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    Fpg protein releases a ring-opened N-7 guanine adduct from DNA that has been modified by sulfur mustard

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    Authors
    Li, Qiong
    Laval, Jacques
    Ludlum, David B.
    UMass Chan Affiliations
    Department of Pharmacology and Molecular Toxicology
    Document Type
    Journal Article
    Publication Date
    1997-05-01
    Keywords
    Adenine
    Alkylation
    Carcinogens
    DNA Adducts
    DNA-Formamidopyrimidine Glycosylase
    Escherichia coli
    *Escherichia coli Proteins
    Guanine
    Mustard Gas
    N-Glycosyl Hydrolases
    Life Sciences
    Medicine and Health Sciences
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    Link to Full Text
    https://doi.org/10.1093/carcin/18.5.1035
    Abstract
    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.
    Source

    Carcinogenesis. 1997 May;18(5):1035-8.

    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/41036
    PubMed ID
    9163692
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