메뉴 건너뛰기




Volumn 45, Issue 6, 2002, Pages 1647-1654

OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CUMENE HYDROPEROXIDE; HYDROGEN PEROXIDE; MESSENGER RNA; PROTEIN OHRR; TERT BUTYL HYDROPEROXIDE; UNCLASSIFIED DRUG;

EID: 0036032183     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03116.x     Document Type: Article
Times cited : (51)

References (25)
  • 1
    • 0032792553 scopus 로고    scopus 로고
    • Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli marRAB locus, by multiple chemicals in vitro
    • Alekshun, M.N., and Levy, S.B. (1999) Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli marRAB locus, by multiple chemicals in vitro. J Bacteriol 181: 4669-4672.
    • (1999) J Bacteriol , vol.181 , pp. 4669-4672
    • Alekshun, M.N.1    Levy, S.B.2
  • 2
    • 0034915594 scopus 로고    scopus 로고
    • Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression
    • Atichartpongkul, S., Loprasert, S., Vattanaviboon, P., Whangsuk, W., Helmann, J.D., and Mongkolsuk, S. (2001) Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression. Microbiology 147: 1775-1782.
    • (2001) Microbiology , vol.147 , pp. 1775-1782
    • Atichartpongkul, S.1    Loprasert, S.2    Vattanaviboon, P.3    Whangsuk, W.4    Helmann, J.D.5    Mongkolsuk, S.6
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., and Rhee, S.G. (1994) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 91: 7017-7021.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 5
    • 0036365511 scopus 로고    scopus 로고
    • Escherichia coli SoxR protein: Sensor/transducer of oxidative stress and nitric oxide
    • Demple, B., Ding, H., and Jorgensen, M. (2002) Escherichia coli SoxR protein: sensor/transducer of oxidative stress and nitric oxide. Meth Enzymol 348: 355-364.
    • (2002) Meth Enzymol , vol.348 , pp. 355-364
    • Demple, B.1    Ding, H.2    Jorgensen, M.3
  • 6
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., and Helmann, J.D. (2002) The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc Natl Acad Sci USA 99: 6690-6695.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 7
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S., and Helmann, J.D. (2001) OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J Bacteriol 183: 4134-4141.
    • (2001) J Bacteriol , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 8
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B., and Gutteridge, J.M. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219: 1-14.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 9
    • 0023200985 scopus 로고
    • A survey of chemicals inducing lipid peroxidation in biological systems
    • Kappus, H. (1987) A survey of chemicals inducing lipid peroxidation in biological systems. Chem Phys Lipids 45: 105-115.
    • (1987) Chem Phys Lipids , vol.45 , pp. 105-115
    • Kappus, H.1
  • 11
    • 0033774725 scopus 로고    scopus 로고
    • Molecular and physiological analysis of an OxyR-regulated ahpC promoter in Xanthomonas campestris pv. phaseoli
    • Loprasert, S., Fuangthong, M., Whangsuk, W., Atichartpongkul, S., and Mongkolsuk, S. (2000) Molecular and physiological analysis of an OxyR-regulated ahpC promoter in Xanthomonas campestris pv. phaseoli. Mol Microbiol 37: 1504-1514.
    • (2000) Mol Microbiol , vol.37 , pp. 1504-1514
    • Loprasert, S.1    Fuangthong, M.2    Whangsuk, W.3    Atichartpongkul, S.4    Mongkolsuk, S.5
  • 12
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons
    • de Lorenzo, V., and Timmis, K.N. (1994) Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Meth Enzymol 235: 386-405.
    • (1994) Meth Enzymol , vol.235 , pp. 386-405
    • De Lorenzo, V.1    Timmis, K.N.2
  • 13
    • 0030974196 scopus 로고    scopus 로고
    • Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk, S., Loprasert, S., Whangsuk, W., Fuangthong, M., and Atichartpongkun, S. (1997) Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli. J Bacteriol 179: 3950-3955.
    • (1997) J Bacteriol , vol.179 , pp. 3950-3955
    • Mongkolsuk, S.1    Loprasert, S.2    Whangsuk, W.3    Fuangthong, M.4    Atichartpongkun, S.5
  • 14
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk, S., Praituan, W., Loprasert, S., Fuangthong, M., and Chamnongpol, S. (1998) Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli. J Bacteriol 180: 2636-2643.
    • (1998) J Bacteriol , vol.180 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 15
    • 0034047382 scopus 로고    scopus 로고
    • Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris
    • Mongkolsuk, S., Whangsuk, W., Fuangthong, M., and Loprasert, S. (2000) Mutations in oxyR resulting in peroxide resistance in Xanthomonas campestris. J Bacteriol 182: 3846-3849.
    • (2000) J Bacteriol , vol.182 , pp. 3846-3849
    • Mongkolsuk, S.1    Whangsuk, W.2    Fuangthong, M.3    Loprasert, S.4
  • 17
    • 0035157997 scopus 로고    scopus 로고
    • Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa
    • Ochsner, U.A., Hassett, D.J., and Vasil, M.L. (2001) Genetic and physiological characterization of ohr, encoding a protein involved in organic hydroperoxide resistance in Pseudomonas aeruginosa. J Bacteriol 183: 773-778.
    • (2001) J Bacteriol , vol.183 , pp. 773-778
    • Ochsner, U.A.1    Hassett, D.J.2    Vasil, M.L.3
  • 18
    • 0030032612 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins
    • Poole, L.B., and Ellis, H.R. (1996) Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35: 56-64.
    • (1996) Biochemistry , vol.35 , pp. 56-64
    • Poole, L.B.1    Ellis, H.R.2
  • 19
    • 0036156059 scopus 로고    scopus 로고
    • ohr, encoding an organic hydroperoxide reductase, is an in vivo-induced gene in Actinobacillus pleuropneumoniae
    • Shea, R.J., and Mulks, M.H. (2002) ohr, encoding an organic hydroperoxide reductase, is an in vivo-induced gene in Actinobacillus pleuropneumoniae. Infect Immun 70: 794-802.
    • (2002) Infect Immun , vol.70 , pp. 794-802
    • Shea, R.J.1    Mulks, M.H.2
  • 20
    • 0034944405 scopus 로고    scopus 로고
    • Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-inducible negative regulator, and post-transcriptional modifications
    • Sukchawalit, R., Loprasert, S., Atichartpongkul, S., and Mongkolsuk, S. (2001) Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-inducible negative regulator, and post-transcriptional modifications. J Bacteriol 183: 4405-4412.
    • (2001) J Bacteriol , vol.183 , pp. 4405-4412
    • Sukchawalit, R.1    Loprasert, S.2    Atichartpongkul, S.3    Mongkolsuk, S.4
  • 21
    • 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., and 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
  • 22
    • 0031039492 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae exhibits a yAP-1-mediated adaptive response to malondialdehyde
    • Turton, H.E., Dawes, I.W., and Grant, C.M. (1997) Saccharomyces cerevisiae exhibits a yAP-1-mediated adaptive response to malondialdehyde. J Bacteriol 179: 1096-1101.
    • (1997) J Bacteriol , vol.179 , pp. 1096-1101
    • Turton, H.E.1    Dawes, I.W.2    Grant, C.M.3
  • 23
    • 0033989856 scopus 로고    scopus 로고
    • Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli
    • Vattanaviboon, P., and Mongkolsuk, S. (2000) Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli. Gene 241: 259-265.
    • (2000) Gene , vol.241 , pp. 259-265
    • Vattanaviboon, P.1    Mongkolsuk, S.2
  • 24
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng, M., and Storz, G. (2000) Redox sensing by prokaryotic transcription factors. Biochem Pharmacol 59: 1-6.
    • (2000) Biochem Pharmacol , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 25
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F., and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.