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    Evidence that covalent complex formation between BCNU-treated oligonucleotides and E. coli alkyltransferases requires the O6-alkylguanine function.

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    Authors
    Gonzaga, P E
    Harris, Linda
    Margison, Geoffrey P
    Brent, T P
    Affiliation
    Department of Biochemical and Clinical Pharmacology, St Jude Children's Research Hospital, Memphis, TN 38101.
    Issue Date
    1990-07-11
    
    Metadata
    Show full item record
    Abstract
    Chloroethylnitrosoureas (CENUs) are thought to induce cytotoxic DNA interstrand cross-links via an initial reaction at O6-position of guanine, yielding a rearranged intermediate, O6,N1-ethanoguanine. Repair of these adducts by mammalian and bacterial DNA alkyltransferases blocks the formation of cross-links. Human alkyltransferase can form a covalent complex with DNA containing BCNU-induced cross-link precursors, but the nature of the DNA-protein linkage remains unknown. Using E. coli alkyltransferases expressed by the ada and ogt genes, we now demonstrate that both enzymes can form such complexes with CENU-treated DNA. We attribute this reaction to the O6-alkylguanine repair function, because an N-terminal fragment of the ada protein, which has only alkylphosphotriester repair activity, failed to form a similar complex. This result is consistent with the idea that complex formation requires an alkyltransferase reaction with a guanine adduct, such as O6,N1-ethanoguanine. It tends to exclude the possibility that such reactions simply involve alkylation of the enzyme by reactive DNA adducts such as chloroethylphosphate or chloroethylguanine.
    Citation
    Evidence that covalent complex formation between BCNU-treated oligonucleotides and E. coli alkyltransferases requires the O6-alkylguanine function. 1990, 18 (13):3961-6 Nucleic Acids Res.
    Journal
    Nucleic Acids Research
    URI
    http://hdl.handle.net/10541/109802
    DOI
    10.1093/nar/18.13.3961
    PubMed ID
    2197601
    Type
    Article
    Language
    en
    ISSN
    0305-1048
    ae974a485f413a2113503eed53cd6c53
    10.1093/nar/18.13.3961
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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