Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts
The S3 ribosomal protein of Drosophila melanogaster possesses various DNA repair activities, including the capacity to incise at apurinic/apyrimidinic (AP) sites and 8‐oxo‐7,8‐dihydroguanine (8‐oxoG) residues. We have recently hypothesized that this multifunctional protein may improve the efficiency...
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| Veröffentlicht in: | Environmental and molecular mutagenesis 2003, Vol.42 (1), p.50-58 |
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| creator | Cappelli, Enrico D'Osualdo, Andrea Bogliolo, Massimo Kelley, Mark R. Frosina, Guido |
| description | The S3 ribosomal protein of Drosophila melanogaster possesses various DNA repair activities, including the capacity to incise at apurinic/apyrimidinic (AP) sites and 8‐oxo‐7,8‐dihydroguanine (8‐oxoG) residues. We have recently hypothesized that this multifunctional protein may improve the efficiency of DNA base excision repair (BER) in mammalian cells. We have investigated the effect of pure GST‐tagged Drosophila S3 on BER of different endogenous lesions performed by human and mouse cell extracts. Drosophila S3 significantly accelerated the BER of 8‐oxoG (initiated by the bifunctional glycosylase OGG1). The stimulating effect was linked to the capacity of S3 to remove the 8‐oxoG lesion and cleave the resulting AP site, rather than acceleration of downstream steps of the BER pathway (e.g., removal of 3′ blocking fragments). No stimulating effect was observed on the BER of uracil, natural AP sites, and β‐lyase‐cleaved AP sites. Heterologous expression of Drosophila S3 may be used to enhance 8‐oxoG repair in human cells. Environ. Mol. Mutagen. 42:50–58, 2003. © 2003 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/em.10166 |
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We have recently hypothesized that this multifunctional protein may improve the efficiency of DNA base excision repair (BER) in mammalian cells. We have investigated the effect of pure GST‐tagged Drosophila S3 on BER of different endogenous lesions performed by human and mouse cell extracts. Drosophila S3 significantly accelerated the BER of 8‐oxoG (initiated by the bifunctional glycosylase OGG1). The stimulating effect was linked to the capacity of S3 to remove the 8‐oxoG lesion and cleave the resulting AP site, rather than acceleration of downstream steps of the BER pathway (e.g., removal of 3′ blocking fragments). No stimulating effect was observed on the BER of uracil, natural AP sites, and β‐lyase‐cleaved AP sites. Heterologous expression of Drosophila S3 may be used to enhance 8‐oxoG repair in human cells. Environ. Mol. Mutagen. 42:50–58, 2003. © 2003 Wiley‐Liss, Inc.</description><identifier>ISSN: 0893-6692</identifier><identifier>EISSN: 1098-2280</identifier><identifier>DOI: 10.1002/em.10166</identifier><identifier>PMID: 12874813</identifier><identifier>CODEN: EMMUEG</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>8-oxoguanine ; Animals ; apurinic sites ; Biological and medical sciences ; Cell Extracts - chemistry ; Cell Extracts - pharmacology ; DNA - drug effects ; DNA base excision repair ; DNA Damage - drug effects ; DNA Repair - drug effects ; DNA-Formamidopyrimidine Glycosylase ; Drosophila melanogaster ; Drosophila melanogaster - physiology ; Drosophila S3 protein ; Fibroblasts - chemistry ; Fibroblasts - drug effects ; Fibroblasts - metabolism ; Fundamental and applied biological sciences. Psychology ; Guanosine - analogs & derivatives ; Guanosine - genetics ; Guanosine - metabolism ; Humans ; Mice ; Molecular and cellular biology ; Molecular genetics ; Mutagenesis. Repair ; N-Glycosyl Hydrolases - toxicity ; Ribosomal Proteins - isolation & purification ; Ribosomal Proteins - pharmacology</subject><ispartof>Environmental and molecular mutagenesis, 2003, Vol.42 (1), p.50-58</ispartof><rights>Copyright © 2003 Wiley‐Liss, Inc.</rights><rights>2004 INIST-CNRS</rights><rights>Copyright 2003 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4826-c005764a8ff44da3ea993a26e29548988358da499b28ea87a302a3fb7b1a53843</citedby><cites>FETCH-LOGICAL-c4826-c005764a8ff44da3ea993a26e29548988358da499b28ea87a302a3fb7b1a53843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fem.10166$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fem.10166$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,4023,27922,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15027778$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12874813$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cappelli, Enrico</creatorcontrib><creatorcontrib>D'Osualdo, Andrea</creatorcontrib><creatorcontrib>Bogliolo, Massimo</creatorcontrib><creatorcontrib>Kelley, Mark R.</creatorcontrib><creatorcontrib>Frosina, Guido</creatorcontrib><title>Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts</title><title>Environmental and molecular mutagenesis</title><addtitle>Environ. Mol. Mutagen</addtitle><description>The S3 ribosomal protein of Drosophila melanogaster possesses various DNA repair activities, including the capacity to incise at apurinic/apyrimidinic (AP) sites and 8‐oxo‐7,8‐dihydroguanine (8‐oxoG) residues. We have recently hypothesized that this multifunctional protein may improve the efficiency of DNA base excision repair (BER) in mammalian cells. We have investigated the effect of pure GST‐tagged Drosophila S3 on BER of different endogenous lesions performed by human and mouse cell extracts. Drosophila S3 significantly accelerated the BER of 8‐oxoG (initiated by the bifunctional glycosylase OGG1). The stimulating effect was linked to the capacity of S3 to remove the 8‐oxoG lesion and cleave the resulting AP site, rather than acceleration of downstream steps of the BER pathway (e.g., removal of 3′ blocking fragments). No stimulating effect was observed on the BER of uracil, natural AP sites, and β‐lyase‐cleaved AP sites. Heterologous expression of Drosophila S3 may be used to enhance 8‐oxoG repair in human cells. Environ. Mol. Mutagen. 42:50–58, 2003. © 2003 Wiley‐Liss, Inc.</description><subject>8-oxoguanine</subject><subject>Animals</subject><subject>apurinic sites</subject><subject>Biological and medical sciences</subject><subject>Cell Extracts - chemistry</subject><subject>Cell Extracts - pharmacology</subject><subject>DNA - drug effects</subject><subject>DNA base excision repair</subject><subject>DNA Damage - drug effects</subject><subject>DNA Repair - drug effects</subject><subject>DNA-Formamidopyrimidine Glycosylase</subject><subject>Drosophila melanogaster</subject><subject>Drosophila melanogaster - physiology</subject><subject>Drosophila S3 protein</subject><subject>Fibroblasts - chemistry</subject><subject>Fibroblasts - drug effects</subject><subject>Fibroblasts - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanosine - analogs & derivatives</subject><subject>Guanosine - genetics</subject><subject>Guanosine - metabolism</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Mutagenesis. Repair</subject><subject>N-Glycosyl Hydrolases - toxicity</subject><subject>Ribosomal Proteins - isolation & purification</subject><subject>Ribosomal Proteins - pharmacology</subject><issn>0893-6692</issn><issn>1098-2280</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10Etv1DAQB3ALgei2IPEJkC-gXgJ-xY8jLWVBXeihRRytSXZCDXlhJ2L32-OygZ56Gln6zYznT8gLzt5wxsRb7HLlWj8iK86cLYSw7DFZMetkobUTR-Q4pR-Mca6ceEqOuLBGWS5XpHsfhzSMt6EFei1pDFV-dtDSMQ4Thp5CXWOLESZMNOIIIdKhobYYdsP3GfrQIx0xNkPscEurPb2dO8hd_ZZ2w5yQ5u6W4m6KUE_pGXnSQJvw-VJPyNcPFzfnH4vN1frT-btNUSsrdFEzVhqtwDaNUluQCM5JEBqFK5V11srSbkE5VwmLYA1IJkA2lak4lNIqeUJeH-bmK37NmCbfhXT3E-gx_8pz44wulc7w9ADrHEOK2Pgxhg7i3nPm76L12Pm_0Wb6cpk5V_nWe7hkmcGrBUCqoW0i9HVI965kwhhjsysO7ndocf_gQn_x-d_ixYc04e6_h_jTayNN6b99Wfsz6_h6c3njtfwDqWWd6Q</recordid><startdate>2003</startdate><enddate>2003</enddate><creator>Cappelli, Enrico</creator><creator>D'Osualdo, Andrea</creator><creator>Bogliolo, Massimo</creator><creator>Kelley, Mark R.</creator><creator>Frosina, Guido</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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></search><sort><creationdate>2003</creationdate><title>Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts</title><author>Cappelli, Enrico ; D'Osualdo, Andrea ; Bogliolo, Massimo ; Kelley, Mark R. ; Frosina, Guido</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4826-c005764a8ff44da3ea993a26e29548988358da499b28ea87a302a3fb7b1a53843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>8-oxoguanine</topic><topic>Animals</topic><topic>apurinic sites</topic><topic>Biological and medical sciences</topic><topic>Cell Extracts - chemistry</topic><topic>Cell Extracts - pharmacology</topic><topic>DNA - drug effects</topic><topic>DNA base excision repair</topic><topic>DNA Damage - drug effects</topic><topic>DNA Repair - drug effects</topic><topic>DNA-Formamidopyrimidine Glycosylase</topic><topic>Drosophila melanogaster</topic><topic>Drosophila melanogaster - physiology</topic><topic>Drosophila S3 protein</topic><topic>Fibroblasts - chemistry</topic><topic>Fibroblasts - drug effects</topic><topic>Fibroblasts - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guanosine - analogs & derivatives</topic><topic>Guanosine - genetics</topic><topic>Guanosine - metabolism</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Mutagenesis. Repair</topic><topic>N-Glycosyl Hydrolases - toxicity</topic><topic>Ribosomal Proteins - isolation & purification</topic><topic>Ribosomal Proteins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cappelli, Enrico</creatorcontrib><creatorcontrib>D'Osualdo, Andrea</creatorcontrib><creatorcontrib>Bogliolo, Massimo</creatorcontrib><creatorcontrib>Kelley, Mark R.</creatorcontrib><creatorcontrib>Frosina, Guido</creatorcontrib><collection>Istex</collection><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><jtitle>Environmental and molecular mutagenesis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cappelli, Enrico</au><au>D'Osualdo, Andrea</au><au>Bogliolo, Massimo</au><au>Kelley, Mark R.</au><au>Frosina, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts</atitle><jtitle>Environmental and molecular mutagenesis</jtitle><addtitle>Environ. Mol. Mutagen</addtitle><date>2003</date><risdate>2003</risdate><volume>42</volume><issue>1</issue><spage>50</spage><epage>58</epage><pages>50-58</pages><issn>0893-6692</issn><eissn>1098-2280</eissn><coden>EMMUEG</coden><abstract>The S3 ribosomal protein of Drosophila melanogaster possesses various DNA repair activities, including the capacity to incise at apurinic/apyrimidinic (AP) sites and 8‐oxo‐7,8‐dihydroguanine (8‐oxoG) residues. We have recently hypothesized that this multifunctional protein may improve the efficiency of DNA base excision repair (BER) in mammalian cells. We have investigated the effect of pure GST‐tagged Drosophila S3 on BER of different endogenous lesions performed by human and mouse cell extracts. Drosophila S3 significantly accelerated the BER of 8‐oxoG (initiated by the bifunctional glycosylase OGG1). The stimulating effect was linked to the capacity of S3 to remove the 8‐oxoG lesion and cleave the resulting AP site, rather than acceleration of downstream steps of the BER pathway (e.g., removal of 3′ blocking fragments). No stimulating effect was observed on the BER of uracil, natural AP sites, and β‐lyase‐cleaved AP sites. Heterologous expression of Drosophila S3 may be used to enhance 8‐oxoG repair in human cells. Environ. Mol. Mutagen. 42:50–58, 2003. © 2003 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>12874813</pmid><doi>10.1002/em.10166</doi><tpages>9</tpages></addata></record> |
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| subjects | 8-oxoguanine Animals apurinic sites Biological and medical sciences Cell Extracts - chemistry Cell Extracts - pharmacology DNA - drug effects DNA base excision repair DNA Damage - drug effects DNA Repair - drug effects DNA-Formamidopyrimidine Glycosylase Drosophila melanogaster Drosophila melanogaster - physiology Drosophila S3 protein Fibroblasts - chemistry Fibroblasts - drug effects Fibroblasts - metabolism Fundamental and applied biological sciences. Psychology Guanosine - analogs & derivatives Guanosine - genetics Guanosine - metabolism Humans Mice Molecular and cellular biology Molecular genetics Mutagenesis. Repair N-Glycosyl Hydrolases - toxicity Ribosomal Proteins - isolation & purification Ribosomal Proteins - pharmacology |
| title | Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts |
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