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Volumn 155, Issue 6, 2009, Pages 1840-1846

Tellurite-mediated disabling of [4Fe-4S] clusters of Escherichia coli dehydratases

Author keywords

[No Author keywords available]

Indexed keywords

2,2' BIPYRIDINE; ACONITATE HYDRATASE; FERROUS ION; FUMARATE HYDRATASE; IRON SULFUR PROTEIN; OXYGEN; REACTIVE OXYGEN METABOLITE; TELLURIUM; FUMARASE C; HYDROLYASE; ISOMERASE; OXALOACETATE TAUTOMERASE; SUPEROXIDE; TELLUROUS ACID;

EID: 67650711065     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.026260-0     Document Type: Article
Times cited : (54)

References (37)
  • 1
    • 0034669393 scopus 로고    scopus 로고
    • On the mechanism of resistance to channel-forming colicins (PacB) and tellurite, encoded by plasmid Mip233 (IncHI3)
    • Alonso, G., Gomes, C., González, C. & Rodríguez-Lemoine, V. (2000). On the mechanism of resistance to channel-forming colicins (PacB) and tellurite, encoded by plasmid Mip233 (IncHI3). FEMS Microbiol Lett 192, 257-261.
    • (2000) FEMS Microbiol Lett , vol.192 , pp. 257-261
    • Alonso, G.1    Gomes, C.2    González, C.3    Rodríguez-Lemoine, V.4
  • 2
    • 24144435333 scopus 로고    scopus 로고
    • Tellurite effects on Rhodobacter capsulatus cell viability and superoxide dismutase activity under oxidative stress conditions
    • Borsetti, F., Tremaroli, V., Michelacci, F., Borghese, R., Winterstein, C., Daldal, F. & Zannoni, D. (2005). Tellurite effects on Rhodobacter capsulatus cell viability and superoxide dismutase activity under oxidative stress conditions. Res Microbiol 156, 807-813.
    • (2005) Res Microbiol , vol.156 , pp. 807-813
    • Borsetti, F.1    Tremaroli, V.2    Michelacci, F.3    Borghese, R.4    Winterstein, C.5    Daldal, F.6    Zannoni, D.7
  • 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
    • 0036510621 scopus 로고    scopus 로고
    • Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling
    • Brown, N. M., Kennedy, M. C., Antholine, W. E., Eisenstein, R. S. & Walden, W. E. (2002). Detection of a [3Fe-4S] cluster intermediate of cytosolic aconitase in yeast expressing iron regulatory protein 1. Insights into the mechanism of Fe-S cluster cycling. J Biol Chem 277, 7246-7254.
    • (2002) J Biol Chem , vol.277 , pp. 7246-7254
    • Brown, N.M.1    Kennedy, M.C.2    Antholine, W.E.3    Eisenstein, R.S.4    Walden, W.E.5
  • 6
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman, O., Outten, W. & Imlay, J. A. (2004). Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem 279, 44590-44599.
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, W.2    Imlay, J.A.3
  • 7
    • 0027375778 scopus 로고
    • The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated
    • Flint, D. H., Smyk-Randall, E., Tuminello, J. F., Draczynska-Lusiak, B. & Brown, O. R. (1993a). The inactivation of dihydroxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated. J Biol Chem 268, 25547-25552.
    • (1993) J Biol Chem , vol.268 , pp. 25547-25552
    • Flint, D.H.1    Smyk-Randall, E.2    Tuminello, J.F.3    Draczynska-Lusiak, B.4    Brown, O.R.5
  • 8
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D. H., Tuminello, J. F. & Emptage, M. (1993b). The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 268, 22369-22376.
    • (1993) J Biol Chem , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.3
  • 9
    • 0027959635 scopus 로고
    • nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters
    • Fu, W., Jack, R., Morgan, T., Dean, D. & Johnson, M. (1994). nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 33, 13455-13463.
    • (1994) Biochemistry , vol.33 , pp. 13455-13463
    • Fu, W.1    Jack, R.2    Morgan, T.3    Dean, D.4    Johnson, M.5
  • 10
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. & Fridovich, I. (1991). Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266, 19328-19333.
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 11
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. (2003). Pathways of oxidative damage. Annu Rev Microbiol 57, 395-418.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 12
    • 0023178381 scopus 로고
    • α,β-Dihydroxyisovalerate dehydratase. A superoxide-sensitive enzyme
    • Kuo, C. F., Mashino, T. & Fridovich, I. (1987). α,β-Dihydroxyisovalerate dehydratase. A superoxide-sensitive enzyme. J Biol Chem 262, 4724-4727.
    • (1987) J Biol Chem , vol.262 , pp. 4724-4727
    • Kuo, C.F.1    Mashino, T.2    Fridovich, I.3
  • 13
    • 0027258954 scopus 로고
    • Modulation of the fumarases of Escherichia coli in response to oxidative stress
    • Liochev, S. I. & Fridovich, I. (1993). Modulation of the fumarases of Escherichia coli in response to oxidative stress. Arch Biochem Biophys 301, 379-384.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 379-384
    • Liochev, S.I.1    Fridovich, I.2
  • 15
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M. & Barras, F. (2003). Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278, 38352-38359.
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-de-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 16
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994). Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 269, 22459-22462.
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 17
    • 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. & Imlay, J. A. (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
  • 18
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • Messner, K. R. & Imlay, J. A. (2002). Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J Biol Chem 277, 42563-42571.
    • (2002) J Biol Chem , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 19
    • 0030732680 scopus 로고    scopus 로고
    • Identification and molecular genetic analysis of multiple loci contributing to high-level tellurite resistance in Rhodobacter sphaeroides 2.4.1
    • O'Gara, J. P., Gomelsky, M. & Kaplan, S. (1997). Identification and molecular genetic analysis of multiple loci contributing to high-level tellurite resistance in Rhodobacter sphaeroides 2.4.1. Appl Environ Microbiol 63, 4713-4720.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 4713-4720
    • O'Gara, J.P.1    Gomelsky, M.2    Kaplan, S.3
  • 20
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten, F. W., Wood, M. J., Muñoz, F. M. & Storz, G. (2003). The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278, 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Muñoz, F.M.3    Storz, G.4
  • 22
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
    • Pérez, J. M., Arenas, F. A., Pradenas, G. A., Sandoval, J. M. & Vásquez, C. C. (2008). Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes. J Biol Chem 283, 7346-7353.
    • (2008) J Biol Chem , vol.283 , pp. 7346-7353
    • Pérez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vásquez, C.C.5
  • 23
    • 33746572731 scopus 로고    scopus 로고
    • Identification, cloning and characterization of cysK, the gene encoding O-acetylserine (thiol)-lyase from Azospirillum brasilense, which is involved in tellurite resistance
    • Ramírez, A., Castañeda, M., Xiqui, M. L., Sosa, A. & Baca, B. E. (2006). Identification, cloning and characterization of cysK, the gene encoding O-acetylserine (thiol)-lyase from Azospirillum brasilense, which is involved in tellurite resistance. FEMS Microbiol Lett 261, 272-279.
    • (2006) FEMS Microbiol Lett , vol.261 , pp. 272-279
    • Ramírez, A.1    Castañeda, M.2    Xiqui, M.L.3    Sosa, A.4    Baca, B.E.5
  • 24
    • 0034681114 scopus 로고    scopus 로고
    • Modifications of proteins by polyunsaturated fatty acid peroxidation products
    • Refsgaard, H. H., Tsai, L. & Stadtman, E. R. (2000). Modifications of proteins by polyunsaturated fatty acid peroxidation products. Proc Natl Acad Sci U S A 97, 611-616.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 611-616
    • Refsgaard, H.H.1    Tsai, L.2    Stadtman, E.R.3
  • 25
    • 18144383858 scopus 로고    scopus 로고
    • Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurases
    • Rojas, D. M. & Vásquez, C. C. (2005). Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurases. Res Microbiol 156, 465-471.
    • (2005) Res Microbiol , vol.156 , pp. 465-471
    • Rojas, D.M.1    Vásquez, C.C.2
  • 28
    • 0141794348 scopus 로고    scopus 로고
    • The Geobacillus stearothermophilus V iscS gene, encoding cysteine desulfurase, confers resistance to potassium tellurite in Escherichia coli K-12
    • Tantaleán, J. C., Araya, M. A., Pichuantes, S. E., Saavedra, C. P., Fuentes, D. E., Pérez, J. M., Calderón, I. L. & Vásquez, C. C. (2003). The Geobacillus stearothermophilus V iscS gene, encoding cysteine desulfurase, confers resistance to potassium tellurite in Escherichia coli K-12. J Bacteriol 185, 5831-5837.
    • (2003) J Bacteriol , vol.185 , pp. 5831-5837
    • Tantaleán, J.C.1    Araya, M.A.2    Pichuantes, S.E.3    Saavedra, C.P.4    Fuentes, D.E.5    Pérez, J.M.6    Calderón, I.L.7    Vásquez, C.C.8
  • 29
    • 0033105190 scopus 로고    scopus 로고
    • Bacterial tellurite resistance
    • Taylor, D. E. (1999). Bacterial tellurite resistance. Trends Microbiol 7, 111-115.
    • (1999) Trends Microbiol , vol.7 , pp. 111-115
    • Taylor, D.E.1
  • 30
    • 33846698565 scopus 로고    scopus 로고
    • Evidence for a tellurite-dependent generation of reactive oxygen species and absence of a tellurite-mediated adaptive response to oxidative stress in cells of Pseudomonas pseudoalcaligenes KF707
    • Tremaroli, V., Fedi, F. & Zannoni, D. (2006). Evidence for a tellurite-dependent generation of reactive oxygen species and absence of a tellurite-mediated adaptive response to oxidative stress in cells of Pseudomonas pseudoalcaligenes KF707. Arch Microbiol 187, 127-135.
    • (2006) Arch Microbiol , vol.187 , pp. 127-135
    • Tremaroli, V.1    Fedi, F.2    Zannoni, D.3
  • 31
    • 0032846820 scopus 로고    scopus 로고
    • Tellurite-mediated thiol oxidation in Escherichia coli
    • Turner, R. J., Weiner, J. & Taylor, D. E. (1999). Tellurite-mediated thiol oxidation in Escherichia coli. Microbiology 145, 2549-2557.
    • (1999) Microbiology , vol.145 , pp. 2549-2557
    • Turner, R.J.1    Weiner, J.2    Taylor, D.E.3
  • 32
    • 0035134056 scopus 로고    scopus 로고
    • Glutathione is a target in tellurite toxicity and is protected by tellurite resistance determinants in Escherichia coli
    • Turner, R. J., Aharonowitz, Y., Weiner, J. & Taylor, D. E. (2001). Glutathione is a target in tellurite toxicity and is protected by tellurite resistance determinants in Escherichia coli. Can J Microbiol 47, 33-40.
    • (2001) Can J Microbiol , vol.47 , pp. 33-40
    • Turner, R.J.1    Aharonowitz, Y.2    Weiner, J.3    Taylor, D.E.4
  • 33
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Várghese, S., Tang, Y. & Imlay, J. A. (2003). Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J Bacteriol 185, 221-230.
    • (2003) J Bacteriol , vol.185 , pp. 221-230
    • Várghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 34
    • 0035197190 scopus 로고    scopus 로고
    • The product of the cysK gene of Bacillus stearothermophilus V mediates potassium tellurite resistance in Escherichia coli
    • Vásquez, C. C., Saavedra, C. P., Loyola, C. A., Araya, M. A. & Pichuantes, S. E. (2001). The product of the cysK gene of Bacillus stearothermophilus V mediates potassium tellurite resistance in Escherichia coli. Curr Microbiol 43, 418-423.
    • (2001) Curr Microbiol , vol.43 , pp. 418-423
    • Vásquez, C.C.1    Saavedra, C.P.2    Loyola, C.A.3    Araya, M.A.4    Pichuantes, S.E.5
  • 35
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis
    • Zheng, L., White, R., Cash, V., Jack, R. & Dean, D. (1993). Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis. Proc Natl Acad Sci U S A 90, 2754-2758.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.2    Cash, V.3    Jack, R.4    Dean, D.5
  • 36
    • 0028265941 scopus 로고
    • Mechanism for the sulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng, L., White, R., Cash, V. & Dean, D. (1994). Mechanism for the sulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry 33, 4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.2    Cash, V.3    Dean, D.4
  • 37
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L., Smulski, D., LaRossa, R. & Storz, G. (2001). DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183, 4562-4570.
    • (2001) J Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.3    Smulski, D.4    LaRossa, R.5    Storz, G.6


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