Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae
A DNA glycosylase that excises 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fap...
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| Veröffentlicht in: | Nucleic acids research 1994-09, Vol.22 (18), p.3760-3764 |
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| creator | Oliveira, R. de Kemp, P.A. van der Thomas, D Geiger, A Nehls, P Boiteux, S |
| description | A DNA glycosylase that excises 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCl. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3-methyladenine or uracil. A repair enzyme for 7,8-dihydro-8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein. |
| doi_str_mv | 10.1093/nar/22.18.3760 |
| format | Article |
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Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCl. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3-methyladenine or uracil. A repair enzyme for 7,8-dihydro-8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/22.18.3760</identifier><identifier>PMID: 7937089</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Base Sequence ; DNA ; DNA Repair - physiology ; DNA-Formamidopyrimidine Glycosylase ; enzyme activity ; Guanine - analogs & derivatives ; Guanine - metabolism ; Molecular Sequence Data ; Molecular Weight ; N-glycoside hydrolases ; N-Glycosyl Hydrolases - chemistry ; N-Glycosyl Hydrolases - isolation & purification ; N-Glycosyl Hydrolases - metabolism ; Polydeoxyribonucleotides - chemical synthesis ; Polydeoxyribonucleotides - metabolism ; pyrimidines ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology</subject><ispartof>Nucleic acids research, 1994-09, Vol.22 (18), p.3760-3764</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-b8f59c0110ba8860c05cdf224386ad96a4a3d2e5d2dcc60873936c8f4dad916a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC308359/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC308359/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7937089$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oliveira, R. de</creatorcontrib><creatorcontrib>Kemp, P.A. van der</creatorcontrib><creatorcontrib>Thomas, D</creatorcontrib><creatorcontrib>Geiger, A</creatorcontrib><creatorcontrib>Nehls, P</creatorcontrib><creatorcontrib>Boiteux, S</creatorcontrib><title>Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>A DNA glycosylase that excises 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCl. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3-methyladenine or uracil. A repair enzyme for 7,8-dihydro-8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein.</description><subject>Base Sequence</subject><subject>DNA</subject><subject>DNA Repair - physiology</subject><subject>DNA-Formamidopyrimidine Glycosylase</subject><subject>enzyme activity</subject><subject>Guanine - analogs & derivatives</subject><subject>Guanine - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>N-glycoside hydrolases</subject><subject>N-Glycosyl Hydrolases - chemistry</subject><subject>N-Glycosyl Hydrolases - isolation & purification</subject><subject>N-Glycosyl Hydrolases - metabolism</subject><subject>Polydeoxyribonucleotides - chemical synthesis</subject><subject>Polydeoxyribonucleotides - metabolism</subject><subject>pyrimidines</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks1vEzEQxS0EKqFw5YbYE7dN_bVe-8ChaimpVOAQCojLaOL1JobddWpvKva_x1WiCE49zeH93uiN3hDymtE5o0acDRjPOJ8zPRe1ok_IjAnFS2kUf0pmVNCqZFTq5-RFSr8oZZJV8oSc1EbUVJsZub4KscfeN2E7RZ-nH1xx-fm8WHeTDWnqMLnCD8W4ccXkMI3FEq3dYAz9ZF0qrIvu3ieP7iV51mKX3KvDPCW3Vx--XizKmy8fry_Ob0orlR7LlW4rYyljdIVaK2ppZZuWcym0wsYolCga7qqGN9YqqmthhLK6lU1WmUJxSt7v9253q9411g1jxA62OT3GCQJ6-F8Z_AbW4R4E1aIy2f_u4I_hbufSCL1P1nUdDi7sEtSqrjXl1aMgy8EkM_JxUCmmuFAZnO9BG0NK0bXH1IzCQ5uQ2wTOgWl4aDMb3vx76xE_1Jf1cq_7NLo_Rxnjb1C1qCtY_PgJnxZiefn9m4Bl5t_u-RYD4Dr6BLdLTpnIj2G0lEb8BXTOtTw</recordid><startdate>19940911</startdate><enddate>19940911</enddate><creator>Oliveira, R. de</creator><creator>Kemp, P.A. van der</creator><creator>Thomas, D</creator><creator>Geiger, A</creator><creator>Nehls, P</creator><creator>Boiteux, S</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19940911</creationdate><title>Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae</title><author>Oliveira, R. de ; Kemp, P.A. van der ; Thomas, D ; Geiger, A ; Nehls, P ; Boiteux, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-b8f59c0110ba8860c05cdf224386ad96a4a3d2e5d2dcc60873936c8f4dad916a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Base Sequence</topic><topic>DNA</topic><topic>DNA Repair - physiology</topic><topic>DNA-Formamidopyrimidine Glycosylase</topic><topic>enzyme activity</topic><topic>Guanine - analogs & derivatives</topic><topic>Guanine - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>N-glycoside hydrolases</topic><topic>N-Glycosyl Hydrolases - chemistry</topic><topic>N-Glycosyl Hydrolases - isolation & purification</topic><topic>N-Glycosyl Hydrolases - metabolism</topic><topic>Polydeoxyribonucleotides - chemical synthesis</topic><topic>Polydeoxyribonucleotides - metabolism</topic><topic>pyrimidines</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oliveira, R. de</creatorcontrib><creatorcontrib>Kemp, P.A. van der</creatorcontrib><creatorcontrib>Thomas, D</creatorcontrib><creatorcontrib>Geiger, A</creatorcontrib><creatorcontrib>Nehls, P</creatorcontrib><creatorcontrib>Boiteux, S</creatorcontrib><collection>AGRIS</collection><collection>Istex</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oliveira, R. de</au><au>Kemp, P.A. van der</au><au>Thomas, D</au><au>Geiger, A</au><au>Nehls, P</au><au>Boiteux, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1994-09-11</date><risdate>1994</risdate><volume>22</volume><issue>18</issue><spage>3760</spage><epage>3764</epage><pages>3760-3764</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>A DNA glycosylase that excises 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCl. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3-methyladenine or uracil. A repair enzyme for 7,8-dihydro-8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>7937089</pmid><doi>10.1093/nar/22.18.3760</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 1994-09, Vol.22 (18), p.3760-3764 |
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| language | eng |
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| subjects | Base Sequence DNA DNA Repair - physiology DNA-Formamidopyrimidine Glycosylase enzyme activity Guanine - analogs & derivatives Guanine - metabolism Molecular Sequence Data Molecular Weight N-glycoside hydrolases N-Glycosyl Hydrolases - chemistry N-Glycosyl Hydrolases - isolation & purification N-Glycosyl Hydrolases - metabolism Polydeoxyribonucleotides - chemical synthesis Polydeoxyribonucleotides - metabolism pyrimidines Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology |
| title | Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae |
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