Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA
UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound...
Gespeichert in:
Veröffentlicht in: | FEBS letters 2006-11, Vol.580 (27), p.6423-6427 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 6427 |
---|---|
container_issue | 27 |
container_start_page | 6423 |
container_title | FEBS letters |
container_volume | 580 |
creator | Waters, Timothy R. Eryilmaz, Jitka Geddes, Stella Barrett, Tracey E. |
description | UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide. |
doi_str_mv | 10.1016/j.febslet.2006.10.051 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68175610</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579306012804</els_id><sourcerecordid>20365040</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5064-61b5ede06456bbbe9749a40f55737364daab737b70e9c9ad8e232b2895f7f6753</originalsourceid><addsrcrecordid>eNqNkcFu1DAQhi0EokvhEUA-ccsyTmI74YJ2ty1FquAAPVt2PKFeZePFdlrl7XG0K3EsJ49Hn3-P5iPkPYM1AyY-7dc9mjhgWpcAIvfWwNkLsmKNrIqqFs1LsgJgdcFlW12QNzHuId8b1r4mF0xCK6ERK9Jd6YP-jdRiwi45P1Iz0_SA9P4xbLY7etTp4UnPn-kuzDHpgcYUpi5NAanvF2hLjZ9GS5On_TD5gLFDNxba2oyhpVffN2_Jq14PEd-dz0tyf3P9a3db3P34-m23uSs6DqIuBDMcLeaSC2MMtrJudQ0957KSlait1iZXRgK2Xattg2VVmrJpeS97IXl1ST6eco_B_5kwJnVweZph0CP6KSrRMMkFg2fBEirBoV5AfgK74GMM2KtjcAcdZsVALRrUXp01qEXD0s4a8rsP5w8mc0D779V57xm4PQFPbsD5_1LVzfW2_Lk4XZSCAFY2UOeoL6cozKt9dBhU7ByOHVoXslJlvXtm2r9o5bBW</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20365040</pqid></control><display><type>article</type><title>Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Access via Wiley Online Library</source><source>Wiley Free Content</source><source>Alma/SFX Local Collection</source><creator>Waters, Timothy R. ; Eryilmaz, Jitka ; Geddes, Stella ; Barrett, Tracey E.</creator><creatorcontrib>Waters, Timothy R. ; Eryilmaz, Jitka ; Geddes, Stella ; Barrett, Tracey E.</creatorcontrib><description>UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2006.10.051</identifier><identifier>PMID: 17097086</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Crystallography, X-Ray - methods ; DNA Adducts - chemistry ; DNA Adducts - metabolism ; DNA Damage ; DNA Helicases - chemistry ; DNA Helicases - metabolism ; Endodeoxyribonucleases - chemistry ; Endodeoxyribonucleases - metabolism ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Models, Molecular ; Oligodeoxyribonucleotides - chemistry ; Oligodeoxyribonucleotides - metabolism ; Protein crystallography ; Protein Structure, Secondary ; Protein Structure, Tertiary ; T-fluorescein ; UvrABC</subject><ispartof>FEBS letters, 2006-11, Vol.580 (27), p.6423-6427</ispartof><rights>2006 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5064-61b5ede06456bbbe9749a40f55737364daab737b70e9c9ad8e232b2895f7f6753</citedby><cites>FETCH-LOGICAL-c5064-61b5ede06456bbbe9749a40f55737364daab737b70e9c9ad8e232b2895f7f6753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2006.10.051$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2006.10.051$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17097086$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Waters, Timothy R.</creatorcontrib><creatorcontrib>Eryilmaz, Jitka</creatorcontrib><creatorcontrib>Geddes, Stella</creatorcontrib><creatorcontrib>Barrett, Tracey E.</creatorcontrib><title>Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide.</description><subject>Crystallography, X-Ray - methods</subject><subject>DNA Adducts - chemistry</subject><subject>DNA Adducts - metabolism</subject><subject>DNA Damage</subject><subject>DNA Helicases - chemistry</subject><subject>DNA Helicases - metabolism</subject><subject>Endodeoxyribonucleases - chemistry</subject><subject>Endodeoxyribonucleases - metabolism</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Models, Molecular</subject><subject>Oligodeoxyribonucleotides - chemistry</subject><subject>Oligodeoxyribonucleotides - metabolism</subject><subject>Protein crystallography</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>T-fluorescein</subject><subject>UvrABC</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhi0EokvhEUA-ccsyTmI74YJ2ty1FquAAPVt2PKFeZePFdlrl7XG0K3EsJ49Hn3-P5iPkPYM1AyY-7dc9mjhgWpcAIvfWwNkLsmKNrIqqFs1LsgJgdcFlW12QNzHuId8b1r4mF0xCK6ERK9Jd6YP-jdRiwi45P1Iz0_SA9P4xbLY7etTp4UnPn-kuzDHpgcYUpi5NAanvF2hLjZ9GS5On_TD5gLFDNxba2oyhpVffN2_Jq14PEd-dz0tyf3P9a3db3P34-m23uSs6DqIuBDMcLeaSC2MMtrJudQ0957KSlait1iZXRgK2Xattg2VVmrJpeS97IXl1ST6eco_B_5kwJnVweZph0CP6KSrRMMkFg2fBEirBoV5AfgK74GMM2KtjcAcdZsVALRrUXp01qEXD0s4a8rsP5w8mc0D779V57xm4PQFPbsD5_1LVzfW2_Lk4XZSCAFY2UOeoL6cozKt9dBhU7ByOHVoXslJlvXtm2r9o5bBW</recordid><startdate>20061127</startdate><enddate>20061127</enddate><creator>Waters, Timothy R.</creator><creator>Eryilmaz, Jitka</creator><creator>Geddes, Stella</creator><creator>Barrett, Tracey E.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20061127</creationdate><title>Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA</title><author>Waters, Timothy R. ; Eryilmaz, Jitka ; Geddes, Stella ; Barrett, Tracey E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5064-61b5ede06456bbbe9749a40f55737364daab737b70e9c9ad8e232b2895f7f6753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Crystallography, X-Ray - methods</topic><topic>DNA Adducts - chemistry</topic><topic>DNA Adducts - metabolism</topic><topic>DNA Damage</topic><topic>DNA Helicases - chemistry</topic><topic>DNA Helicases - metabolism</topic><topic>Endodeoxyribonucleases - chemistry</topic><topic>Endodeoxyribonucleases - metabolism</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Models, Molecular</topic><topic>Oligodeoxyribonucleotides - chemistry</topic><topic>Oligodeoxyribonucleotides - metabolism</topic><topic>Protein crystallography</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>T-fluorescein</topic><topic>UvrABC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Waters, Timothy R.</creatorcontrib><creatorcontrib>Eryilmaz, Jitka</creatorcontrib><creatorcontrib>Geddes, Stella</creatorcontrib><creatorcontrib>Barrett, Tracey E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Waters, Timothy R.</au><au>Eryilmaz, Jitka</au><au>Geddes, Stella</au><au>Barrett, Tracey E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-11-27</date><risdate>2006</risdate><volume>580</volume><issue>27</issue><spage>6423</spage><epage>6427</epage><pages>6423-6427</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>17097086</pmid><doi>10.1016/j.febslet.2006.10.051</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0014-5793 |
ispartof | FEBS letters, 2006-11, Vol.580 (27), p.6423-6427 |
issn | 0014-5793 1873-3468 |
language | eng |
recordid | cdi_proquest_miscellaneous_68175610 |
source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Wiley Free Content; Alma/SFX Local Collection |
subjects | Crystallography, X-Ray - methods DNA Adducts - chemistry DNA Adducts - metabolism DNA Damage DNA Helicases - chemistry DNA Helicases - metabolism Endodeoxyribonucleases - chemistry Endodeoxyribonucleases - metabolism Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Models, Molecular Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - metabolism Protein crystallography Protein Structure, Secondary Protein Structure, Tertiary T-fluorescein UvrABC |
title | Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-21T09%3A54%3A23IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Damage%20detection%20by%20the%20UvrABC%20pathway:%20Crystal%20structure%20of%20UvrB%20bound%20to%20fluorescein-adducted%20DNA&rft.jtitle=FEBS%20letters&rft.au=Waters,%20Timothy%20R.&rft.date=2006-11-27&rft.volume=580&rft.issue=27&rft.spage=6423&rft.epage=6427&rft.pages=6423-6427&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/j.febslet.2006.10.051&rft_dat=%3Cproquest_cross%3E20365040%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20365040&rft_id=info:pmid/17097086&rft_els_id=S0014579306012804&rfr_iscdi=true |