Role for BLM in replication-fork restart and suppression of origin firing after replicative stress
Mutations in BLM give rise to Bloom's syndrome, a genetic disorder associated with cancer predisposition and chromosomal instability. Using a dual-labeling system in isolated chromosome fibers, we show that the BLM protein is required for two aspects of the cellular response to replicative stre...
Gespeichert in:
| Veröffentlicht in: | Nature structural & molecular biology 2007-07, Vol.14 (7), p.677-679 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 679 |
|---|---|
| container_issue | 7 |
| container_start_page | 677 |
| container_title | Nature structural & molecular biology |
| container_volume | 14 |
| creator | Hickson, Ian D Davies, Sally L North, Phillip S |
| description | Mutations in BLM give rise to Bloom's syndrome, a genetic disorder associated with cancer predisposition and chromosomal instability. Using a dual-labeling system in isolated chromosome fibers, we show that the BLM protein is required for two aspects of the cellular response to replicative stress: efficient replication-fork restart and suppression of new origin firing. These functions require the helicase activity of BLM and the Thr99 residue targeted by stress-activated kinases. |
| doi_str_mv | 10.1038/nsmb1267 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_70705850</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A182029100</galeid><sourcerecordid>A182029100</sourcerecordid><originalsourceid>FETCH-LOGICAL-c563t-603d70a424f43668f89d4d635dd7a755894cecd969fb585a7fb740b3138daa7d3</originalsourceid><addsrcrecordid>eNqFktFuFCEUhonR2FpNfAJDNDF6MRWGYYDL2tS2yRqTqteEGWBDnYERGKNvXya77mabGsMFcPj-_5wTDgAvMTrFiPAPPo0drlv2CBxj2tBKCE4f786CHIFnKd0iVFPKyFNwhFmLSCPYMehuwmCgDRF-XH2GzsNopsH1KrvgqxL-UQIpq5ih8hqmeZrKPZVHGCwM0a2LxLro_Boqm03c638ZmPICPwdPrBqSebHdT8D3Txffzq-q1ZfL6_OzVdXTluSqVKQZUk3d2Ia0Lbdc6Ea3hGrNFKOUi6Y3vRatsB3lVDHbsQZ1BBOulWKanIC3G98php9zqVqOLvVmGJQ3YU6SIYaKEP0XxCUHRy0u4Ot74G2Yoy9NyLrmhLIakQK92UBrNRjpvA05qn5xlGeY16gWGC05Tx-gytJmdH3wxroSPxC8PxAUJpvfea3mlOT115tD9t2G7WNIKRorp-hGFf9IjOQyIPLvgBT01baluRuN3oPbidjnTdPyqybue_63mVd5jmZntgPuAGaOzE4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>228357203</pqid></control><display><type>article</type><title>Role for BLM in replication-fork restart and suppression of origin firing after replicative stress</title><source>MEDLINE</source><source>Nature Journals Online</source><source>Alma/SFX Local Collection</source><creator>Hickson, Ian D ; Davies, Sally L ; North, Phillip S</creator><creatorcontrib>Hickson, Ian D ; Davies, Sally L ; North, Phillip S</creatorcontrib><description>Mutations in BLM give rise to Bloom's syndrome, a genetic disorder associated with cancer predisposition and chromosomal instability. Using a dual-labeling system in isolated chromosome fibers, we show that the BLM protein is required for two aspects of the cellular response to replicative stress: efficient replication-fork restart and suppression of new origin firing. These functions require the helicase activity of BLM and the Thr99 residue targeted by stress-activated kinases.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb1267</identifier><identifier>PMID: 17603497</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - physiology ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; brief-communication ; Cancer ; Cells, Cultured ; Chromosomes ; Complications and side effects ; DNA Helicases - genetics ; DNA Helicases - physiology ; DNA replication ; DNA Replication - drug effects ; Fibers ; Gene mutations ; Genetic disorders ; Humans ; Kinases ; Labeling ; Life Sciences ; Membrane Biology ; Mutation ; Physiological aspects ; Protein Structure ; Protein-Serine-Threonine Kinases - metabolism ; RecQ Helicases ; Replication Origin ; Risk factors ; Threonine - metabolism</subject><ispartof>Nature structural & molecular biology, 2007-07, Vol.14 (7), p.677-679</ispartof><rights>Springer Nature America, Inc. 2007</rights><rights>COPYRIGHT 2007 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c563t-603d70a424f43668f89d4d635dd7a755894cecd969fb585a7fb740b3138daa7d3</citedby><cites>FETCH-LOGICAL-c563t-603d70a424f43668f89d4d635dd7a755894cecd969fb585a7fb740b3138daa7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17603497$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hickson, Ian D</creatorcontrib><creatorcontrib>Davies, Sally L</creatorcontrib><creatorcontrib>North, Phillip S</creatorcontrib><title>Role for BLM in replication-fork restart and suppression of origin firing after replicative stress</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Mutations in BLM give rise to Bloom's syndrome, a genetic disorder associated with cancer predisposition and chromosomal instability. Using a dual-labeling system in isolated chromosome fibers, we show that the BLM protein is required for two aspects of the cellular response to replicative stress: efficient replication-fork restart and suppression of new origin firing. These functions require the helicase activity of BLM and the Thr99 residue targeted by stress-activated kinases.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - physiology</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>brief-communication</subject><subject>Cancer</subject><subject>Cells, Cultured</subject><subject>Chromosomes</subject><subject>Complications and side effects</subject><subject>DNA Helicases - genetics</subject><subject>DNA Helicases - physiology</subject><subject>DNA replication</subject><subject>DNA Replication - drug effects</subject><subject>Fibers</subject><subject>Gene mutations</subject><subject>Genetic disorders</subject><subject>Humans</subject><subject>Kinases</subject><subject>Labeling</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Mutation</subject><subject>Physiological aspects</subject><subject>Protein Structure</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>RecQ Helicases</subject><subject>Replication Origin</subject><subject>Risk factors</subject><subject>Threonine - metabolism</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFktFuFCEUhonR2FpNfAJDNDF6MRWGYYDL2tS2yRqTqteEGWBDnYERGKNvXya77mabGsMFcPj-_5wTDgAvMTrFiPAPPo0drlv2CBxj2tBKCE4f786CHIFnKd0iVFPKyFNwhFmLSCPYMehuwmCgDRF-XH2GzsNopsH1KrvgqxL-UQIpq5ih8hqmeZrKPZVHGCwM0a2LxLro_Boqm03c638ZmPICPwdPrBqSebHdT8D3Txffzq-q1ZfL6_OzVdXTluSqVKQZUk3d2Ia0Lbdc6Ea3hGrNFKOUi6Y3vRatsB3lVDHbsQZ1BBOulWKanIC3G98php9zqVqOLvVmGJQ3YU6SIYaKEP0XxCUHRy0u4Ot74G2Yoy9NyLrmhLIakQK92UBrNRjpvA05qn5xlGeY16gWGC05Tx-gytJmdH3wxroSPxC8PxAUJpvfea3mlOT115tD9t2G7WNIKRorp-hGFf9IjOQyIPLvgBT01baluRuN3oPbidjnTdPyqybue_63mVd5jmZntgPuAGaOzE4</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Hickson, Ian D</creator><creator>Davies, Sally L</creator><creator>North, Phillip S</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</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>C1K</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>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20070701</creationdate><title>Role for BLM in replication-fork restart and suppression of origin firing after replicative stress</title><author>Hickson, Ian D ; Davies, Sally L ; North, Phillip S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c563t-603d70a424f43668f89d4d635dd7a755894cecd969fb585a7fb740b3138daa7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - physiology</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>brief-communication</topic><topic>Cancer</topic><topic>Cells, Cultured</topic><topic>Chromosomes</topic><topic>Complications and side effects</topic><topic>DNA Helicases - genetics</topic><topic>DNA Helicases - physiology</topic><topic>DNA replication</topic><topic>DNA Replication - drug effects</topic><topic>Fibers</topic><topic>Gene mutations</topic><topic>Genetic disorders</topic><topic>Humans</topic><topic>Kinases</topic><topic>Labeling</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Mutation</topic><topic>Physiological aspects</topic><topic>Protein Structure</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>RecQ Helicases</topic><topic>Replication Origin</topic><topic>Risk factors</topic><topic>Threonine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hickson, Ian D</creatorcontrib><creatorcontrib>Davies, Sally L</creatorcontrib><creatorcontrib>North, Phillip S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hickson, Ian D</au><au>Davies, Sally L</au><au>North, Phillip S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role for BLM in replication-fork restart and suppression of origin firing after replicative stress</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>14</volume><issue>7</issue><spage>677</spage><epage>679</epage><pages>677-679</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Mutations in BLM give rise to Bloom's syndrome, a genetic disorder associated with cancer predisposition and chromosomal instability. Using a dual-labeling system in isolated chromosome fibers, we show that the BLM protein is required for two aspects of the cellular response to replicative stress: efficient replication-fork restart and suppression of new origin firing. These functions require the helicase activity of BLM and the Thr99 residue targeted by stress-activated kinases.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>17603497</pmid><doi>10.1038/nsmb1267</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1545-9993 |
| ispartof | Nature structural & molecular biology, 2007-07, Vol.14 (7), p.677-679 |
| issn | 1545-9993 1545-9985 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70705850 |
| source | MEDLINE; Nature Journals Online; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - physiology Biochemistry Biological Microscopy Biomedical and Life Sciences brief-communication Cancer Cells, Cultured Chromosomes Complications and side effects DNA Helicases - genetics DNA Helicases - physiology DNA replication DNA Replication - drug effects Fibers Gene mutations Genetic disorders Humans Kinases Labeling Life Sciences Membrane Biology Mutation Physiological aspects Protein Structure Protein-Serine-Threonine Kinases - metabolism RecQ Helicases Replication Origin Risk factors Threonine - metabolism |
| title | Role for BLM in replication-fork restart and suppression of origin firing after replicative stress |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T07%3A39%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Role%20for%20BLM%20in%20replication-fork%20restart%20and%20suppression%20of%20origin%20firing%20after%20replicative%20stress&rft.jtitle=Nature%20structural%20&%20molecular%20biology&rft.au=Hickson,%20Ian%20D&rft.date=2007-07-01&rft.volume=14&rft.issue=7&rft.spage=677&rft.epage=679&rft.pages=677-679&rft.issn=1545-9993&rft.eissn=1545-9985&rft_id=info:doi/10.1038/nsmb1267&rft_dat=%3Cgale_proqu%3EA182029100%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=228357203&rft_id=info:pmid/17603497&rft_galeid=A182029100&rfr_iscdi=true |