01, Vol.23 (1), p.149-156 |
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| creator | Machwe, Amrita Xiao, Liren Orren, David K |
| description | The cancer-prone and premature aging disease Werner syndrome is due to loss of
WRN
gene function. Cells lacking WRN demonstrate genomic instability, including telomeric abnormalities and undergo premature senescence, suggesting defects in telomere metabolism. This notion is strongly supported by our finding of physical and functional interactions between WRN and TRF2, a telomeric repeat binding factor essential for proper telomeric structure. TRF2 binds to DNA substrates containing telomeric repeats and facilitates their degradation specifically by WRN exonuclease activity. WRN and TRF2 also interact directly in the absence of DNA. These results suggest that TRF2 recruits WRN for accurate processing of telomeric structures
in vivo
. Thus, our findings link problems in telomere maintenance to both carcinogenesis and specific features of aging. |
| doi_str_mv | 10.1038/sj.onc.1206906 |
| format | Article |
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WRN
gene function. Cells lacking WRN demonstrate genomic instability, including telomeric abnormalities and undergo premature senescence, suggesting defects in telomere metabolism. This notion is strongly supported by our finding of physical and functional interactions between WRN and TRF2, a telomeric repeat binding factor essential for proper telomeric structure. TRF2 binds to DNA substrates containing telomeric repeats and facilitates their degradation specifically by WRN exonuclease activity. WRN and TRF2 also interact directly in the absence of DNA. These results suggest that TRF2 recruits WRN for accurate processing of telomeric structures
in vivo
. Thus, our findings link problems in telomere maintenance to both carcinogenesis and specific features of aging.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1206906</identifier><identifier>PMID: 14712220</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Aging ; Apoptosis ; Base Sequence ; Biological and medical sciences ; Cancer ; Cell Biology ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; DNA - metabolism ; DNA Helicases - physiology ; Exodeoxyribonucleases ; Exonucleases - physiology ; Fundamental and applied biological sciences. Psychology ; Genotype & phenotype ; Human Genetics ; Internal Medicine ; Medicine ; Medicine & Public Health ; Metabolism ; Molecular and cellular biology ; Molecular Sequence Data ; Oncology ; original-paper ; RecQ Helicases ; Senescence ; Telomerase ; Telomere - metabolism ; Telomeric Repeat Binding Protein 1 - physiology ; Telomeric repeat binding protein 2 ; Telomeric Repeat Binding Protein 2 - physiology ; Toxicology ; Werner Syndrome - genetics ; Werner Syndrome Helicase ; Yeast</subject><ispartof>Oncogene, 2004-01, Vol.23 (1), p.149-156</ispartof><rights>Springer Nature Limited 2003</rights><rights>2004 INIST-CNRS</rights><rights>COPYRIGHT 2004 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jan 8, 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c564t-87bed38f2e2f08d97a868bd0b4d9a5c8d64d0bee21ab40f9e4394d4db80f46d3</citedby><cites>FETCH-LOGICAL-c564t-87bed38f2e2f08d97a868bd0b4d9a5c8d64d0bee21ab40f9e4394d4db80f46d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.onc.1206906$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.onc.1206906$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15673901$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14712220$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Machwe, Amrita</creatorcontrib><creatorcontrib>Xiao, Liren</creatorcontrib><creatorcontrib>Orren, David K</creatorcontrib><title>TRF2 recruits the Werner syndrome (WRN) exonuclease for processing of telomeric DNA</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>The cancer-prone and premature aging disease Werner syndrome is due to loss of
WRN
gene function. Cells lacking WRN demonstrate genomic instability, including telomeric abnormalities and undergo premature senescence, suggesting defects in telomere metabolism. This notion is strongly supported by our finding of physical and functional interactions between WRN and TRF2, a telomeric repeat binding factor essential for proper telomeric structure. TRF2 binds to DNA substrates containing telomeric repeats and facilitates their degradation specifically by WRN exonuclease activity. WRN and TRF2 also interact directly in the absence of DNA. These results suggest that TRF2 recruits WRN for accurate processing of telomeric structures
in vivo
. Thus, our findings link problems in telomere maintenance to both carcinogenesis and specific features of aging.</description><subject>Aging</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cancer</subject><subject>Cell Biology</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>DNA - metabolism</subject><subject>DNA Helicases - physiology</subject><subject>Exodeoxyribonucleases</subject><subject>Exonucleases - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genotype & phenotype</subject><subject>Human Genetics</subject><subject>Internal Medicine</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Oncology</subject><subject>original-paper</subject><subject>RecQ Helicases</subject><subject>Senescence</subject><subject>Telomerase</subject><subject>Telomere - metabolism</subject><subject>Telomeric Repeat Binding Protein 1 - physiology</subject><subject>Telomeric repeat binding protein 2</subject><subject>Telomeric Repeat Binding Protein 2 - physiology</subject><subject>Toxicology</subject><subject>Werner Syndrome - genetics</subject><subject>Werner Syndrome Helicase</subject><subject>Yeast</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp10UFrHCEUB3ApLc026bXHIoWW9jAbdRxnPC5p0xRCAulCjuLoc-syo4nOQPPta9iBhULwIOpP35M_Qh8oWVNSd-d5v47BrCkjQhLxCq0ob0XVNJK_RisiG1JJVrMT9C7nPSGklYS9RScFUcYYWaHf27tLhhOYNPsp4-kP4HtIARLOT8GmOAL-en938w3D3xhmM4DOgF1M-CFFAzn7sMPR4QmGQpM3-PvN5gy9cXrI8H6ZT9H28sf24qq6vv3562JzXZlG8Knq2h5s3TkGzJHOylZ3oust6bmVujGdFbwsABjVPSdOAq8lt9z2HXFc2PoUfTk8W1p5nCFPavTZwDDoAHHOikomGBeswE__wX2cUyitKcbamoumEQWtD2inB1A-uDglbcqwMHoTAzhf9je0k1QIKenxgkkx5wROPSQ_6vSkKFHP2ai8VyUbtWRTLnxc2pj7EeyRL2EU8HkBOhs9uKSD8fnoGtHWkjxXPj-4XI7CDtLxPy-U_gfAJKZ6</recordid><startdate>20040108</startdate><enddate>20040108</enddate><creator>Machwe, Amrita</creator><creator>Xiao, Liren</creator><creator>Orren, David K</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</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>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20040108</creationdate><title>TRF2 recruits the Werner syndrome (WRN) exonuclease for processing of telomeric DNA</title><author>Machwe, Amrita ; Xiao, Liren ; Orren, David K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c564t-87bed38f2e2f08d97a868bd0b4d9a5c8d64d0bee21ab40f9e4394d4db80f46d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Aging</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cancer</topic><topic>Cell Biology</topic><topic>Cell physiology</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>DNA - metabolism</topic><topic>DNA Helicases - physiology</topic><topic>Exodeoxyribonucleases</topic><topic>Exonucleases - physiology</topic><topic>Fundamental and applied biological sciences. 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WRN
gene function. Cells lacking WRN demonstrate genomic instability, including telomeric abnormalities and undergo premature senescence, suggesting defects in telomere metabolism. This notion is strongly supported by our finding of physical and functional interactions between WRN and TRF2, a telomeric repeat binding factor essential for proper telomeric structure. TRF2 binds to DNA substrates containing telomeric repeats and facilitates their degradation specifically by WRN exonuclease activity. WRN and TRF2 also interact directly in the absence of DNA. These results suggest that TRF2 recruits WRN for accurate processing of telomeric structures
in vivo
. Thus, our findings link problems in telomere maintenance to both carcinogenesis and specific features of aging.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>14712220</pmid><doi>10.1038/sj.onc.1206906</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0950-9232 1476-5594 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online; EZB-FREE-00999 freely available EZB journals |
| subjects | Aging Apoptosis Base Sequence Biological and medical sciences Cancer Cell Biology Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes DNA - metabolism DNA Helicases - physiology Exodeoxyribonucleases Exonucleases - physiology Fundamental and applied biological sciences. Psychology Genotype & phenotype Human Genetics Internal Medicine Medicine Medicine & Public Health Metabolism Molecular and cellular biology Molecular Sequence Data Oncology original-paper RecQ Helicases Senescence Telomerase Telomere - metabolism Telomeric Repeat Binding Protein 1 - physiology Telomeric repeat binding protein 2 Telomeric Repeat Binding Protein 2 - physiology Toxicology Werner Syndrome - genetics Werner Syndrome Helicase Yeast |
| title | TRF2 recruits the Werner syndrome (WRN) exonuclease for processing of telomeric DNA |
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