Mechanism of regulation of 8-hydroxyguanine endonuclease oxidative stress: Roles of fnr, arcA, and fur

Free Radical Biology and Medicine

Volumn 24, Issue 7-8, 1998, Pages 1193-1201

  Lee, Hye Sook ^a   Lee, Yun Song ^b   Kim, Hun Sik ^c   Choi, Jeong Yun ^a   Hassan, Hosni M ^d   Chung, Myung Hee ^a  

^a Seoul National University College of Medicine   (South Korea)

^b University of Ulsan College of Medicine   (South Korea)

^c Chungbuk National University College of Medicine   (South Korea)

^d Department of Microbiology   (United States)

Author keywords

DNA repair; FPG; Free radical; MutM; Oh8Gua endonuclease; Regulation; Regulon genes

Indexed keywords

8 HYDROXYGUANINE; ENDONUCLEASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; METAL CHELATE; PARAQUAT; SUPEROXIDE DISMUTASE;

ARTICLE; BACTERIAL GENETICS; DETOXIFICATION; DNA REPAIR; ENZYME INDUCTION; ENZYME REGULATION; ESCHERICHIA COLI; GENE CONTROL; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; REGULON; SIGNAL TRANSDUCTION;

BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; BASE SEQUENCE; CATALASE; CHELATING AGENTS; DNA, BACTERIAL; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE; ENZYME INDUCTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FREE RADICALS; GENES, BACTERIAL; GLUCOSEPHOSPHATE DEHYDROGENASE; HYDROGEN PEROXIDE; IRON-SULFUR PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; N-GLYCOSYL HYDROLASES; OXIDATIVE STRESS; PARAQUAT; REPRESSOR PROTEINS; SUPEROXIDE DISMUTASE;

ARCA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032078778     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00427-9     Document Type: Article

References (65)

1. Kasai H., Crain P. F., Kuchino T., Nishimura S., Ootsuyama A., Tanooka H. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis. 7:1986;1849-1851.
2. Kasai H., Nishimura S., Kurokawa Y., Hayashi Y. Oral administration of the renal carcinogen, potassium bromate, specifically produces 8-hydroxy-deoxyguanosine in rat target organ DNA. Carcinogenesis. 8:1987;1959-1961.
3. Kasai H., Nishimura S. Formation of 8-Hydroxydeoxyguanosine in DNA by oxygen radicals and its biological significance. Sies H. Oxidative stress; oxidants and antioxidants. 1991;99-116 Academic Press, London.
4. Shibutani S., Takeshita M., Grollman A. P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
5. Kamiya H., Miura K., Ishikawa H., Inoue H., Nishimura S., Ohtsuka E. c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions. Cancer Res. 52:1992;3483-3485.
6. Chung M.H., Kasai H., Jones D.S., Inoue H., Ishikawa H., Ohtsuka E., Nishimura S. An endonuclease activity of Escherichia coli that specifically removes 8-hydroxyguanine residues from DNA. Mutation Res. 254:1991;1-12.
7. Tchou J., Kasai H., Shibutani S., Chung M. H., Laval J., Grollman A. P., Nishmura S. 8-oxoguanine (8-hydroxyguanine) DNA glycosylase and its substrate specificity. Proc. Natl. Acad. Sci. USA. 88:1991;4690-4694.
8. Lee Y. S., Lee H. S., Park M. K., Hwang E. S., Park E. M., Kasai H., Chung M. H. Identification of 8-hydroxyguanine glycosylase activity in mammalian tissues using 8-hydroxyguanine specific monoclonal antibody. Biochem. Biophys. Res. Commun. 196:1993;1545-1551.
9. Boiteux S., O'Connor T. R., Lederer F., Gouyette A., Laval J. Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem. 265:1990;3916-3922.
10. Cabrera M., Nghiem Y., Miller J. H. mutM, a second mutator locus in Escherichia coli that generates G:C→T:A transversions. J. Bacteriol. 170:1988;5405-5407.
11. Michaels M. L., Pham L., Cruz C., Miller J. H. MutM, a protein that prevents G:C→T:A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 19:1991;3629-3632.
12. 8Gua endonuclease by oxidative stress: Its significance in aerobic life. Mutation Res. 363:1996;115-124.
13. Niederhoffer E. C., Naranjo C. M., Bradley K. L., Fee J. A. Control of E. coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. J. Bacteriol. 172:1990;1930-1938.
14. Demple B., Amabile-Cuevas C. F. Redox redux The control of oxidative stress response . Cell. 67:1991;837-839.
15. Hassan H. M., Sun H.-C. Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in E. coli. Proc. Natl. Acad. Sci. USA. 89:1992;3217-3221.
16. Schellhorn H. E. Regulation of hydroperoxidase (catalase) expression in E. coli. FEMS Microbiol. Lett. 131:1994;113-119.
17. Chung, M. H.; Kim, H. S.; Ohtsuka, E.; Kasai, H.; Yamamoto, F.; Nishimura, S. An endonuclease activity in human polymorphonuclear neutrophils that removes 8-hydroxyguanine residues from DNA [published erratum appears in Biochem. Biophys. Res. Commun.180(1):462; 1991]. Biochem. Biophys. Res. Commun. 178:1472-1478; 1991.
18. Chung, M. H.; Kim, H. S.; Ohtsuka, E.; Kasai, H.; Yamamoto, F.; Nishimura, S. An endonuclease activity in human polymorphonuclear neutrophils that removes 8-hydroxyguanine residues from DNA [published erratum appears in Biochem. Biophys. Res. Commun.180(1):462; 1991]. Biochem. Biophys. Res. Commun. 178:1472-1478; 1991.
19. Yamamoto F., Kasai H., Bessho T., Chung M. H., Inoue H., Ohtsuka E., Hori T., Nishimura S. Ubiquitous presence in mammalian cells of enzymatic activity specifically cleaving 8-hydroxyguanine-containing DNA. Jpn. J. Cancer Res. 83:1992;351-357.
20. Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. 1989;A3 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
21. 32P]cordycepin-5′-triphosphate. Gene. 10:1980;177-183.
22. Smith P. K., Krohr R. I., Hermanson G. T., Mallia A. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:1985;76-85.
23. McCord J., Fridovich I. Superoxide dismutase; an enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:1969;6049-6055.
24. Beer R. F., Sizer I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195:1952;133-140.
25. Dutch J. Glucose-6-phosphate dehydrogenase. Bergmeyer H.U., Berhmeyer J., Grassl M. Methods of Enzymatic Analysis. 3rd ed. 1983;190-197 Verlag Chemie, Wieheim, Deerfield Beach, Florida.
26. Hassan H. M., Fridovich I. Regulation of the synthesis of superoxide dismutase in E. coli induction by methyl viologen. J. Biol. Chem. 252:1977;7667-7672.
27. Richter H. E., Loewen P. C. Induction of catalase in E. coli by ascorbic acid involves hydrogen peroxide. Biochem. Biophys. Res. Commun. 100:1981;1039-1046.
28. Christman M. F., Morgan R. W., Jacobson F. S., Ames B. N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhymurium. Cell. 41:1985;753-762.
29. Wu J., Weiss B. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of E. coli. J. Bacteriol. 173:1991;2864-2871.
30. Greenberg J. T., Monach P., Chou J. H., Josephy P. D., Demple B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in E. coli. Proc. Natl. Acad. Sci. USA. 87:1990;6181-6185.
31. Tsaneva I. R., Weiss B. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172:1990;4197-4205.
32. Moody C. S., Hassan H. M. Anaerobic biosynthesis of the manganese-containing superoxide dismutase in E. coli. J. Biol. Chem. 259:1984;12821-12825.
33. 2 and iron availability. Arch. Microbiol. 156:1991;463-470.
34. Hassan H. M. Microbial superoxide dismutases. Adv. Genet. 26:1989;65-97.
35. Tardat B., Touati D. Two global regulators repress the anaerobic expression of MnSOD in E. coli: fur and arc. Mol. Microbiol. 5:1991;455-465.
36. Beaumont M. D., Hassan H. M. Characterization of trans-acting regulatory elements affecting the expression of Mn-superoxide dismutase (sodA) in E. coli. Curr. Microbiol. 25:1992;135-141.
37. Bowen S. W., Hassan H. M. Characterization of cis-acting regulatory mutations causing anaerobic expression of the sodA gene in E. coli. Arch. Biochem. Biophys. 302:1993;372-379.
38. Hassan H. M., Schrum L. W. Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in E. coli. FEMS Microbiol. Rev. 14:1994;315-324.
39. Wu J., Weiss B. Two-stage induction of the soxRS(superoxide response) regulon of E. coli. J. Bacteriol. 174:1992;3915-3920.
40. Storz G., Tartaglia L. A., Ames B. N. Transcriptional regulator of oxidative stress-inducible genes Direct activation by oxidation . Science. 248:1990;180-194.
41. Schiavone J. R., Hassan H. M. The role of redox in the regulation of manganese-containing superoxide dismutase biosynthesis in E. coli. J. Biol. Chem. 263:1988;4269-4273.
42. Bagg A., Neilands J. B. Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in E. coli. Biochemistry. 26:1987;5471-5477.
43. Spiro S., Guest J. R. FNR and its role in oxygen-regulated gene expression in E. coli. FEMS Microbiol. Rev. 75:1990;399-428.
44. Spiro S., Robert R. E., Guest J. R. FNR-dependent repression of the ndh gene of Escherichia coli and metal ion requirement for FNR-regulated gene expression. Mol. Microbiol. 3:1989;601-608.
45. Cotter P. A., Chepuri V., Gennis R. B., Gunsalus R. P. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in E. coli is regulated by oxygen, pH, and the fnr gene product. J. Bacteriol. 172:1990;6333-6338.
46. Unden G., Trageser M., Duchene A. Effect of positive redox potentials (greater than +400 mM) on the expression of anaerobic respiratory enzyme in E. coli. Mol. Microbiol. 4:1990;315-319.
47. Green J., Sharrocks A. D., Green B., Geisow M., Guest J. R. Properties of FNR proteins substituted at each of the five cysteine residues. Mol. Microbiol. 8:1993;61-68.
48. Green J., Guest J. A role of iron in transcriptional activation by FNR. FEBS Lett. 329:1993;55-58.
49. Khoroshilova N., Beinert H., Kiley P. J. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc. Natl. Acad. Sci. USA. 92:1995;2499-2503.
50. 2 as the regulatory signal for FNR-dependent gene regulation in E. coli. J. Bacteriol. 178:1996;4515-4521.
51. Iuchi S., Lin E.C.C. arcA(dye), a global regulatory gene in E. coli mediating repression of enzymes in aerobic pathways. Proc. Natl. Acad. Sci. USA. 85:1988;1888-1892.
52. Lynch A. S., Lin E. C. C. Transcriptional control mediated by the ArcA two-component response regulator protein of E. coli: Characterization of DNA binding at target promoters. J. Bacteriol. 178:1996;6238-6249.
53. Bessho T., Tano K., Kasai H., Nishimura S. Deficiency of 8-hydroxyguanine DNA endonuclease activity and accumulation of the 8-hydroxyguanine in mutator mutant (mutM) of E. coli. Biochem. Biophys. Res. Commun. 188:1992;372-378.
54. Laval F. Expression of the E. coli fpg gene in mammalian cells reduces the mutagenicity of gamma-rays. Nucleic Acids Res. 22:1994;4943-4946.
55. Fraga C. G., Shigenega M. K., Park J.-W., Degan P., Ames B. N. Oxidative damage to DNA during aging 8-hydroxy-2'-deoxyguanosine in rat organ DNA and urine . Proc. Natl. Acad. Sci. USA. 87:1990;4533-4537.
56. 3), a renal oxidative carcinogen. Mutat. Res. 364:1996;227-233.
57. Bachmann B. J. Pedigrees of mutant strains of E. coli K-12. Bacteriol. Rev. 36:1972;525-527.
58. Carlioz A., Touati D. Isolation of superoxide dismutase mutants in E. coli: Is superoxide dismutase necessary for aerobic life? EMBO J. 5:1986;623-630.
59. Aranki A., Freter R. Use of anaerobic glove boxes for the cultivation of strictly anaerobic bacteria. Am. J. Clin. Nutr. 25:1969;1329-1334.
60. Greenberg J. T., Demple B. A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. J. Bacteriol. 171:1989;3933-3939.
61. Bagg A., Neilands J. B. Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol. Rev. 51:1987;509-518.
62. Sharrocks A., Green J., Guest J. FNR activates and represses transcription in vitro. Proc. R. Soc. Lond. B. 245:1991;219-226.
63. Iuchi S., Lim E. C. C. Adaptation of Escherichia coli to respiratory conditions Regulation of gene expression . Cell. 66:1991;5-7.
64. s. J. Bacteriol. 179:1997;3164-3170.
65. Park S. J., Gunsalus R. P. Oxygen, iron, carbon and superoxide control the fumarase fumA and fumC genes of Escherichia coli. Role of the arcA, fnr, and soxR gene products. J. Bacteriol. 177:1995;6255-6262.