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dc.contributor.authorLi, Qiong
dc.contributor.authorLaval, Jacques
dc.contributor.authorLudlum, David B.
dc.date2022-08-11T08:09:53.000
dc.date.accessioned2022-08-23T16:47:13Z
dc.date.available2022-08-23T16:47:13Z
dc.date.issued1997-05-01
dc.date.submitted2008-06-18
dc.identifier.citation<p>Carcinogenesis. 1997 May;18(5):1035-8.</p>
dc.identifier.issn0143-3334 (Print)
dc.identifier.pmid9163692
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41036
dc.description.abstractTransfection of the Escherichia coli fpg gene into Chinese hamster ovary cells has been reported to enhance survival after exposure to aziridine (C.Cussac and F.Laval, 1996, Nucleic Acids Res., 24, 1742-1746). This result suggests that Fpg protein protects cells from toxicity by removing ring-opened N-7 guanine adducts from DNA, and raises the possibility that Fpg protein would offer protection from other agents that alkylate the N-7 position of guanine. Since the major adduct formed by sulfur mustard in DNA is 7-hydroxyethyl-thioethylguanine (HETEG), we have investigated the action of Fpg protein on the ring-opened form of this adduct (ro-HETEG). A substrate containing ro-HETEG was prepared by alkaline treatment of DNA modified by [14C]sulfur mustard. Fpg protein purified from an over-producing strain of E. coli released ro-HETEG from this substrate in an enzyme- and time-dependent manner, and at a rate that is similar to that at which it releases ring-opened 7-methylguanine. Thus, Fpg protein acts efficiently on ro-HETEG, and may offer some protection against the toxic action of sulfur mustard.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9163692&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1093/carcin/18.5.1035
dc.subjectAdenine
dc.subjectAlkylation
dc.subjectCarcinogens
dc.subjectDNA Adducts
dc.subjectDNA-Formamidopyrimidine Glycosylase
dc.subjectEscherichia coli
dc.subject*Escherichia coli Proteins
dc.subjectGuanine
dc.subjectMustard Gas
dc.subjectN-Glycosyl Hydrolases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleFpg protein releases a ring-opened N-7 guanine adduct from DNA that has been modified by sulfur mustard
dc.typeJournal Article
dc.source.journaltitleCarcinogenesis
dc.source.volume18
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/383
dc.identifier.contextkey533095
html.description.abstract<p>Transfection of the Escherichia coli fpg gene into Chinese hamster ovary cells has been reported to enhance survival after exposure to aziridine (C.Cussac and F.Laval, 1996, Nucleic Acids Res., 24, 1742-1746). This result suggests that Fpg protein protects cells from toxicity by removing ring-opened N-7 guanine adducts from DNA, and raises the possibility that Fpg protein would offer protection from other agents that alkylate the N-7 position of guanine. Since the major adduct formed by sulfur mustard in DNA is 7-hydroxyethyl-thioethylguanine (HETEG), we have investigated the action of Fpg protein on the ring-opened form of this adduct (ro-HETEG). A substrate containing ro-HETEG was prepared by alkaline treatment of DNA modified by [14C]sulfur mustard. Fpg protein purified from an over-producing strain of E. coli released ro-HETEG from this substrate in an enzyme- and time-dependent manner, and at a rate that is similar to that at which it releases ring-opened 7-methylguanine. Thus, Fpg protein acts efficiently on ro-HETEG, and may offer some protection against the toxic action of sulfur mustard.</p>
dc.identifier.submissionpathoapubs/383
dc.contributor.departmentDepartment of Pharmacology and Molecular Toxicology
dc.source.pages1035-8


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