메뉴 건너뛰기




Volumn 69, Issue 6, 2003, Pages 3406-3411

Increasing the oxidative stress response allows Escherichia coli to overcome inhibitory effects of condensed tannins

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; HYDROGEN PEROXIDE; PHENOLS; TOXICITY;

EID: 0037641066     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.6.3406-3411.2003     Document Type: Article
Times cited : (61)

References (34)
  • 1
    • 0033990087 scopus 로고    scopus 로고
    • The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment
    • Aiyar, A. 2000. The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment. Methods Mol. Biol. 132:221-241.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 221-241
    • Aiyar, A.1
  • 2
    • 0001187084 scopus 로고
    • Use of dye-labeled protein as spectrophotometric assay for protein precipitants such as tannin
    • Asquith, T. N., and L. G. Butler. 1985. Use of dye-labeled protein as spectrophotometric assay for protein precipitants such as tannin. J. Chem. Ecol. 11:1535-1544.
    • (1985) J. Chem. Ecol. , vol.11 , pp. 1535-1544
    • Asquith, T.N.1    Butler, L.G.2
  • 3
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman, M. F., R. W. Morgan, F. S. Jacobson, and B. N. Ames. 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
  • 4
    • 0032409385 scopus 로고    scopus 로고
    • Mechanism of inhibition of tannic acid and related compounds on the growth of intestinal bacteria
    • Chung, K. T., Z. Lu, and M. W. Chou. 1998. Mechanism of inhibition of tannic acid and related compounds on the growth of intestinal bacteria. Food Chem. Toxicol. 36:1053-1060.
    • (1998) Food Chem. Toxicol. , vol.36 , pp. 1053-1060
    • Chung, K.T.1    Lu, Z.2    Chou, M.W.3
  • 5
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Costa Seaver, L., and J. A. Imlay. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:7173-7181.
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Costa Seaver, L.1    Imlay, J.A.2
  • 6
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Costa Seaver, L., and J. A. Imlay. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183:7182-7189.
    • (2001) J. Bacteriol. , vol.183 , pp. 7182-7189
    • Costa Seaver, L.1    Imlay, J.A.2
  • 7
    • 0024064790 scopus 로고
    • Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants
    • Greenberg, J. T., and B. Demple. 1988. Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants. EMBO J. 7:2611-2617.
    • (1988) EMBO J. , vol.7 , pp. 2611-2617
    • Greenberg, J.T.1    Demple, B.2
  • 9
    • 0033250139 scopus 로고    scopus 로고
    • Interaction of tea catechins with lipid bilayers investigated with liposome systems
    • Hashimoto, T., S. Kumazawa, F. Nanjo, Y. Hara, and T. Nakayama. 1999. Interaction of tea catechins with lipid bilayers investigated with liposome systems. Biosci. Biotechnol. Biochem. 63:2252-2255.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2252-2255
    • Hashimoto, T.1    Kumazawa, S.2    Nanjo, F.3    Hara, Y.4    Nakayama, T.5
  • 10
    • 0033822849 scopus 로고    scopus 로고
    • Bactericidal activity of catechin-copper (II) complexes against Staphylococcus aureus compared with Escherichia coli
    • Hoshino, N., T. Kimura, F. Hayakawa, A. Yamaji, and T. Ando. 2000. Bactericidal activity of catechin-copper (II) complexes against Staphylococcus aureus compared with Escherichia coli. Lett. Appl. Microbiol. 31:213-217.
    • (2000) Lett. Appl. Microbiol. , vol.31 , pp. 213-217
    • Hoshino, N.1    Kimura, T.2    Hayakawa, F.3    Yamaji, A.4    Ando, T.5
  • 11
    • 0033408462 scopus 로고    scopus 로고
    • Damage to the cytoplasmic membrane of Escherichia coli by catechin-copper (II) complexes
    • Hoshino, N., T. Kimura, A. Yamaji, and T. Ando. 1999. Damage to the cytoplasmic membrane of Escherichia coli by catechin-copper (II) complexes. Free Radic. Biol. Med. 27:1245-1250.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1245-1250
    • Hoshino, N.1    Kimura, T.2    Yamaji, A.3    Ando, T.4
  • 13
    • 0030941215 scopus 로고    scopus 로고
    • Sealing effects of (-)-epigallocatechin gallate on protein kinase C and protein phosphatase 2A
    • Kitano, K., K. Y. Nam, S. Kimura, H. Fujiki, and Y. Imanishi. 1997. Sealing effects of (-)-epigallocatechin gallate on protein kinase C and protein phosphatase 2A. Biophys. Chem. 65:157-164.
    • (1997) Biophys. Chem. , vol.65 , pp. 157-164
    • Kitano, K.1    Nam, K.Y.2    Kimura, S.3    Fujiki, H.4    Imanishi, Y.5
  • 14
    • 0033804622 scopus 로고    scopus 로고
    • Heat-induced, metal-catalyzed oxidative degradation of quercetin and rutin (quercetin 3-O -rhamnosylglucoside) in aqueous model systems
    • Makris, D., and J. Rossiter. 2000. Heat-induced, metal-catalyzed oxidative degradation of quercetin and rutin (quercetin 3-O -rhamnosylglucoside) in aqueous model systems. J. Agric. Food Chem. 48:3830-3838.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 3830-3838
    • Makris, D.1    Rossiter, J.2
  • 15
    • 0001368233 scopus 로고    scopus 로고
    • Precipitation of metal ions by plant polyphenols: Optimal conditions and origin of precipitation
    • McDonald, M., I. Mila, and A. Scalbert. 1996. Precipitation of metal ions by plant polyphenols: optimal conditions and origin of precipitation. J. Agric. Food Chem. 44:599-606.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 599-606
    • McDonald, M.1    Mila, I.2    Scalbert, A.3
  • 16
    • 0033538048 scopus 로고    scopus 로고
    • The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
    • Messner, K. R., and J. A. Imlay. 1999. The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J. Biol. Chem. 274:10119-10128.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10119-10128
    • Messner, K.R.1    Imlay, J.A.2
  • 17
    • 0025353046 scopus 로고
    • Identification of phosphate starvation-inducible genes in Escherichia coli K-12 by DNA sequence analysis of psi::lacZ(Mu d1) transcriptional fusions
    • Metcalf, W. W., P. M. Steed, and B. L. Wanner. 1990. Identification of phosphate starvation-inducible genes in Escherichia coli K-12 by DNA sequence analysis of psi::lacZ(Mu d1) transcriptional fusions. J. Bacteriol. 172:3191-3200.
    • (1990) J. Bacteriol. , vol.172 , pp. 3191-3200
    • Metcalf, W.W.1    Steed, P.M.2    Wanner, B.L.3
  • 18
  • 21
    • 0023872648 scopus 로고
    • Interaction of flavonoids with 1,1-diphenyl-2-picrylhydrazyl free radical, liposomal membranes and soybean lipoxygenase-1
    • Ratty, A. K., J. Sunamoto, and N. P. Das. 1988. Interaction of flavonoids with 1,1-diphenyl-2-picrylhydrazyl free radical, liposomal membranes and soybean lipoxygenase-1. Biochem. Pharmacol. 37:989-995.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 989-995
    • Ratty, A.K.1    Sunamoto, J.2    Das, N.P.3
  • 22
    • 0032913243 scopus 로고    scopus 로고
    • Hydrogen peroxide and coffee induce G:C→T:A transversions in the lacI gene of catalase-defective Escherichia coli
    • Ruiz-Laguna, J., and C. Pueyo. 1999. Hydrogen peroxide and coffee induce G:C→T:A transversions in the lacI gene of catalase-defective Escherichia coli. Mutagenesis 14:95-102.
    • (1999) Mutagenesis , vol.14 , pp. 95-102
    • Ruiz-Laguna, J.1    Pueyo, C.2
  • 23
    • 31144447841 scopus 로고
    • Antimicrobial properties of tannins
    • Scalbert, A. 1991. Antimicrobial properties of tannins. Phytochemistry 30: 3875-3883.
    • (1991) Phytochemistry , vol.30 , pp. 3875-3883
    • Scalbert, A.1
  • 26
    • 0000269492 scopus 로고
    • Tannins from four common Acacia species of Texas and northeastern Mexico
    • Seigler, D. S., S. Seilheimer, J. Keesy, and H. F. Huang. 1986. Tannins from four common Acacia species of Texas and northeastern Mexico. Econ. Bot. 40:220-232.
    • (1986) Econ. Bot. , vol.40 , pp. 220-232
    • Seigler, D.S.1    Seilheimer, S.2    Keesy, J.3    Huang, H.F.4
  • 27
    • 0002789825 scopus 로고
    • Oxygen with phenols and related reactions in musts, wines, and model systems: Observations with practical implications
    • Singleton, V. L. 1987. Oxygen with phenols and related reactions in musts, wines, and model systems: observations with practical implications. Am. J. Enol. Vitic. 38:69-77.
    • (1987) Am. J. Enol. Vitic. , vol.38 , pp. 69-77
    • Singleton, V.L.1
  • 28
    • 0028809521 scopus 로고
    • Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase α subunit
    • Tao, K., C. Zou, N. Fujita, and A. Ishihama. 1995. Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase α subunit. J. Bacteriol. 177:6740-6744.
    • (1995) J. Bacteriol. , vol.177 , pp. 6740-6744
    • Tao, K.1    Zou, C.2    Fujita, N.3    Ishihama, A.4
  • 29
    • 0028287637 scopus 로고
    • Protective effect of epicatechin, epicatechin gallate, and quercetin on lipid peroxidation in phospholipid bilayers
    • Terao, J., M. Piskula, and Q. Yao. 1994. Protective effect of epicatechin, epicatechin gallate, and quercetin on lipid peroxidation in phospholipid bilayers. Arch. Biochem. Biophys. 308:278-284.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 278-284
    • Terao, J.1    Piskula, M.2    Yao, Q.3
  • 30
    • 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., I. Kullik, F. Trinh, P. T. Baird, T. D. Schneider, and G. Storz. 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
  • 32
    • 0033018333 scopus 로고    scopus 로고
    • Effects of green tea catechins on membrane fluidity
    • Tsuchiya, H. 1999. Effects of green tea catechins on membrane fluidity. Pharmacology 59:34-44.
    • (1999) Pharmacology , vol.59 , pp. 34-44
    • Tsuchiya, H.1
  • 33
    • 0012578288 scopus 로고
    • Synthesis of condensed tannins. Part 7. Angular [4,6:4,8]-prorobinetinidin triflavonoids from black wattle ("Mimosa") bark extract
    • Viviers, P. M., J. J. Botha, D. Ferreira, and D. G. Roux. 1983. Synthesis of condensed tannins. Part 7. Angular [4,6:4,8]-prorobinetinidin triflavonoids from black wattle ("Mimosa") bark extract. J. Chem. Soc. Perkin Trans. 1:17-22.
    • (1983) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 17-22
    • Viviers, P.M.1    Botha, J.J.2    Ferreira, D.3    Roux, D.G.4
  • 34
    • 0030833642 scopus 로고    scopus 로고
    • Microbiological activity of whole and fractionated crude extracts of tea (Camellia sinensis), and of tea components
    • Yam, T. S., S. Shah, and J. M. Hamilton-Miller. 1997. Microbiological activity of whole and fractionated crude extracts of tea (Camellia sinensis), and of tea components. FEMS Microbiol. Lett. 152:169-174.
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 169-174
    • Yam, T.S.1    Shah, S.2    Hamilton-Miller, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.