title: Induction of E. coli oh8Gua endonuclease by oxidative stress: its significance in aerobic life.
abstract: The induction of 8-hydroxyguanine (oh8Gua) endonuclease, a DNA repair enzyme for an oxidatively modified guanine, oh8Gua was studied in various growth conditions in Escherichia coli (AB1157). Anaerobically grown E. coli were found to have a very low activity of this enzyme while aerobically grown cells showed activity about 20 times that of the anaerobic level. Under the same condition, superoxide dismutase (SOD) showed about 6-fold increase in activity. A shift in growth conditions from anaerobic to aerobic resulted in rapid induction of this enzyme, and this induction was blocked (but not completely) by chloramphenicol. It is indicated that molecular oxygen is an effective stimulator to the induction of this enzyme and its induction depends partly on protein synthesis. Superoxide-producing compounds such as paraquat and menadione also increased the activity of endonuclease as well as SOD, but H2O2 showed no effect. Thus, superoxides are also implied as a stimulator. In contrast, hyperoxia induced only SOD not the endonuclease. This induction of the endonuclease by hyperoxia was only observed in a SOD-deficient strain (QC774). The aerobic activity of the endonuclease in QC774 was the same as that of wild types (AB1157, GC4468). It is implied that the responsiveness of oh8Gua endonuclease to superoxides is less sensitive than that of SOD. The endonuclease was also induced by a temperature shift from 30 to 43 degrees C and treatment with nalidixic acid. Among the stimuli used, molecular oxygen seems to be most effective for its induction. The inducible nature of this enzyme will serve as an important mechanism for the protection of oxidative DNA damage in the aerobic environment.
authors.affiliation: Department of Pharmacology, College of Medicine, Chungbuk National University, Cheongju, South Korea.
authors.forename: H S
authors.initials: HS
authors.lastname: Kim
authors.forename: Y W
authors.initials: YW
authors.lastname: Park
authors.forename: H
authors.initials: H
authors.lastname: Kasai
authors.forename: S
authors.initials: S
authors.lastname: Nishimura
authors.forename: C W
authors.initials: CW
authors.lastname: Park
authors.forename: K H
authors.initials: KH
authors.lastname: Choi
authors.forename: M H
authors.initials: MH
authors.lastname: Chung
mesh_terms: D000332:Aerobiosis / Q000502:physiology; D001483:Base Sequence; D002455:Cell Division; D043382:DNA-Formamidopyrimidine Glycosylase; D004789:Enzyme Activation / Q000502:physiology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology; D029968:Escherichia coli Proteins; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000187:drug effects / Q000378:metabolism*; D016877:Oxidants / Q000494:pharmacology; D018384:Oxidative Stress / Q000502:physiology*; D010100:Oxygen / Q000378:metabolism / Q000494:pharmacology
chemical_list: D029968:Escherichia coli Proteins; D016877:Oxidants; D009699:N-Glycosyl Hydrolases; D043382:DNA-Formamidopyrimidine Glycosylase; C468610:DNA-formamidopyrimidine glycosylase, E coli; D010100:Oxygen