title: Ntg2 of Saccharomyces cerevisiae repairs the oxidation products of 8-hydroxyguanine.
abstract: In Escherichia coli, endonuclease III (endo III) repairs the oxidation products of 8-OHGua. However, the corresponding repair enzymes in eukaryotes have not been identified. Here we report that 8-hydroxyguanine (8-OHGua) is highly sensitive to further oxidation. We also show that Ntg2, a functional homolog of endo III in Saccharomyces cerevisiae, is capable of nicking the irradiated duplex DNA containing 8-OHGua. Moreover, Ntg2 formed a stable complex with the DNA upon incubation with NaBH(4). In contrast, Ntg1, another functional homolog of endo III, showed no such activities. These findings indicate that Ntg2 is, at least in part, responsible for repairing the oxidation products of 8-OHGua in eukaryotic cells.
authors.affiliation: Department of Pharmacology, Seoul National University College of Medicine, 28 Yongon-dong, Chongno-gu, Seoul, 110-799, Korea.
authors.forename: J E
authors.initials: JE
authors.lastname: Kim
authors.forename: H J
authors.initials: HJ
authors.lastname: You
authors.forename: J Y
authors.initials: JY
authors.lastname: Choi
authors.forename: P W
authors.initials: PW
authors.lastname: Doetsch
authors.forename: J S
authors.initials: JS
authors.lastname: Kim
authors.forename: M H
authors.initials: MH
authors.lastname: Chung
mesh_terms: D001894:Borohydrides / Q000494:pharmacology; D004247:DNA / Q000737:chemistry / Q000528:radiation effects; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D043382:DNA-Formamidopyrimidine Glycosylase; D003839:Deoxyadenosines / Q000737:chemistry; D003841:Deoxycytidine / Q000737:chemistry; D003849:Deoxyguanosine / Q000737:chemistry; D004307:Dose-Response Relationship, Radiation; D029968:Escherichia coli Proteins; D005720:Gamma Rays; D006147:Guanine / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000528:radiation effects; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000494:pharmacology; D017665:Hydroxyl Radical / Q000737:chemistry / Q000494:pharmacology; D007501:Iron / Q000737:chemistry / Q000494:pharmacology; D046911:Macromolecular Substances; D009699:N-Glycosyl Hydrolases / Q000737:chemistry*; D010084:Oxidation-Reduction; D010880:Piperidines / Q000737:chemistry; D011485:Protein Binding / Q000187:drug effects / Q000502:physiology; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity / Q000528:radiation effects; D013936:Thymidine / Q000737:chemistry
chemical_list: D001894:Borohydrides; D003839:Deoxyadenosines; D029968:Escherichia coli Proteins; C045076:Fenton's reagent; D046911:Macromolecular Substances; D010880:Piperidines; D029701:Saccharomyces cerevisiae Proteins; D003841:Deoxycytidine; D017665:Hydroxyl Radical; C024829:8-hydroxyguanine; D006147:Guanine; C032727:piperidine; C025364:sodium borohydride; D004247:DNA; D006861:Hydrogen Peroxide; D007501:Iron; D009699:N-Glycosyl Hydrolases; D043382:DNA-Formamidopyrimidine Glycosylase; C468610:DNA-formamidopyrimidine glycosylase, E coli; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; C101825:NTG1 protein, S cerevisiae; C116827:NTG2 protein, S cerevisiae; D003849:Deoxyguanosine; D013936:Thymidine