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Volumn 152, Issue 4, 2006, Pages 955-966

Superoxide dismutase-encoding gene of the obligate anaerobe Porphyromonas gingivalis is regulated by the redox-sensing transcription activator OxyR

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; DNA FRAGMENT; GENOMIC DNA; HYDROGEN PEROXIDE; PROTEIN OXYR; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 33645543011     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28537-0     Document Type: Article
Times cited : (41)

References (43)
  • 1
    • 0025816912 scopus 로고
    • Molecular characterization of the soxRS genes of Escherichia coli: Two genes control a superoxide stress regulon
    • Amabile-Cuevas, C. F. & Demple, B. (1991). Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulon. Nucleic Acids Res 19, 4479-4484.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4479-4484
    • Amabile-Cuevas, C.F.1    Demple, B.2
  • 2
    • 0025219013 scopus 로고
    • Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis
    • Amano, A., Shizukuishi, S., Tsumagawa, H., Iwakura, K., Tsunasawa, S. & Tsunemitsu, A. (1990). Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis. J Bacteriol 172, 1457-1463.
    • (1990) J Bacteriol , vol.172 , pp. 1457-1463
    • Amano, A.1    Shizukuishi, S.2    Tsumagawa, H.3    Iwakura, K.4    Tsunasawa, S.5    Tsunemitsu, A.6
  • 3
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Aslund, F., Zheng, M., Beckwith, J. & Storz, G. (1999). Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A 96, 6161-6165.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 4
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium-4 is homologous to a family of bacterial regulatory proteins
    • Christman, M. F., Storz, G. & Ames, B. N. (1989). OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium-4 is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci U S A 86, 3484-3488.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 5
    • 0027410196 scopus 로고
    • Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12
    • Compan, I. & Touati, D. (1993). Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12. J Bacteriol 175, 1687-1696.
    • (1993) J Bacteriol , vol.175 , pp. 1687-1696
    • Compan, I.1    Touati, D.2
  • 6
    • 2442423017 scopus 로고    scopus 로고
    • Studies on NADH oxidase and alkyl hydroperoxide reductase produced by Porphyromonas gingivalis
    • Diaz, P. I., Zilm, P. S., Wasinger, V., Corthals, G. L. & Rogers, A. H. (2004). Studies on NADH oxidase and alkyl hydroperoxide reductase produced by Porphyromonas gingivalis. Oral Microbiol Immunol 19, 137-143.
    • (2004) Oral Microbiol Immunol , vol.19 , pp. 137-143
    • Diaz, P.I.1    Zilm, P.S.2    Wasinger, V.3    Corthals, G.L.4    Rogers, A.H.5
  • 7
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • Ding, H., Hidalgo, E. & Demple, B. (1996). The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem 271, 33173-33175.
    • (1996) J Biol Chem , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 8
    • 0036148389 scopus 로고    scopus 로고
    • Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli
    • Dubrac, S. & Touati, D. (2002). Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli. Microbiology 148, 147-156.
    • (2002) Microbiology , vol.148 , pp. 147-156
    • Dubrac, S.1    Touati, D.2
  • 9
    • 0029790760 scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu, P. & Weiss, B. (1995). SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc Natl Acad Sci U S A 93, 10094-10098.
    • (1995) Proc Natl Acad Sci U S A , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 10
    • 0022273807 scopus 로고
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis. Arch Biochem Biophys 238, 83-89.
    • (1985) Arch Biochem Biophys , vol.238 , pp. 83-89
    • Gregory, E.M.1
  • 12
    • 20444471123 scopus 로고    scopus 로고
    • Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: The "red complex", a prototype polybacterial pathogenic consortium in periodontitis
    • Holt S. C. & Ebersole, J. L (2005). Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: the "red complex", a prototype polybacterial pathogenic consortium in periodontitis. Periodontol 2000 38, 72-122.
    • (2005) Periodontol 2000 , vol.38 , pp. 72-122
    • Holt, S.C.1    Ebersole, J.L.2
  • 13
    • 0030447225 scopus 로고    scopus 로고
    • Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic enviromnents
    • Iuchi, S. & Weiner, L. (1996). Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic enviromnents. J Biochem 120, 1055-1063.
    • (1996) J Biochem , vol.120 , pp. 1055-1063
    • Iuchi, S.1    Weiner, L.2
  • 15
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin dependent hydroperoxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family
    • Jeong, W., Cha, M.-K. & Kim, I.-H. (2000). Thioredoxin dependent hydroperoxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family. J Biol Chem 275,2924-2930.
    • (2000) J Biol Chem , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.-K.2    Kim, I.-H.3
  • 16
    • 3142663916 scopus 로고    scopus 로고
    • Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the vilurence of Porphyromonas gingivalis W83
    • Johnson, N. A., Liu, Y. & Fletcher, H. M. (2004). Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the vilurence of Porphyromonas gingivalis W83. Oral Microbiol Immunol 19, 233-239.
    • (2004) Oral Microbiol Immunol , vol.19 , pp. 233-239
    • Johnson, N.A.1    Liu, Y.2    Fletcher, H.M.3
  • 17
    • 15844383444 scopus 로고    scopus 로고
    • Novel stationary-phase-upregulated protein of Porphyromonas gingivalis influences production of superoxide dismutase, thiol peroxidase and thioredoxin
    • Kikuchi, Y., Ohara, N., Sato, K., Yoshimura, M, Yukitake, H., Sakai, E., Shoji, M., Naito, M. & Nakayama, K. (2005). Novel stationary-phase-upregulated protein of Porphyromonas gingivalis influences production of superoxide dismutase, thiol peroxidase and thioredoxin. Microbiology 151, 841-853.
    • (2005) Microbiology , vol.151 , pp. 841-853
    • Kikuchi, Y.1    Ohara, N.2    Sato, K.3    Yoshimura, M.4    Yukitake, H.5    Sakai, E.6    Shoji, M.7    Naito, M.8    Nakayama, K.9
  • 19
    • 0034306117 scopus 로고    scopus 로고
    • A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp)
    • Kong, W., Shiota, S., Shi, Y., Nakayama, H. & Nakayama, K. (2000). A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp). Biochem J 351, 107-114.
    • (2000) Biochem J , vol.351 , pp. 107-114
    • Kong, W.1    Shiota, S.2    Shi, Y.3    Nakayama, H.4    Nakayama, K.5
  • 20
    • 0030574283 scopus 로고    scopus 로고
    • Probing the structure of catalase HPII of Escherichia coli
    • Loewen, P. (1996). Probing the structure of catalase HPII of Escherichia coli. Gene 179, 39-44.
    • (1996) Gene , vol.179 , pp. 39-44
    • Loewen, P.1
  • 21
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse, E. & Gottesman, S. (2002). A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99, 4620-4625.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (11987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262, 10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 23
  • 24
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk, S. & Helmann, J. D. (2002). Regulation of inducible peroxide stress responses. Mol Microbiol 45, 9-15.
    • (2002) Mol Microbiol , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 25
    • 0025696672 scopus 로고
    • The superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis
    • Nakayama, K. (1990). The superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis. Gene 96, 149-150.
    • (1990) Gene , vol.96 , pp. 149-150
    • Nakayama, K.1
  • 26
    • 0028349368 scopus 로고
    • Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis
    • Nakayama, K. (1994). Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis. J Bacteriol 176, 1939-1943.
    • (1994) J Bacteriol , vol.176 , pp. 1939-1943
    • Nakayama, K.1
  • 27
    • 0028839251 scopus 로고
    • Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain) -deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence
    • Nakayama, K, Kadowaki, T., Okamoto, K. & Yamamoto, K. (1995). Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain) -deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence. J Biol Chem 270, 23619-23626.
    • (1995) J Biol Chem , vol.270 , pp. 23619-23626
    • Nakayama, K.1    Kadowaki, T.2    Okamoto, K.3    Yamamoto, K.4
  • 28
    • 0041335299 scopus 로고    scopus 로고
    • Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83
    • 20 other authors
    • Nelson, K. E., Fleischmann, R. D., DeBoy, R. T. & 20 other authors (2003). Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83. J Bacteriol 185, 5591-5601.
    • (2003) J Bacteriol , vol.185 , pp. 5591-5601
    • Nelson, K.E.1    Fleischmann, R.D.2    DeBoy, R.T.3
  • 29
    • 0033874090 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF
    • Ochsner, U. A., Vasil, M. L., Alsabbagh, E., Parvatiyar, K. & Hassett, D. J. (2000). Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. J Bacteriol 182, 4533-4544.
    • (2000) J Bacteriol , vol.182 , pp. 4533-4544
    • Ochsner, U.A.1    Vasil, M.L.2    Alsabbagh, E.3    Parvatiyar, K.4    Hassett, D.J.5
  • 30
    • 0032960139 scopus 로고    scopus 로고
    • Influence of sample preparation technique on two-dimensional gel electrophoresis of proteins from Porphyromonas gingivalis
    • Pridmore, A. M., Devine, D. A., Bonass, W. A. & Silley, P. (1999). Influence of sample preparation technique on two-dimensional gel electrophoresis of proteins from Porphyromonas gingivalis. Lett Appl Microbiol 28, 245-249.
    • (1999) Lett Appl Microbiol , vol.28 , pp. 245-249
    • Pridmore, A.M.1    Devine, D.A.2    Bonass, W.A.3    Silley, P.4
  • 31
    • 0033816764 scopus 로고    scopus 로고
    • The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis
    • Rocha, E. R., Owens, G., Jr & Smith, C. J. (2000). The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis. J Bacteriol 182, 5059-5069.
    • (2000) J Bacteriol , vol.182 , pp. 5059-5069
    • Rocha, E.R.1    Owens Jr., G.2    Smith, C.J.3
  • 33
    • 0037834629 scopus 로고    scopus 로고
    • Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily
    • Schroder, E. & Ponting, C. P. (1998). Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily. Protein Sci 7, 2465-2468.
    • (1998) Protein Sci , vol.7 , pp. 2465-2468
    • Schroder, E.1    Ponting, C.P.2
  • 34
    • 0036155121 scopus 로고    scopus 로고
    • Aerobic-type ribonucleotidereductase in the anaerobic Bacteroides fragilis
    • Smalley, D., Rocha, E. R. & Smith, C. F. (2002). Aerobic-type ribonucleotidereductase in the anaerobic Bacteroides fragilis. J Bacteriol 184, 895-903.
    • (2002) J Bacteriol , vol.184 , pp. 895-903
    • Smalley, D.1    Rocha, E.R.2    Smith, C.F.3
  • 36
    • 0002463721 scopus 로고    scopus 로고
    • Oxidative stress
    • Edited by G. Storz & R. Hengge-Aronis. Washington, DC: American Society for Microbiology
    • Storz, G. & Zheng, M. (2000). Oxidative stress. In Bacterial Stress Responses, pp. 47-59. Edited by G. Storz & R. Hengge-Aronis. Washington, DC: American Society for Microbiology.
    • (2000) Bacterial Stress Responses , pp. 47-59
    • Storz, G.1    Zheng, M.2
  • 37
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G. Tartaglia, L A. & Ames, B. N. (1990). Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248, 189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 38
    • 0028023175 scopus 로고
    • Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • Toledano, M. B., Kullik, I., Trinh, F., Baird, P. T., Schneider, T. D. & Storz, G. (1994). Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78, 897-909.
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 39
    • 0033673079 scopus 로고    scopus 로고
    • Sensing and protecting against superoxide stress in Escherichia coli - How many ways are there to trigger soxRS response
    • Touati, D. (2000). Sensing and protecting against superoxide stress in Escherichia coli - how many ways are there to trigger soxRS response? Redox Rep 5, 287-293.
    • (2000) Redox Rep , vol.5 , pp. 287-293
    • Touati, D.1
  • 40
    • 0037371197 scopus 로고    scopus 로고
    • Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis
    • Ueshima, J., Shoji, M., Ratnayake, D. B., Abe, K., Yoshida, S., Yamamoto, K. & Nakayama, K. (2003). Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect Immun 71, 1170-1178.
    • (2003) Infect Immun , vol.71 , pp. 1170-1178
    • Ueshima, J.1    Shoji, M.2    Ratnayake, D.B.3    Abe, K.4    Yoshida, S.5    Yamamoto, K.6    Nakayama, K.7
  • 41
    • 0025809949 scopus 로고
    • Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli
    • Wu, J. & Weiss, B. (1991). Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli J Bacteriol 174, 2864-2871.
    • (1991) J Bacteriol , vol.174 , pp. 2864-2871
    • Wu, J.1    Weiss, B.2
  • 42
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F. & Storz, G. (1998). Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 43
    • 0034943657 scopus 로고    scopus 로고
    • Computation-directed identification of OxyR DNA binding sites in Escherichia coli
    • Zheng, M., Wang, X., Doan, B., Lewis, K. A., Schneider, T. D. & Storz, G. (2001). Computation-directed identification of OxyR DNA binding sites in Escherichia coli. J Bacteriol 183, 4571-4579.
    • (2001) J Bacteriol , vol.183 , pp. 4571-4579
    • Zheng, M.1    Wang, X.2    Doan, B.3    Lewis, K.A.4    Schneider, T.D.5    Storz, G.6


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