Loss of an Apurinic/Apyrimidinic Site Endonuclease Increases the Mutagenicity of N-methyl-N′-nitro-N-nitrosoguanidine to Escherichia coli
xthA-Escherichia coli, which are missing a major cellular apurinic/apyrimidinic (AP) endonuclease, are 5- to 10-fold more sensitive than xthA+bacteria to mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) under conditions that induce the ``adaptive response.'' The xthA--dependent m...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1987-05, Vol.84 (9), p.2891-2895 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Foster, Patricia L. Davis, Elaine F. |
| description | xthA-Escherichia coli, which are missing a major cellular apurinic/apyrimidinic (AP) endonuclease, are 5- to 10-fold more sensitive than xthA+bacteria to mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) under conditions that induce the ``adaptive response.'' The xthA--dependent mutations are also dependent on SOS mutagenic processing and consist of both transversion and transition base substitutions. When MNNG-adapted xthA-bacteria are challenged with a high dose of MNNG, more xthA--dependent SOS-dependent mutations are induced, and transversions are enhanced relative to transitions. The mutations induced by challenge are eliminated in xthA-alkA-bacteria, which are also deficient for 3-methyladenine glycosylase II activity. These data are consistent with the hypothesis that AP sites, at least some of which are produced by glycosylase activity, are mutagenic intermediates following cellular DNA alkylation. |
| doi_str_mv | 10.1073/pnas.84.9.2891 |
| format | Article |
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The xthA--dependent mutations are also dependent on SOS mutagenic processing and consist of both transversion and transition base substitutions. When MNNG-adapted xthA-bacteria are challenged with a high dose of MNNG, more xthA--dependent SOS-dependent mutations are induced, and transversions are enhanced relative to transitions. The mutations induced by challenge are eliminated in xthA-alkA-bacteria, which are also deficient for 3-methyladenine glycosylase II activity. These data are consistent with the hypothesis that AP sites, at least some of which are produced by glycosylase activity, are mutagenic intermediates following cellular DNA alkylation.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.84.9.2891</identifier><identifier>PMID: 2437587</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Bacteria ; Bacteriology ; Biological and medical sciences ; Codon ; Codons ; Deoxyribonuclease IV (Phage T4-Induced) ; DNA ; DNA damage ; DNA-(Apurinic or Apyrimidinic Site) Lyase ; Endodeoxyribonucleases - genetics ; Endodeoxyribonucleases - metabolism ; Escherichia coli ; Escherichia coli - drug effects ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Escherichia coli Proteins ; Fundamental and applied biological sciences. Psychology ; Genetic mutation ; Genetic SOS response ; Genetics ; Lesions ; Methylnitronitrosoguanidine - pharmacology ; Microbiology ; Mutagenesis ; Mutagenicity ; Mutation ; Phenotypes ; Species Specificity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1987-05, Vol.84 (9), p.2891-2895</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c582t-9b557ec2ecf46b160dd7913aa2de055ae8ae45929bfa2cd14a2527ca481e9d333</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/84/9.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/29291$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/29291$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27929,27930,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8248245$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2437587$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Foster, Patricia L.</creatorcontrib><creatorcontrib>Davis, Elaine F.</creatorcontrib><title>Loss of an Apurinic/Apyrimidinic Site Endonuclease Increases the Mutagenicity of N-methyl-N′-nitro-N-nitrosoguanidine to Escherichia coli</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>xthA-Escherichia coli, which are missing a major cellular apurinic/apyrimidinic (AP) endonuclease, are 5- to 10-fold more sensitive than xthA+bacteria to mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) under conditions that induce the ``adaptive response.'' The xthA--dependent mutations are also dependent on SOS mutagenic processing and consist of both transversion and transition base substitutions. When MNNG-adapted xthA-bacteria are challenged with a high dose of MNNG, more xthA--dependent SOS-dependent mutations are induced, and transversions are enhanced relative to transitions. The mutations induced by challenge are eliminated in xthA-alkA-bacteria, which are also deficient for 3-methyladenine glycosylase II activity. These data are consistent with the hypothesis that AP sites, at least some of which are produced by glycosylase activity, are mutagenic intermediates following cellular DNA alkylation.</description><subject>Bacteria</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Codon</subject><subject>Codons</subject><subject>Deoxyribonuclease IV (Phage T4-Induced)</subject><subject>DNA</subject><subject>DNA damage</subject><subject>DNA-(Apurinic or Apyrimidinic Site) Lyase</subject><subject>Endodeoxyribonucleases - genetics</subject><subject>Endodeoxyribonucleases - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic mutation</subject><subject>Genetic SOS response</subject><subject>Genetics</subject><subject>Lesions</subject><subject>Methylnitronitrosoguanidine - pharmacology</subject><subject>Microbiology</subject><subject>Mutagenesis</subject><subject>Mutagenicity</subject><subject>Mutation</subject><subject>Phenotypes</subject><subject>Species Specificity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUbGOEzEQXSHQcRy0FEhILhDd5myvN2sXFNEpwEkhFEBtTbyziU8bO9jeE-no-Rs-iS_Bq4QQJCRLY-u9eW_GryieMzphtKmudw7iRIqJmnCp2IPiklHFyqlQ9GFxSSlvSim4eFw8ifGOUqpqSS-KCy6qppbNZfFj4WMkviPgyGw3BOusuZ7t9sFubTs-yCebkMxd691geoSI5NaZMF4iSRskH4YEa8xMm_aj0LLcYtrs-3L56_vP0tkUfLk81OjXA7hRF0nyZB7NBoM1GwvE-N4-LR510Ed8dqxXxZe3888378vFx3e3N7NFaWrJU6lWdd2g4Wg6MV2xKW3bRrEKgLdI6xpQAopacbXqgJuWCeA1bwwIyVC1VVVdFW8OurthtcXWoEsBer3LO0PYaw9W_4s4u9Frf68rKprpNPe_PvYH_3XAmPTWRoN9Dw79EDXLLMZkk4mTA9Hk3WPA7uTBqB7T02N6Wgqt9Jhebnh5PtmJfowr46-OOEQDfRfAGRtPNMlFPvXZgKP8Cf1jo7uh7xN-S2d-_yVm_MUBv4vJh7_j5M9l1W_Ld8iW</recordid><startdate>19870501</startdate><enddate>19870501</enddate><creator>Foster, Patricia L.</creator><creator>Davis, Elaine F.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19870501</creationdate><title>Loss of an Apurinic/Apyrimidinic Site Endonuclease Increases the Mutagenicity of N-methyl-N′-nitro-N-nitrosoguanidine to Escherichia coli</title><author>Foster, Patricia L. ; Davis, Elaine F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c582t-9b557ec2ecf46b160dd7913aa2de055ae8ae45929bfa2cd14a2527ca481e9d333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Bacteria</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Codon</topic><topic>Codons</topic><topic>Deoxyribonuclease IV (Phage T4-Induced)</topic><topic>DNA</topic><topic>DNA damage</topic><topic>DNA-(Apurinic or Apyrimidinic Site) Lyase</topic><topic>Endodeoxyribonucleases - genetics</topic><topic>Endodeoxyribonucleases - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic mutation</topic><topic>Genetic SOS response</topic><topic>Genetics</topic><topic>Lesions</topic><topic>Methylnitronitrosoguanidine - pharmacology</topic><topic>Microbiology</topic><topic>Mutagenesis</topic><topic>Mutagenicity</topic><topic>Mutation</topic><topic>Phenotypes</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Foster, Patricia L.</creatorcontrib><creatorcontrib>Davis, Elaine F.</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Foster, Patricia L.</au><au>Davis, Elaine F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Loss of an Apurinic/Apyrimidinic Site Endonuclease Increases the Mutagenicity of N-methyl-N′-nitro-N-nitrosoguanidine to Escherichia coli</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1987-05-01</date><risdate>1987</risdate><volume>84</volume><issue>9</issue><spage>2891</spage><epage>2895</epage><pages>2891-2895</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>xthA-Escherichia coli, which are missing a major cellular apurinic/apyrimidinic (AP) endonuclease, are 5- to 10-fold more sensitive than xthA+bacteria to mutagenesis by N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) under conditions that induce the ``adaptive response.'' The xthA--dependent mutations are also dependent on SOS mutagenic processing and consist of both transversion and transition base substitutions. When MNNG-adapted xthA-bacteria are challenged with a high dose of MNNG, more xthA--dependent SOS-dependent mutations are induced, and transversions are enhanced relative to transitions. The mutations induced by challenge are eliminated in xthA-alkA-bacteria, which are also deficient for 3-methyladenine glycosylase II activity. These data are consistent with the hypothesis that AP sites, at least some of which are produced by glycosylase activity, are mutagenic intermediates following cellular DNA alkylation.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2437587</pmid><doi>10.1073/pnas.84.9.2891</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Bacteriology Biological and medical sciences Codon Codons Deoxyribonuclease IV (Phage T4-Induced) DNA DNA damage DNA-(Apurinic or Apyrimidinic Site) Lyase Endodeoxyribonucleases - genetics Endodeoxyribonucleases - metabolism Escherichia coli Escherichia coli - drug effects Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genetic mutation Genetic SOS response Genetics Lesions Methylnitronitrosoguanidine - pharmacology Microbiology Mutagenesis Mutagenicity Mutation Phenotypes Species Specificity |
| title | Loss of an Apurinic/Apyrimidinic Site Endonuclease Increases the Mutagenicity of N-methyl-N′-nitro-N-nitrosoguanidine to Escherichia coli |
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