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• W2001362843 startingPage "13851" @default.
• W2001362843 abstract "An important feature of the common DNA oxidation product 8-oxo-7,8-dihydroguanine (OG) is its susceptibility to further oxidation that produces guanidinohydantoin (Gh) and spiroiminodihydantoin (Sp) lesions. In the presence of amines, G or OG oxidation produces hydantoin amine adducts. Such adducts may form in cells via interception of oxidized intermediates by protein-derived nucleophiles or naturally occurring amines that are tightly associated with DNA. Gh and Sp are known to be substrates for base excision repair (BER) glycosylases; however, large Sp–amine adducts would be expected to be more readily repaired by nucleotide excision repair (NER). A series of Sp adducts differing in the size of the attached amine were synthesized to evaluate the relative processing by NER and BER. The UvrABC complex excised Gh, Sp, and the Sp–amine adducts from duplex DNA, with the greatest efficiency for the largest Sp–amine adducts. The affinity of UvrA for all of the lesion duplexes was found to be similar, whereas the efficiency of UvrB loading tracked with the efficiency of UvrABC excision. In contrast, the human BER glycosylase NEIL1 exhibited robust activity for all Sp–amine adducts irrespective of size. These studies suggest that both NER and BER pathways mediate repair of a diverse set of hydantoin lesions in cells." @default.
• W2001362843 created "2016-06-24" @default.
• W2001362843 creator A5003239051 @default.
• W2001362843 creator A5005659666 @default.
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• W2001362843 creator A5042677072 @default.
• W2001362843 creator A5050502321 @default.
• W2001362843 creator A5055919829 @default.
• W2001362843 date "2013-09-05" @default.
• W2001362843 modified "2023-10-02" @default.
• W2001362843 title "Repair of Hydantoin Lesions and Their Amine Adducts in DNA by Base and Nucleotide Excision Repair" @default.
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