Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses
The cyclobutane pyrimidine dimer (CPD) is one of the major forms of DNA damage caused by irradiation with ultraviolet (UV) light. CPD photolyases recognize and repair UV-damaged DNA. The DNA recognition mechanism of the CPD photolyase has remained obscure because of a lack of structural information...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2004-07, Vol.279 (31), p.32950-32956 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 32956 |
|---|---|
| container_issue | 31 |
| container_start_page | 32950 |
| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Torizawa, Takuya Ueda, Takumi Kuramitsu, Seiki Hitomi, Kenichi Todo, Takeshi Iwai, Shigenori Morikawa, Kosuke Shimada, Ichio |
| description | The cyclobutane pyrimidine dimer (CPD) is one of the major forms of DNA damage caused by irradiation with ultraviolet (UV)
light. CPD photolyases recognize and repair UV-damaged DNA. The DNA recognition mechanism of the CPD photolyase has remained
obscure because of a lack of structural information about DNA-CPD photolyase complexes. In order to elucidate the CPD photolyase
DNA binding mode, we performed NMR analyses of the DNA-CPD photolyase complex. Based upon results from 31 P NMR measurements, in combination with site-directed mutagenesis, we have demonstrated the orientation of CPD-containing
single-stranded DNA (ssDNA) on the CPD photolyase. In addition, chemical shift perturbation analyses, using stable isotope-labeled
DNA, revealed that the CPD is buried in a cavity within CPD photolyase. Finally, NMR analyses of a double-stranded DNA (dsDNA)-CPD
photolyase complex indicated that the CPD is flipped out of the dsDNA by the enzyme, to gain access to the active site. |
| doi_str_mv | 10.1074/jbc.M404536200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_18011313</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18011313</sourcerecordid><originalsourceid>FETCH-LOGICAL-c391t-66603ff88504292dd61eb87db23b0d7ffa2991cdcee8f2b6f14104cf8e58b54d3</originalsourceid><addsrcrecordid>eNpFkE1r3DAQhkVJabZJrzkGHUJoD95qJH9Ix2XTj0A2XUIKvQlLHq0VbCuxvC3-91W7C9FlxPDMC-9DyAWwJbAq__xk7HKTs7wQJWfsDVkAkyITBfw6IQvGOGSKF_KUvI_xiaWXK3hHTqGAUlWSLUh3O_zGOPldPfkw0ODo1CJdz7YLZj_VA9LtPPreNz59b3yPI_243t58ots2TKGb65jW9yv6gDbsBv8_ZIO2rQcfe2pmer95oKuh7uaI8Zy8dXUX8cNxnpGfX788rr9ndz--3a5Xd5kVCqasLEsmnJOyYDlXvGlKQCOrxnBhWFM5V3OlwDYWUTpuSgc5sNw6iYU0Rd6IM3J9yH0ew8s-1dO9jxa7LvUJ-6hBMgABIoHLA2jHEOOITj-nsvU4a2D6n1-d_OpXv-ng8pi8Nz02r_hRaAKuDkDrd-0fP6I2PtgWe80rpQVowVXBxF9sPIJE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18011313</pqid></control><display><type>article</type><title>Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Torizawa, Takuya ; Ueda, Takumi ; Kuramitsu, Seiki ; Hitomi, Kenichi ; Todo, Takeshi ; Iwai, Shigenori ; Morikawa, Kosuke ; Shimada, Ichio</creator><creatorcontrib>Torizawa, Takuya ; Ueda, Takumi ; Kuramitsu, Seiki ; Hitomi, Kenichi ; Todo, Takeshi ; Iwai, Shigenori ; Morikawa, Kosuke ; Shimada, Ichio</creatorcontrib><description>The cyclobutane pyrimidine dimer (CPD) is one of the major forms of DNA damage caused by irradiation with ultraviolet (UV)
light. CPD photolyases recognize and repair UV-damaged DNA. The DNA recognition mechanism of the CPD photolyase has remained
obscure because of a lack of structural information about DNA-CPD photolyase complexes. In order to elucidate the CPD photolyase
DNA binding mode, we performed NMR analyses of the DNA-CPD photolyase complex. Based upon results from 31 P NMR measurements, in combination with site-directed mutagenesis, we have demonstrated the orientation of CPD-containing
single-stranded DNA (ssDNA) on the CPD photolyase. In addition, chemical shift perturbation analyses, using stable isotope-labeled
DNA, revealed that the CPD is buried in a cavity within CPD photolyase. Finally, NMR analyses of a double-stranded DNA (dsDNA)-CPD
photolyase complex indicated that the CPD is flipped out of the dsDNA by the enzyme, to gain access to the active site.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M404536200</identifier><identifier>PMID: 15169780</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Binding Sites ; Deoxyribodipyrimidine Photo-Lyase - chemistry ; Dimerization ; DNA - chemistry ; DNA, Single-Stranded - metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Models, Chemical ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Pyrimidines - chemistry ; Spectrophotometry ; Surface Plasmon Resonance ; Thermus thermophilus - metabolism ; Ultraviolet Rays</subject><ispartof>The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32950-32956</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-66603ff88504292dd61eb87db23b0d7ffa2991cdcee8f2b6f14104cf8e58b54d3</citedby><cites>FETCH-LOGICAL-c391t-66603ff88504292dd61eb87db23b0d7ffa2991cdcee8f2b6f14104cf8e58b54d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15169780$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Torizawa, Takuya</creatorcontrib><creatorcontrib>Ueda, Takumi</creatorcontrib><creatorcontrib>Kuramitsu, Seiki</creatorcontrib><creatorcontrib>Hitomi, Kenichi</creatorcontrib><creatorcontrib>Todo, Takeshi</creatorcontrib><creatorcontrib>Iwai, Shigenori</creatorcontrib><creatorcontrib>Morikawa, Kosuke</creatorcontrib><creatorcontrib>Shimada, Ichio</creatorcontrib><title>Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The cyclobutane pyrimidine dimer (CPD) is one of the major forms of DNA damage caused by irradiation with ultraviolet (UV)
light. CPD photolyases recognize and repair UV-damaged DNA. The DNA recognition mechanism of the CPD photolyase has remained
obscure because of a lack of structural information about DNA-CPD photolyase complexes. In order to elucidate the CPD photolyase
DNA binding mode, we performed NMR analyses of the DNA-CPD photolyase complex. Based upon results from 31 P NMR measurements, in combination with site-directed mutagenesis, we have demonstrated the orientation of CPD-containing
single-stranded DNA (ssDNA) on the CPD photolyase. In addition, chemical shift perturbation analyses, using stable isotope-labeled
DNA, revealed that the CPD is buried in a cavity within CPD photolyase. Finally, NMR analyses of a double-stranded DNA (dsDNA)-CPD
photolyase complex indicated that the CPD is flipped out of the dsDNA by the enzyme, to gain access to the active site.</description><subject>Binding Sites</subject><subject>Deoxyribodipyrimidine Photo-Lyase - chemistry</subject><subject>Dimerization</subject><subject>DNA - chemistry</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Pyrimidines - chemistry</subject><subject>Spectrophotometry</subject><subject>Surface Plasmon Resonance</subject><subject>Thermus thermophilus - metabolism</subject><subject>Ultraviolet Rays</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1r3DAQhkVJabZJrzkGHUJoD95qJH9Ix2XTj0A2XUIKvQlLHq0VbCuxvC3-91W7C9FlxPDMC-9DyAWwJbAq__xk7HKTs7wQJWfsDVkAkyITBfw6IQvGOGSKF_KUvI_xiaWXK3hHTqGAUlWSLUh3O_zGOPldPfkw0ODo1CJdz7YLZj_VA9LtPPreNz59b3yPI_243t58ots2TKGb65jW9yv6gDbsBv8_ZIO2rQcfe2pmer95oKuh7uaI8Zy8dXUX8cNxnpGfX788rr9ndz--3a5Xd5kVCqasLEsmnJOyYDlXvGlKQCOrxnBhWFM5V3OlwDYWUTpuSgc5sNw6iYU0Rd6IM3J9yH0ew8s-1dO9jxa7LvUJ-6hBMgABIoHLA2jHEOOITj-nsvU4a2D6n1-d_OpXv-ng8pi8Nz02r_hRaAKuDkDrd-0fP6I2PtgWe80rpQVowVXBxF9sPIJE</recordid><startdate>20040730</startdate><enddate>20040730</enddate><creator>Torizawa, Takuya</creator><creator>Ueda, Takumi</creator><creator>Kuramitsu, Seiki</creator><creator>Hitomi, Kenichi</creator><creator>Todo, Takeshi</creator><creator>Iwai, Shigenori</creator><creator>Morikawa, Kosuke</creator><creator>Shimada, Ichio</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope></search><sort><creationdate>20040730</creationdate><title>Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses</title><author>Torizawa, Takuya ; Ueda, Takumi ; Kuramitsu, Seiki ; Hitomi, Kenichi ; Todo, Takeshi ; Iwai, Shigenori ; Morikawa, Kosuke ; Shimada, Ichio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-66603ff88504292dd61eb87db23b0d7ffa2991cdcee8f2b6f14104cf8e58b54d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Binding Sites</topic><topic>Deoxyribodipyrimidine Photo-Lyase - chemistry</topic><topic>Dimerization</topic><topic>DNA - chemistry</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>Kinetics</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Pyrimidines - chemistry</topic><topic>Spectrophotometry</topic><topic>Surface Plasmon Resonance</topic><topic>Thermus thermophilus - metabolism</topic><topic>Ultraviolet Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Torizawa, Takuya</creatorcontrib><creatorcontrib>Ueda, Takumi</creatorcontrib><creatorcontrib>Kuramitsu, Seiki</creatorcontrib><creatorcontrib>Hitomi, Kenichi</creatorcontrib><creatorcontrib>Todo, Takeshi</creatorcontrib><creatorcontrib>Iwai, Shigenori</creatorcontrib><creatorcontrib>Morikawa, Kosuke</creatorcontrib><creatorcontrib>Shimada, Ichio</creatorcontrib><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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Torizawa, Takuya</au><au>Ueda, Takumi</au><au>Kuramitsu, Seiki</au><au>Hitomi, Kenichi</au><au>Todo, Takeshi</au><au>Iwai, Shigenori</au><au>Morikawa, Kosuke</au><au>Shimada, Ichio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-07-30</date><risdate>2004</risdate><volume>279</volume><issue>31</issue><spage>32950</spage><epage>32956</epage><pages>32950-32956</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The cyclobutane pyrimidine dimer (CPD) is one of the major forms of DNA damage caused by irradiation with ultraviolet (UV)
light. CPD photolyases recognize and repair UV-damaged DNA. The DNA recognition mechanism of the CPD photolyase has remained
obscure because of a lack of structural information about DNA-CPD photolyase complexes. In order to elucidate the CPD photolyase
DNA binding mode, we performed NMR analyses of the DNA-CPD photolyase complex. Based upon results from 31 P NMR measurements, in combination with site-directed mutagenesis, we have demonstrated the orientation of CPD-containing
single-stranded DNA (ssDNA) on the CPD photolyase. In addition, chemical shift perturbation analyses, using stable isotope-labeled
DNA, revealed that the CPD is buried in a cavity within CPD photolyase. Finally, NMR analyses of a double-stranded DNA (dsDNA)-CPD
photolyase complex indicated that the CPD is flipped out of the dsDNA by the enzyme, to gain access to the active site.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15169780</pmid><doi>10.1074/jbc.M404536200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32950-32956 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_18011313 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Binding Sites Deoxyribodipyrimidine Photo-Lyase - chemistry Dimerization DNA - chemistry DNA, Single-Stranded - metabolism Kinetics Magnetic Resonance Spectroscopy Models, Chemical Models, Molecular Mutagenesis, Site-Directed Mutation Protein Binding Protein Conformation Protein Structure, Tertiary Pyrimidines - chemistry Spectrophotometry Surface Plasmon Resonance Thermus thermophilus - metabolism Ultraviolet Rays |
| title | Investigation of the Cyclobutane Pyrimidine Dimer (CPD) Photolyase DNA Recognition Mechanism by NMR Analyses |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-15T20%3A35%3A36IST&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=Investigation%20of%20the%20Cyclobutane%20Pyrimidine%20Dimer%20(CPD)%20Photolyase%20DNA%20Recognition%20Mechanism%20by%20NMR%20Analyses&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Torizawa,%20Takuya&rft.date=2004-07-30&rft.volume=279&rft.issue=31&rft.spage=32950&rft.epage=32956&rft.pages=32950-32956&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M404536200&rft_dat=%3Cproquest_cross%3E18011313%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=18011313&rft_id=info:pmid/15169780&rfr_iscdi=true |