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Volumn 173, Issue 1, 2000, Pages 78-82

Indole-inducible proteins in bacteria suggest membrane and oxidant toxicity

Author keywords

Cpx regulon; Cumene hydroperoxide; Membrane adhesion sites; Tetralin

Indexed keywords

INDOLE;

EID: 0033978494     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050012     Document Type: Article
Times cited : (71)

References (28)
  • 1
    • 0030800698 scopus 로고    scopus 로고
    • First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis
    • Antelmann H, Bernhardt J, Schmid R, Mach H, Völker U, Hecker M (1997) First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis. Electrophoresis 18:1451-1463
    • (1997) Electrophoresis , vol.18 , pp. 1451-1463
    • Antelmann, H.1    Bernhardt, J.2    Schmid, R.3    Mach, H.4    Völker, U.5    Hecker, M.6
  • 2
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44:276-287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 3
    • 0020622839 scopus 로고
    • Degradation of indole by Alcaligenes spec
    • Claus G, Kutzner HJ (1983) Degradation of indole by Alcaligenes spec. Syst Appl Microbiol 4:169-180
    • (1983) Syst Appl Microbiol , vol.4 , pp. 169-180
    • Claus, G.1    Kutzner, H.J.2
  • 4
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese PN, Silhavy TJ (1998) CpxP, a stress-combative member of the Cpx regulon. J Bacteriol 180:831-839
    • (1998) J Bacteriol , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 5
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • Demple B, Amábile-Cuevas CF (1991) Redox redux: the control of oxidative stress responses. Cell 67: 837-839
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amábile-Cuevas, C.F.2
  • 6
    • 0031129944 scopus 로고    scopus 로고
    • Biodegradation of indole at high concentration by persolvent fermentation with Pseudomonas sp. ST-200
    • Doukyu N, Aono R (1997) Biodegradation of indole at high concentration by persolvent fermentation with Pseudomonas sp. ST-200. Extremophiles 1:100-105
    • (1997) Extremophiles , vol.1 , pp. 100-105
    • Doukyu, N.1    Aono, R.2
  • 7
    • 0032015703 scopus 로고    scopus 로고
    • SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms
    • Ehrenshaft M, Jenns AE, Chung KR, Daub ME (1998) SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms. Mol Cell 1:603-609
    • (1998) Mol Cell , vol.1 , pp. 603-609
    • Ehrenshaft, M.1    Jenns, A.E.2    Chung, K.R.3    Daub, M.E.4
  • 8
    • 0033529936 scopus 로고    scopus 로고
    • A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis
    • Ehrenshaft M, Bilski P, Li MY, Chignell CF, Daub ME (1999) A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. Proc Natl Acad Sci USA 96:9374-9378
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9374-9378
    • Ehrenshaft, M.1    Bilski, P.2    Li, M.Y.3    Chignell, C.F.4    Daub, M.E.5
  • 9
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Fair SB, Kogoma T (1991) Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev 55: 561-585
    • (1991) Microbiol Rev , vol.55 , pp. 561-585
    • Fair, S.B.1    Kogoma, T.2
  • 10
    • 0029128195 scopus 로고
    • Cloning of an organic solvent-resistance gene in Escherichia coli: The unexpected role of alkylhydroperoxide reductase
    • Ferrante AA, Augliera J, Lewis K, Klibanov AM (1995) Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase. Proc Natl Acad Sci USA 2:7617-7621
    • (1995) Proc Natl Acad Sci USA , vol.2 , pp. 7617-7621
    • Ferrante, A.A.1    Augliera, J.2    Lewis, K.3    Klibanov, A.M.4
  • 11
    • 0032893417 scopus 로고    scopus 로고
    • Response to reactive nitrogen intermediates in Mycobacterium tuberculosis: Induction of the 16-kilodalton alpha-crystalline homolog by exposure to nitric oxide donors
    • Garbe TR, Hibler NS, Deretic V (1999) Response to reactive nitrogen intermediates in Mycobacterium tuberculosis: induction of the 16-kilodalton alpha-crystalline homolog by exposure to nitric oxide donors. Infect Immun 67:460-465
    • (1999) Infect Immun , vol.67 , pp. 460-465
    • Garbe, T.R.1    Hibler, N.S.2    Deretic, V.3
  • 12
    • 0025369970 scopus 로고
    • The measurement and mechanism of lipid peroxidation in biological systems
    • Gutteridge JMC, Halliwell B (1990) The measurement and mechanism of lipid peroxidation in biological systems. Trends Biochem Sci 15:129-135
    • (1990) Trends Biochem Sci , vol.15 , pp. 129-135
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 13
    • 0030906081 scopus 로고    scopus 로고
    • A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells
    • Hagenmaier S, Stierhof Y-D, Henning U (1997) A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells. J Bacteriol 179: 2073-2076
    • (1997) J Bacteriol , vol.179 , pp. 2073-2076
    • Hagenmaier, S.1    Stierhof, Y.-D.2    Henning, U.3
  • 14
    • 0008943936 scopus 로고    scopus 로고
    • Mechanisms of DNA transformation
    • Neidhardt FC (ed) American Society Microbiology, Washington, DC
    • Hanahan D, Bloom FR (1996) Mechanisms of DNA transformation. In: Neidhardt FC (ed) Escherichia coli and Salmonella, 2nd edn. American Society Microbiology, Washington, DC, 2449-2459
    • (1996) Escherichia Coli and Salmonella, 2nd Edn. , pp. 2449-2459
    • Hanahan, D.1    Bloom, F.R.2
  • 15
    • 0019494586 scopus 로고
    • Induction of Heinz body formation by sodium dithionite
    • Imanishi H, Hosokawa K, Itano HA (1981) Induction of Heinz body formation by sodium dithionite. Hemoglobin 5:453-461
    • (1981) Hemoglobin , vol.5 , pp. 453-461
    • Imanishi, H.1    Hosokawa, K.2    Itano, H.A.3
  • 16
    • 0025012839 scopus 로고
    • New pathway for the biodegradation of indole in Aspergillus niger
    • Kamath AV, Vaidyanathan CS (1990) New pathway for the biodegradation of indole in Aspergillus niger. Appl Environ Microbiol 56:275-280
    • (1990) Appl Environ Microbiol , vol.56 , pp. 275-280
    • Kamath, A.V.1    Vaidyanathan, C.S.2
  • 17
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: Redox cycling and lipid peroxidation
    • Kappus H, Sies H (1981) Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 37:1233-1241
    • (1981) Experientia , vol.37 , pp. 1233-1241
    • Kappus, H.1    Sies, H.2
  • 18
    • 0025378940 scopus 로고
    • Electroporation-transformation system for corynebacteria by auxotrophic complementation
    • Kurusu Y, Kainuma M, Inui M, Satoh Y, Yukawa H (1990) Electroporation-transformation system for corynebacteria by auxotrophic complementation. Agric Biol Chem 54:443-447
    • (1990) Agric Biol Chem , vol.54 , pp. 443-447
    • Kurusu, Y.1    Kainuma, M.2    Inui, M.3    Satoh, Y.4    Yukawa, H.5
  • 19
    • 0028303794 scopus 로고
    • Comparative toxicity of alkyl-1,4-naphthoquinones in rats: Relationship to free radical production in vitro
    • Munday R, Fowke EA, Smith BL, Munday CM (1994) Comparative toxicity of alkyl-1,4-naphthoquinones in rats: relationship to free radical production in vitro. Free Radic Biol Med 16: 725-731
    • (1994) Free Radic Biol Med , vol.16 , pp. 725-731
    • Munday, R.1    Fowke, E.A.2    Smith, B.L.3    Munday, C.M.4
  • 20
    • 0030068461 scopus 로고    scopus 로고
    • Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen
    • Nohl H, Gille E, Schönheit K, Liu Y (1996) Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen. Free Radic Biol Med 20:207-213
    • (1996) Free Radic Biol Med , vol.20 , pp. 207-213
    • Nohl, H.1    Gille, E.2    Schönheit, K.3    Liu, Y.4
  • 21
    • 0032408936 scopus 로고    scopus 로고
    • The biochemical, pathophysiological, and medical aspects of ubiquinone function
    • Nohl H, Gille L, Staniek K (1998) The biochemical, pathophysiological, and medical aspects of ubiquinone function. Ann NY Acad Sci 854:394-409
    • (1998) Ann NY Acad Sci , vol.854 , pp. 394-409
    • Nohl, H.1    Gille, L.2    Staniek, K.3
  • 22
    • 0002660099 scopus 로고    scopus 로고
    • Periplasm
    • Neidhardt FC (ed) American Society Microbiology, Washington, DC
    • Oliver DB (1996) Periplasm. In: Neidhardt FC (ed) Escherichia coli and Salmonella, 2nd edn. American Society Microbiology, Washington, DC, pp 88-103
    • (1996) Escherichia Coli and Salmonella, 2nd Edn. , pp. 88-103
    • Oliver, D.B.1
  • 25
    • 0026723765 scopus 로고
    • Effects of the membrane action of tetralin on the functional and structural properties of artificial and bacterial membranes
    • Sikkema J, Poolman B, Konings WN, de Bont JA (1992) Effects of the membrane action of tetralin on the functional and structural properties of artificial and bacterial membranes. J Bacteriol 174:2986-2992
    • (1992) J Bacteriol , vol.174 , pp. 2986-2992
    • Sikkema, J.1    Poolman, B.2    Konings, W.N.3    De Bont, J.A.4
  • 27
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Storz G, Jacobson FS, Tartaglia LA, Morgan RW, Silveira LA, Ames BN (1989) An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J Bacteriol 171:2049-2055
    • (1989) J Bacteriol , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 28
    • 0025365949 scopus 로고
    • Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases
    • Tartaglia LA, Storz G, Brodsky MH, Lai A, Ames BN (1990) Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J Biol Chem 265: 10535-10540
    • (1990) J Biol Chem , vol.265 , pp. 10535-10540
    • Tartaglia, L.A.1    Storz, G.2    Brodsky, M.H.3    Lai, A.4    Ames, B.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.