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- W1995421049 abstract "DNA adducts are mutagenic and clastogenic. Because of their harmful nature, lesions are recognized by many proteins involved in DNA repair. However, mounting evidence suggests that lesions also are recognized by proteins with no obvious role in repair processes. One such protein is topoisomerase II, an essential enzyme that removes knots and tangles from the DNA. Because topoisomerase II generates a protein-linked double-stranded DNA break during its catalytic cycle, it has the potential to fragment the genome. Previous studies indicate that abasic sites and other lesions that distort the double helix stimulate topoisomerase II-mediated DNA cleavage. Therefore, to further explore interactions between DNA lesions and the enzyme, the effects of exocyclic adducts on DNA cleavage mediated by human topoisomerase IIα were determined. When located within the four-base overhang of a topoisomerase II cleavage site (at the +2 or +3 position 3‘ relative to the scissile bond), 3,N4-ethenodeoxycytidine, 3,N4-etheno-2‘-ribocytidine, 1,N2-ethenodeoxyguanosine, pyrimido[1,2-a]purin-10(3H)-one deoxyribose (M1dG), and 1,N2-propanodeoxyguanosine increased DNA scission ∼5−17-fold. Enhanced cleavage did not result from an increased affinity of topoisomerase IIα for adducted DNA or a decreased rate of religation. Therefore, it is concluded that these exocyclic lesions act by accelerating the forward rate of enzyme-mediated DNA scission. Finally, treatment of cultured human cells with 2-chloroacetaldehyde, a reactive metabolite of vinyl chloride that generates etheno adducts, increased cellular levels of DNA cleavage by topoisomerase IIα. This finding suggests that type II topoisomerases interact with exocyclic DNA lesions in physiological systems." @default.
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- W1995421049 date "2005-02-12" @default.
- W1995421049 modified "2023-09-27" @default.
- W1995421049 title "Exocyclic DNA Lesions Stimulate DNA Cleavage Mediated by Human Topoisomerase IIα in Vitro and in Cultured Cells" @default.
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- W1995421049 doi "https://doi.org/10.1021/bi0478289" @default.
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