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Volumn 18, Issue 15, 1999, Pages 4292-4298

RsrA, an anti-sigma factor regulated by redox change

Author keywords

Anti sigma factor; Disulfide bond formation; Oxidative stress; Redox regulation; Thioredoxin

Indexed keywords

BACTERIAL PROTEIN; SIGMA FACTOR; THIOL; THIOREDOXIN;

EID: 0033517138     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.15.4292     Document Type: Article
Times cited : (223)

References (25)
  • 1
    • 0027479268 scopus 로고
    • Characterization of a broad-range disulfide reductase from Streptomyces clavuligerus and its possible role in β-lactam antibiotic biosynthesis
    • Aharonowitz, Y., Av-Gay, Y., Schreiber, R. and Cohen, G. (1993) Characterization of a broad-range disulfide reductase from Streptomyces clavuligerus and its possible role in β-lactam antibiotic biosynthesis. J. Bacteriol., 175, 623-629.
    • (1993) J. Bacteriol. , vol.175 , pp. 623-629
    • Aharonowitz, Y.1    Av-Gay, Y.2    Schreiber, R.3    Cohen, G.4
  • 2
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: Sensing stress by disulfide bond formation
    • Åslund, F. and Beckwith, J. (1999) Bridge over troubled waters: sensing stress by disulfide bond formation. Cell, 96, 751-753.
    • (1999) Cell , vol.96 , pp. 751-753
    • Åslund, F.1    Beckwith, J.2
  • 3
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Åslund, F., Berndt, K.D. and Holmgren, A. (1997) Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem., 272, 30780-30786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 4
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman, M.F., Morgan, R.W., Jacobson, F.S. and Ames, B.N. (1985) Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell, 41, 753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 5
    • 0027282914 scopus 로고
    • Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus: Sequences, expression, and organization of the genes
    • Cohen, G., Yanko, M., Mislovati, M., Argaman, A., Schreiber, R., Av-Gay, Y. and Aharonowitz, Y. (1993) Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus: sequences, expression, and organization of the genes. J. Bacteriol., 175, 5159-5167.
    • (1993) J. Bacteriol. , vol.175 , pp. 5159-5167
    • Cohen, G.1    Yanko, M.2    Mislovati, M.3    Argaman, A.4    Schreiber, R.5    Av-Gay, Y.6    Aharonowitz, Y.7
  • 6
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T. et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature, 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1
  • 7
    • 0001922433 scopus 로고
    • Disulphide bonds between cysteine residues
    • Creighton, T.E., (ed.), IRL Press, Oxford, UK
    • Creighton, T.E (1989) Disulphide bonds between cysteine residues. In Creighton, T.E., (ed.), Protein Structure. IRL Press, Oxford, UK, p. 156.
    • (1989) Protein Structure , pp. 156
    • Creighton, T.E.1
  • 8
    • 0032513315 scopus 로고    scopus 로고
    • A bridge to control
    • Demple, B. (1998) A bridge to control. Science, 279, 1655-1656.
    • (1998) Science , vol.279 , pp. 1655-1656
    • Demple, B.1
  • 9
    • 0032213238 scopus 로고    scopus 로고
    • Bacterial senescence: Stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon
    • Dukan, S. and Nyström, T. (1998) Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev., 12, 3431-3441.
    • (1998) Genes Dev. , vol.12 , pp. 3431-3441
    • Dukan, S.1    Nyström, T.2
  • 10
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert, H.F. (1990) Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol., 63, 69-72.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.63 , pp. 69-72
    • Gilbert, H.F.1
  • 11
    • 0031882182 scopus 로고    scopus 로고
    • A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei
    • Gostick, D.O., Green, J., Irvine, A.S., Gasson, M.J. and Guest, J.R. (1998) A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei. Microbiology, 144, 705-717.
    • (1998) Microbiology , vol.144 , pp. 705-717
    • Gostick, D.O.1    Green, J.2    Irvine, A.S.3    Gasson, M.J.4    Guest, J.R.5
  • 12
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. (1989) Thioredoxin and glutaredoxin systems. J. Biol. Chem., 264, 13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 13
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A.J. and Lodish, H.F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science, 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 14
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob, U., Muse, W., Eser, M. and Bardwell, J.C.A. (1999) Chaperone activity with a redox switch. Cell, 96, 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 15
    • 0030856418 scopus 로고    scopus 로고
    • Identification of sigma factors for growth phase-related promoter selectivity of RNA polymerases from Streptomyces coelicolor A3(2)
    • Kang, J.-G., Hahn, M.-Y., Ishihama, A. and Roe, J.-H. (1997) Identification of sigma factors for growth phase-related promoter selectivity of RNA polymerases from Streptomyces coelicolor A3(2). Nucleic Acids Res., 25, 2566-2573.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2566-2573
    • Kang, J.-G.1    Hahn, M.-Y.2    Ishihama, A.3    Roe, J.-H.4
  • 16
    • 0028848166 scopus 로고
    • A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins
    • Loferer, H., Wunderlich, M., Hennecke, H. and Glockshuber, R. (1995) A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins. J. Biol. Chem., 270, 26178-26183.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26178-26183
    • Loferer, H.1    Wunderlich, M.2    Hennecke, H.3    Glockshuber, R.4
  • 17
    • 9244225687 scopus 로고    scopus 로고
    • Distribution of thiols in microorganisms: Mycothiol is a major thiol in most actinomycetes
    • Newton, G.L. et al. (1996) Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J. Bacteriol., 178, 1990-1995.
    • (1996) J. Bacteriol. , vol.178 , pp. 1990-1995
    • Newton, G.L.1
  • 18
    • 0032190375 scopus 로고    scopus 로고
    • R, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2)
    • R, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). EMBO J., 17, 5776-5782.
    • (1998) EMBO J. , vol.17 , pp. 5776-5782
    • Paget, M.S.B.1    Kang, J.-G.2    Roe, J.-H.3    Buttner, M.J.4
  • 19
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz, W.A., Åslund, F., Holmgren, A. and Beckwith, J. (1997) The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem., 272, 15661-15667.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Åslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 20
    • 0030765627 scopus 로고    scopus 로고
    • Making and breaking disulfide bonds
    • Raina, S. and Missiakas, D. (1997) Making and breaking disulfide bonds. Annu. Rev. Microbiol., 51, 179-202.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 179-202
    • Raina, S.1    Missiakas, D.2
  • 21
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • Rietsch, A. and Beckwith, J. (1998) The genetics of disulfide bond metabolism. Annu. Rev. Genet., 32, 163-184.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 22
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak, J. and Lindsay, R.H. (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem., 25, 192-205.
    • (1968) Anal. Biochem. , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 23
    • 0030724011 scopus 로고    scopus 로고
    • High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein, HPr
    • Seok, Y.J., Sondej, M., Badawi, P., Lewis, M.S., Briggs, M.C., Jaffe, H. and Peterkofsky, A. (1997) High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein, HPr. J. Biol. Chem., 272, 26511-26521.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26511-26521
    • Seok, Y.J.1    Sondej, M.2    Badawi, P.3    Lewis, M.S.4    Briggs, M.C.5    Jaffe, H.6    Peterkofsky, A.7
  • 24
    • 0030930252 scopus 로고    scopus 로고
    • oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress
    • Tao, K. (1997) oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress. J. Bacteriol., 179, 5967-5970.
    • (1997) J. Bacteriol. , vol.179 , pp. 5967-5970
    • Tao, K.1
  • 25
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, 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    Åslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.