Repair of Oxidatively Induced DNA Damage by DNA Glycosylases: Mechanisms of Action, Substrate Specificities and Excision Kinetics
Miral M. Dizdar, Erdem Coskun, Pawel Jaruga
ABSTRACT Endogenous and exogenous reactive species cause oxidatively induced DNA damage in living organisms by a variety of mechanisms. As a result, a plethora of mutagenic and/or cytotoxic products are formed in cellular DNA. This type of DNA damage is repaired by base excision repair, although nucleotide excision repair also plays a limited role. DNA glycosylases remove modified DNA bases from DNA by hydrolyzing the glycosidic bond leaving behind an apurinic/apyrimidinic (AP) site. Some of them also possess an accompanying AP lyase activity that cleaves the sugar-phosphate chain of DNA. Since the first discovery of a DNA glycosylase, many studies have elucidated the mechanisms of action, substrate specificities and excision kinetics of these enzymes present in all living organisms. For this purpose, most studies used single- or double-stranded oligodeoxynucleotides with a single DNA lesion embedded at a defined position. High-molecular weight DNA with multiple base lesions has been used in other studies with the advantage of the simultaneous investigation of many DNA base lesions as substrates. Differences between the substrate specificities and excision kinetics of DNA glycosylases have been found when these two different substrates were used.
, Coskun, E.
and Jaruga, P.
Repair of Oxidatively Induced DNA Damage by DNA Glycosylases: Mechanisms of Action, Substrate Specificities and Excision Kinetics, Mutation Research-Reviews in Mutation Research, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=922326
(Accessed March 1, 2024)