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Volumn 136, Issue 5, 2004, Pages 607-615

Activation of SoxR-dependent transcription in Pseudomonas aeruginosa

Author keywords

Iron sulfur cluster; Pseudomonas aeruginosa; Redox signal; SoxR; Transcription activator

Indexed keywords

IRON SULFUR PROTEIN; MESSENGER RNA; PARAQUAT; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SOXR; TRANSCRIPTION FACTOR SOXS; UNCLASSIFIED DRUG;

EID: 14944340675     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh168     Document Type: Article
Times cited : (50)

References (40)
  • 1
    • 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. Methods Enzymol. 348, 355-364
    • (2002) Methods Enzymol. , vol.348 , pp. 355-364
    • Demple, B.1    Ding, H.2    Jorgensen, M.3
  • 2
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello, P.J. and Demple, B. (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19, 109-114
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 3
    • 0025816912 scopus 로고
    • Molecular characterization of the soxRS genes of Escherichia coli: Two genes control a superoxide stress regulon
    • Amábile Cuevas, C.F. and 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
    • Amábile Cuevas, C.F.1    Demple, B.2
  • 4
    • 0025809949 scopus 로고
    • Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli
    • Wu, J. and Weiss, B. (1991) Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli. J. Bacteriol. 173, 2864-2871
    • (1991) J. Bacteriol. , vol.173 , pp. 2864-2871
    • Wu, J.1    Weiss, B.2
  • 5
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba, T., deRojas-Walker, T., Wishnok, J.S. Tannenbaum, S.R., and Demple, B. (1993) Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages. Proc. Natl Acad. Sci. USA 90, 9993-9997
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 6
    • 0028960382 scopus 로고
    • Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages
    • Nunoshiba, T., deRojas-Walker, T., Tannenbaum, S.R., and Demple, B. (1995) Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Infect. Immun. 63, 794-798
    • (1995) Infect. Immun. , vol.63 , pp. 794-798
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Tannenbaum, S.R.3    Demple, B.4
  • 7
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator
    • Ding, H. and Demple, B. (2000) Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator. Proc. Natl Acad. Sci. USA 97, 5146-5150
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 8
    • 0028929893 scopus 로고
    • Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli
    • Wu, J., Williams, R.D., and Weiss, B. (1995) Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli. J. Biol. Chem. 270, 10323-1032
    • (1995) J. Biol. Chem. , vol.270 , pp. 10323-11032
    • Wu, J.1    Williams, R.D.2    Weiss, B.3
  • 9
    • 0029152251 scopus 로고
    • Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • Hidalgo, E., Bollinger, J.M. Jr., Bradley, T.M., Walsh, C.T., and Demple, B. (1995) Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270, 20908-20914
    • (1995) J. Biol. Chem. , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger Jr., J.M.2    Bradley, T.M.3    Walsh, C.T.4    Demple, B.5
  • 10
    • 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., and 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
  • 11
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu, P. and Weiss, B. (1996) SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl Acad. Sci. USA 93, 10094-10098
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 12
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding, H. and Demple, B. (1997) In vivo kinetics of a redox-regulated transcriptional switch. Proc. Natl Acad. Sci. USA 94, 8445-8449
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 13
    • 0031048106 scopus 로고    scopus 로고
    • Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo
    • Gaudu, P., Moon, N., and Weiss, B. (1997) Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo. J. Biol. Chem. 272, 5082-5086
    • (1997) J. Biol. Chem. , vol.272 , pp. 5082-5086
    • Gaudu, P.1    Moon, N.2    Weiss, B.3
  • 14
    • 0030936964 scopus 로고    scopus 로고
    • Redox signal transduction: Mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form
    • Hidalgo, E.E., Ding, H. and Demple, B. (1997) Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 88, 121-129
    • (1997) Cell , vol.88 , pp. 121-129
    • Hidalgo, E.E.1    Ding, H.2    Demple, B.3
  • 15
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg, J.T., Monach, P., Chou, J.H., Josephy, D., and Demple, B. (1990) Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl Acad. Sci. USA 87, 6181-6185
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, D.4    Demple, B.5
  • 16
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva, I.R. and Weiss, B. (1990) soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172, 4197-4205
    • (1990) J. Bacteriol. , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 17
    • 0030983818 scopus 로고    scopus 로고
    • Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli
    • White, D.G., Goldman, J.D., Demple, B., and Levy, S.V. (1997) Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli. J. Bacteriol. 179, 6122-6126
    • (1997) J. Bacteriol. , vol.179 , pp. 6122-6126
    • White, D.G.1    Goldman, J.D.2    Demple, B.3    Levy, S.V.4
  • 18
    • 0028924091 scopus 로고
    • Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein
    • Ariza, R.R., Li, Z., Ringstad, N., and Demple, B. (1995) Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein. J. Bacteriol. 177, 1655-1661
    • (1995) J. Bacteriol. , vol.177 , pp. 1655-1661
    • Ariza, R.R.1    Li, Z.2    Ringstad, N.3    Demple, B.4
  • 19
    • 0027411681 scopus 로고
    • Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: Positive control of the micF antisense RNA by the soxRS locus
    • Chou, J.H., Greenberg, J.T., and Demple, B. (1993) Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus. J. Bacteriol. 175, 1026-1031
    • (1993) J. Bacteriol. , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 20
    • 0032079338 scopus 로고    scopus 로고
    • The redox-regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator
    • Hidalgo, F.E., Leautaud, V., and Demple, B. (1998) The redox-regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator. EMBO J. 17, 2629-2636
    • (1998) EMBO J. , vol.17 , pp. 2629-2636
    • Hidalgo, F.E.1    Leautaud, V.2    Demple, B.3
  • 22
    • 0027215943 scopus 로고
    • A simple and rapid method for the preparation of gram-negative bacterial genomic DNA
    • Chen, W. and Kuo, T. (1993) A simple and rapid method for the preparation of gram-negative bacterial genomic DNA. Nucleic Acids Res. 21, 2260
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2260
    • Chen, W.1    Kuo, T.2
  • 23
    • 0028049068 scopus 로고
    • An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
    • Hidalgo, E. and Demple, B. (1994) An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J. 13, 138-146
    • (1994) EMBO J. , vol.13 , pp. 138-146
    • Hidalgo, E.1    Demple, B.2
  • 24
    • 0033021117 scopus 로고    scopus 로고
    • Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli
    • Kobayashi, K. and Tagawa, S. (1999) Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli. FEBS Lett. 451, 227-230
    • (1999) FEBS Lett. , vol.451 , pp. 227-230
    • Kobayashi, K.1    Tagawa, S.2
  • 25
    • 2442452545 scopus 로고    scopus 로고
    • The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus
    • Newberry, K.J. and Brennan, R.G. (2004) The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus. J. Biol. Chem. 279, 20356-20362
    • (2004) J. Biol. Chem. , vol.279 , pp. 20356-20362
    • Newberry, K.J.1    Brennan, R.G.2
  • 26
    • 0022183725 scopus 로고
    • Biochemical characterization of a paraquat-tolerant mutant of Escherichia coli
    • Kao, S.M. and Hassen, H.M. (1985) Biochemical characterization of a paraquat-tolerant mutant of Escherichia coli. J. Biol. Chem. 260, 10478-10481
    • (1985) J. Biol. Chem. , vol.260 , pp. 10478-10481
    • Kao, S.M.1    Hassen, H.M.2
  • 27
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 29
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • Liochev, S.I. and Fridovich, I. (1992) Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl Acad. Sci. USA 89, 5892-5896
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 30
    • 0029796248 scopus 로고    scopus 로고
    • Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein
    • Ding, H. and Demple, B. (1996) Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein. Proc. Natl Acad. Sci. USA 93, 9449-9453
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9449-9453
    • Ding, H.1    Demple, B.2
  • 31
    • 0032497908 scopus 로고    scopus 로고
    • Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR
    • Ding, H. and Demple, B. (1998) Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR. Biochemistry 37, 17280-17286
    • (1998) Biochemistry , vol.37 , pp. 17280-17286
    • Ding, H.1    Demple, B.2
  • 32
    • 0032884073 scopus 로고    scopus 로고
    • Expression of the soxR gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia
    • Ha, U. and Jin, S. (1999) Expression of the soxR gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia. Infect. Immun. 67, 5324-5331
    • (1999) Infect. Immun. , vol.67 , pp. 5324-5331
    • Ha, U.1    Jin, S.2
  • 33
    • 0031041391 scopus 로고    scopus 로고
    • Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor
    • Hidalgo, E. and Demple, B. (1997) Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor. EMBO J. 16, 1056-1065
    • (1997) EMBO J. , vol.16 , pp. 1056-1065
    • Hidalgo, E.1    Demple, B.2
  • 34
    • 0028358807 scopus 로고
    • SoxS, an activator of superoxide stress genes in Escherichia coli. Purification and interaction with DNA
    • Li, Z. and Demple, B. (1994) SoxS, an activator of superoxide stress genes in Escherichia coli. Purification and interaction with DNA. J. Biol. Chem. 269, 18371-18377
    • (1994) J. Biol. Chem. , vol.269 , pp. 18371-18377
    • Li, Z.1    Demple, B.2
  • 35
    • 0023027071 scopus 로고
    • Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB
    • Lundrigan, M.D. and Kadner, R.J. (1986) Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB. J. Biol. Chem. 261, 10797-10801
    • (1986) J. Biol. Chem. , vol.261 , pp. 10797-10801
    • Lundrigan, M.D.1    Kadner, R.J.2
  • 36
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm, E., Mende, J., Braun, V., and Kamp, R.M. (1987) Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 169, 3350-3357
    • (1987) J. Bacteriol. , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 37
    • 0024593726 scopus 로고
    • Evolutionary relationship between the TonB-dependent outer membrane transport proteins: Nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene
    • Nau, C.D. and Konisky, J. (1989) Evolutionary relationship between the TonB-dependent outer membrane transport proteins: nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene. J. Bacteriol. 171, 1041-1047
    • (1989) J. Bacteriol. , vol.171 , pp. 1041-1047
    • Nau, C.D.1    Konisky, J.2
  • 38
    • 0024368556 scopus 로고
    • Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport
    • Gudmunsdottir, A., Bell, P.E., Lundrigan, M.D., Bradbeer, and Kadner, R.J. (1989) Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport. J. Bacteriol. 171, 6526-6533
    • (1989) J. Bacteriol. , vol.171 , pp. 6526-6533
    • Gudmunsdottir, A.1    Bell, P.E.2    Lundrigan, M.D.3    Bradbeer4    Kadner, R.J.5
  • 39
    • 0029966305 scopus 로고    scopus 로고
    • Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: Cycle selection of iron-regulated genes
    • Ochsner, U.A. and Vasil, M.L. (1996) Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: Cycle selection of iron-regulated genes. Proc. Natl Acad. Sci. USA 93, 4409-4414
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4409-4414
    • Ochsner, U.A.1    Vasil, M.L.2
  • 40
    • 0037076382 scopus 로고    scopus 로고
    • Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa
    • Lamont, I.L., Beare, P.A., Ochsner, U., Vasil, A.I., and Vasil, M.L. (2002) Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa. Proc. Natl Acad. Sci. USA 99, 7027-7027
    • (2002) Proc. Natl. Sci. USA , vol.99 , pp. 7027-7027
    • Lamont, I.L.1    Beare, P.A.2    Ochsner, U.3    Vasil, A.I.4    Vasil, M.L.5


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