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Volumn 87, Issue 3, 2013, Pages 447-454

A fresh view of the cell biology of copper in enterobacteria

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM DERIVATIVE; CALCIUM; COBALT; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; COPPER ION; IRON; MAGNESIUM; MANGANESE; MOLYBDENUM; NICKEL; ZINC;

EID: 84873055243     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12123     Document Type: Note
Times cited : (43)

References (87)
  • 1
    • 84859899394 scopus 로고    scopus 로고
    • Redox-changes associated with the glutathione-dependent ability of the Cu(II)-GSSG complex to generate superoxide
    • Aliaga, M.E., Lopez-Alarcon, C., Garcia-Rio, L., Martin-Pastor, M., and Speisky, H. (2012) Redox-changes associated with the glutathione-dependent ability of the Cu(II)-GSSG complex to generate superoxide. Bioorg Med Chem 20: 2869-2876.
    • (2012) Bioorg Med Chem , vol.20 , pp. 2869-2876
    • Aliaga, M.E.1    Lopez-Alarcon, C.2    Garcia-Rio, L.3    Martin-Pastor, M.4    Speisky, H.5
  • 2
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P-1B-ATPases
    • Argüello, J.M., Eren, E., and Gonzalez-Guerrero, M. (2007) The structure and function of heavy metal transport P-1B-ATPases. Biometals 20: 233-248.
    • (2007) Biometals , vol.20 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    Gonzalez-Guerrero, M.3
  • 3
    • 55249109759 scopus 로고    scopus 로고
    • Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone
    • Bagai, I., Rensing, C., Blackburn, N.J., and McEvoy, M.M. (2008) Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry 47: 11408-11414.
    • (2008) Biochemistry , vol.47 , pp. 11408-11414
    • Bagai, I.1    Rensing, C.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 4
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • Benov, L.T., and Fridovich, I. (1994) Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem 269: 25310-25314.
    • (1994) J Biol Chem , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 5
    • 0001548495 scopus 로고
    • The stability constants of metal complexes of amino acids with polar side chains
    • Berton, G. (1995) The stability constants of metal complexes of amino acids with polar side chains. Pure Appl Chem 67: 1117-1240.
    • (1995) Pure Appl Chem , vol.67 , pp. 1117-1240
    • Berton, G.1
  • 6
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun, V., and Braun, M. (2002) Active transport of iron and siderophore antibiotics. Curr Opin Microbiol 5: 194-201.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 194-201
    • Braun, V.1    Braun, M.2
  • 9
    • 77952056332 scopus 로고    scopus 로고
    • Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis
    • Chillappagari, S., Seubert, A., Trip, H., Kuipers, O.P., Marahiel, M.A., and Miethke, M. (2010) Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis. J Bacteriol 192: 2512-2524.
    • (2010) J Bacteriol , vol.192 , pp. 2512-2524
    • Chillappagari, S.1    Seubert, A.2    Trip, H.3    Kuipers, O.P.4    Marahiel, M.A.5    Miethke, M.6
  • 10
    • 0023094254 scopus 로고
    • Characterization of a copper resistance plasmid conserved in copper-resistant strains of Pseudomonas syringae pv tomato
    • Cooksey, D.A. (1987) Characterization of a copper resistance plasmid conserved in copper-resistant strains of Pseudomonas syringae pv tomato. Appl Environ Microbiol 53: 454-456.
    • (1987) Appl Environ Microbiol , vol.53 , pp. 454-456
    • Cooksey, D.A.1
  • 11
    • 0026482980 scopus 로고
    • Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the Gram-negative bacterium Escherichia coli K-12
    • Cooper, R.A., Knowles, P.F., Brown, D.E., McGuirl, M.A., and Dooley, D.M. (1992) Evidence for copper and 3, 4, 6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the Gram-negative bacterium Escherichia coli K-12. Biochem J 288: 337-340.
    • (1992) Biochem J , vol.288 , pp. 337-340
    • Cooper, R.A.1    Knowles, P.F.2    Brown, D.E.3    McGuirl, M.A.4    Dooley, D.M.5
  • 12
    • 0025944026 scopus 로고
    • Determinants encoding multiple metal resistance in newly isolated copper-resistant bacteria
    • Dressler, C., Kües, U., Nies, D.H., and Friedrich, B. (1991) Determinants encoding multiple metal resistance in newly isolated copper-resistant bacteria. Appl Environ Microbiol 57: 3079-3085.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 3079-3085
    • Dressler, C.1    Kües, U.2    Nies, D.H.3    Friedrich, B.4
  • 13
    • 15344343162 scopus 로고    scopus 로고
    • Role of ECF sigma factor RpoE in heavy metal resistance of Escherichia coli
    • Egler, M., Große, C., Grass, G., and Nies, D.H. (2005) Role of ECF sigma factor RpoE in heavy metal resistance of Escherichia coli. J Bacteriol 187: 2297-2307.
    • (2005) J Bacteriol , vol.187 , pp. 2297-2307
    • Egler, M.1    Große, C.2    Grass, G.3    Nies, D.H.4
  • 15
    • 0035047623 scopus 로고    scopus 로고
    • The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions
    • Franke, S., Grass, G., and Nies, D.H. (2001) The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions. Microbiology 147: 965-972.
    • (2001) Microbiology , vol.147 , pp. 965-972
    • Franke, S.1    Grass, G.2    Nies, D.H.3
  • 16
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting CusCFBA efflux system from Escherichia coli
    • Franke, S., Grass, G., Rensing, C., and Nies, D.H. (2003) Molecular analysis of the copper-transporting CusCFBA efflux system from Escherichia coli. J Bacteriol 185: 3804-3812.
    • (2003) J Bacteriol , vol.185 , pp. 3804-3812
    • Franke, S.1    Grass, G.2    Rensing, C.3    Nies, D.H.4
  • 17
    • 0024554012 scopus 로고
    • The role of glutathione in copper metabolism and toxicity
    • Freedman, J.H., Ciriolo, M.R., and Peisach, J. (1989) The role of glutathione in copper metabolism and toxicity. J Biol Chem 264: 5598-5605.
    • (1989) J Biol Chem , vol.264 , pp. 5598-5605
    • Freedman, J.H.1    Ciriolo, M.R.2    Peisach, J.3
  • 18
    • 78649536013 scopus 로고    scopus 로고
    • Distinct functional roles of homologous Cu plus efflux ATPases in Pseudomonas aeruginosa
    • Gonzalez-Guerrero, M., Raimunda, D., Cheng, X., and Argüello, J.M. (2010) Distinct functional roles of homologous Cu plus efflux ATPases in Pseudomonas aeruginosa. Mol Microbiol 78: 1246-1258.
    • (2010) Mol Microbiol , vol.78 , pp. 1246-1258
    • Gonzalez-Guerrero, M.1    Raimunda, D.2    Cheng, X.3    Argüello, J.M.4
  • 19
    • 0034817086 scopus 로고    scopus 로고
    • CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
    • Grass, G., and Rensing, C. (2001a) CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem Biophys Res Commun 286: 902-908.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 902-908
    • Grass, G.1    Rensing, C.2
  • 20
    • 0035101356 scopus 로고    scopus 로고
    • Genes involved in copper homeostasis in Escherichia coli
    • Grass, G., and Rensing, C. (2001b) Genes involved in copper homeostasis in Escherichia coli. J Bacteriol 183: 2145-2147.
    • (2001) J Bacteriol , vol.183 , pp. 2145-2147
    • Grass, G.1    Rensing, C.2
  • 21
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • Grass, G., Franke, S., Taudte, N., Nies, D.H., Kucharski, L.M., Maguire, M.E., and Rensing, C. (2005) The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J Bacteriol 187: 1604-1611.
    • (2005) J Bacteriol , vol.187 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6    Rensing, C.7
  • 22
    • 84859425452 scopus 로고    scopus 로고
    • Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor kinase CusS
    • Gudipaty, S.A., Larsen, A.S., Rensing, C., and McEvoy, M.M. (2012) Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor kinase CusS. FEMS Microbiol Lett 330: 30-37.
    • (2012) FEMS Microbiol Lett , vol.330 , pp. 30-37
    • Gudipaty, S.A.1    Larsen, A.S.2    Rensing, C.3    McEvoy, M.M.4
  • 23
    • 34250942854 scopus 로고
    • Über die Katalyse des Hydroperoxydes
    • Haber, F., and Weiss, J. (1932) Über die Katalyse des Hydroperoxydes. Naturwissenschaften 20: 948-950.
    • (1932) Naturwissenschaften , vol.20 , pp. 948-950
    • Haber, F.1    Weiss, J.2
  • 24
    • 84867150749 scopus 로고    scopus 로고
    • Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgin network
    • Hasan, N.M., Gupta, A., Polishchuk, E., Yu, C.H., Polishchuk, R., Dmitriev, O.Y., and Lutsenko, S. (2012) Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgin network. J Biol Chem 287: 36041-36050.
    • (2012) J Biol Chem , vol.287 , pp. 36041-36050
    • Hasan, N.M.1    Gupta, A.2    Polishchuk, E.3    Yu, C.H.4    Polishchuk, R.5    Dmitriev, O.Y.6    Lutsenko, S.7
  • 25
    • 48149108241 scopus 로고    scopus 로고
    • Glutathione and transition metal homeostasis in Escherichia coli
    • Helbig, K., Bleuel, C., Krauss, G.J., and Nies, D.H. (2008) Glutathione and transition metal homeostasis in Escherichia coli. J Bacteriol 190: 5431-5438.
    • (2008) J Bacteriol , vol.190 , pp. 5431-5438
    • Helbig, K.1    Bleuel, C.2    Krauss, G.J.3    Nies, D.H.4
  • 26
    • 0037031263 scopus 로고    scopus 로고
    • Spectroscopy of Cu(II)-PcoC and the multicopper oxidase function of PcoA, two essential components of Escherichia coli pco copper resistance operon
    • Huffman, D.L., Huyett, J., Outten, F.W., Doan, P.E., Finney, L.A., Hoffman, B.M., and O'Halloran, T.V. (2002) Spectroscopy of Cu(II)-PcoC and the multicopper oxidase function of PcoA, two essential components of Escherichia coli pco copper resistance operon. Biochemistry 41: 10046-10055.
    • (2002) Biochemistry , vol.41 , pp. 10046-10055
    • Huffman, D.L.1    Huyett, J.2    Outten, F.W.3    Doan, P.E.4    Finney, L.A.5    Hoffman, B.M.6    O'Halloran, T.V.7
  • 27
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: a case study using the Phyre server
    • Kelley, L.A., and Sternberg, M.J.E. (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat Protoc 4: 363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 28
    • 0030928221 scopus 로고    scopus 로고
    • Intracellular generation of superoxide by copper sulphate in Escherichia coli
    • Kimura, T., and Nishioka, H. (1997) Intracellular generation of superoxide by copper sulphate in Escherichia coli. Mutat Res 389: 237-242.
    • (1997) Mutat Res , vol.389 , pp. 237-242
    • Kimura, T.1    Nishioka, H.2
  • 29
    • 80052541464 scopus 로고    scopus 로고
    • Contributions of five secondary metal uptake systems to metal homeostasis of Cupriavidus metallidurans CH34
    • Kirsten, A., Herzberg, M., Voigt, A., Seravalli, J., Grass, G., Scherer, J., and Nies, D.H. (2011) Contributions of five secondary metal uptake systems to metal homeostasis of Cupriavidus metallidurans CH34. J Bacteriol 193: 4652-4663.
    • (2011) J Bacteriol , vol.193 , pp. 4652-4663
    • Kirsten, A.1    Herzberg, M.2    Voigt, A.3    Seravalli, J.4    Grass, G.5    Scherer, J.6    Nies, D.H.7
  • 30
    • 4043114792 scopus 로고    scopus 로고
    • Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism
    • Kuper, J., Llamas, A., Hecht, H.J., Mendel, R.R., and Schwarz, G. (2004) Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism. Nature 430: 803-806.
    • (2004) Nature , vol.430 , pp. 803-806
    • Kuper, J.1    Llamas, A.2    Hecht, H.J.3    Mendel, R.R.4    Schwarz, G.5
  • 31
    • 77956179036 scopus 로고    scopus 로고
    • Mechanisms underlying iron and copper ions toxicity in biological systems: pro-oxidant activity and protein-binding effects
    • Letelier, M.E., Sanchez-Jofre, S., Peredo-Silva, L., Cortes-Troncoso, J., and Aracena-Parks, P. (2010) Mechanisms underlying iron and copper ions toxicity in biological systems: pro-oxidant activity and protein-binding effects. Chem Biol Interact 188: 220-227.
    • (2010) Chem Biol Interact , vol.188 , pp. 220-227
    • Letelier, M.E.1    Sanchez-Jofre, S.2    Peredo-Silva, L.3    Cortes-Troncoso, J.4    Aracena-Parks, P.5
  • 32
    • 0037206561 scopus 로고    scopus 로고
    • cuiD is a crucial gene for survival at high copper environment in Salmonella enterica serovar typhimurium
    • Lim, S.Y., Joe, M.H., Song, S.S., Lee, M.H., Foster, J.W., Park, Y.K., etal. (2002) cuiD is a crucial gene for survival at high copper environment in Salmonella enterica serovar typhimurium. Mol Cells 14: 177-184.
    • (2002) Mol Cells , vol.14 , pp. 177-184
    • Lim, S.Y.1    Joe, M.H.2    Song, S.S.3    Lee, M.H.4    Foster, J.W.5    Park, Y.K.6
  • 33
    • 0036211994 scopus 로고    scopus 로고
    • The Haber-Weiss cycle - 70 years later: an alternative view
    • Liochev, S.I., and Fridovich, I. (2002) The Haber-Weiss cycle - 70 years later: an alternative view. Redox Rep 7: 55-57.
    • (2002) Redox Rep , vol.7 , pp. 55-57
    • Liochev, S.I.1    Fridovich, I.2
  • 34
    • 23244451021 scopus 로고    scopus 로고
    • A novel copper-binding fold for the periplasmic copper resistance protein CusF
    • Loftin, I.R., Franke, S., Roberts, S.A., Weichsel, A., Heroux, A., Montfort, W.R., etal. (2005) A novel copper-binding fold for the periplasmic copper resistance protein CusF. Biochemistry 44: 10533-10540.
    • (2005) Biochemistry , vol.44 , pp. 10533-10540
    • Loftin, I.R.1    Franke, S.2    Roberts, S.A.3    Weichsel, A.4    Heroux, A.5    Montfort, W.R.6
  • 35
  • 36
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L., and Imlay, J.A. (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc Natl Acad Sci USA 106: 8344-8349.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 37
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L., Rensing, C., and Imlay, J.A. (2007) Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J Bacteriol 189: 1616-1626.
    • (2007) J Bacteriol , vol.189 , pp. 1616-1626
    • Macomber, L.1    Rensing, C.2    Imlay, J.A.3
  • 38
    • 0024022864 scopus 로고
    • Nucleotide sequence and organization of copper resistance genes from Pseudomonas syringae pv. tomato
    • Mellano, M.A., and Cooksey, D.A. (1988) Nucleotide sequence and organization of copper resistance genes from Pseudomonas syringae pv. tomato. J Bacteriol 170: 2879-2883.
    • (1988) J Bacteriol , vol.170 , pp. 2879-2883
    • Mellano, M.A.1    Cooksey, D.A.2
  • 39
    • 0021925630 scopus 로고
    • Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals
    • Mergeay, M., Nies, D., Schlegel, H.G., Gerits, J., Charles, P., and van Gijsegem, F. (1985) Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals. J Bacteriol 162: 328-334.
    • (1985) J Bacteriol , vol.162 , pp. 328-334
    • Mergeay, M.1    Nies, D.2    Schlegel, H.G.3    Gerits, J.4    van Charles, P.5    Gijsegem, F.6
  • 40
    • 84861216569 scopus 로고    scopus 로고
    • The copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli
    • Mermod, M., Magnani, D., Solioz, M., and Stoyanov, J.V. (2012) The copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli. Biometals 25: 33-43.
    • (2012) Biometals , vol.25 , pp. 33-43
    • Mermod, M.1    Magnani, D.2    Solioz, M.3    Stoyanov, J.V.4
  • 42
    • 33646348921 scopus 로고    scopus 로고
    • Transcriptomics and proteomic analysis of the pMOL30-encoded copper resistance in Cupriavidus metallidurans strain CH34
    • Monchy, S., Benotmane, M.A., Wattiez, R., van Aelst, S., Auquier, V., Borremans, B., etal. (2006) Transcriptomics and proteomic analysis of the pMOL30-encoded copper resistance in Cupriavidus metallidurans strain CH34. Microbiology 152: 1765-1776.
    • (2006) Microbiology , vol.152 , pp. 1765-1776
    • Monchy, S.1    Benotmane, M.A.2    van Wattiez, R.3    Aelst, S.4    Auquier, V.5    Borremans, B.6
  • 43
    • 0033813832 scopus 로고    scopus 로고
    • Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12
    • Munson, G.P., Lam, D.L., Outten, F.W., and O'Halloran, T.V. (2000) Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. J Bacteriol 182: 5864-5871.
    • (2000) J Bacteriol , vol.182 , pp. 5864-5871
    • Munson, G.P.1    Lam, D.L.2    Outten, F.W.3    O'Halloran, T.V.4
  • 44
    • 84861361870 scopus 로고    scopus 로고
    • Characterization of the response to zinc-deficiency in the cyanobacterium Anabaena sp. PCC 7120
    • Napolitano, M., Rubio, M.A., Santamaria-Gomez, J., Olmedo-Verd, E., Robinson, N.J., and Luque, I. (2012) Characterization of the response to zinc-deficiency in the cyanobacterium Anabaena sp. PCC 7120. J Bacteriol 194: 2426-2436.
    • (2012) J Bacteriol , vol.194 , pp. 2426-2436
    • Napolitano, M.1    Rubio, M.A.2    Santamaria-Gomez, J.3    Olmedo-Verd, E.4    Robinson, N.J.5    Luque, I.6
  • 45
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies, D.H. (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol Rev 27: 313-339.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 46
    • 35448993202 scopus 로고    scopus 로고
    • Bacterial transition metal homeostasis
    • Nies, D.H., and Silver, S. (eds). Berlin: Springer-Verlag
    • Nies, D.H. (2007) Bacterial transition metal homeostasis. In Molecular Microbiology of Heavy Metals. Nies, D.H., and Silver, S. (eds). Berlin: Springer-Verlag, pp. 118-142.
    • (2007) Molecular Microbiology of Heavy Metals , pp. 118-142
    • Nies, D.H.1
  • 47
    • 84861393835 scopus 로고    scopus 로고
    • Zinc starvation response in a cyanobacterium revealed
    • Nies, D.H. (2012) Zinc starvation response in a cyanobacterium revealed. J Bacteriol 194: 2407-2412.
    • (2012) J Bacteriol , vol.194 , pp. 2407-2412
    • Nies, D.H.1
  • 48
    • 84873058607 scopus 로고    scopus 로고
    • RND-efflux pumps for metal cations
    • Yu, E.W. (ed.). Norwich: Horizon Scientific Press Ltd (in press).
    • Nies, D.H. (2013) RND-efflux pumps for metal cations. In Microbial Efflux Pumps: Current Research. Yu, E.W. (ed.). Norwich: Horizon Scientific Press Ltd (in press).
    • (2013) Microbial Efflux Pumps: Current Research
    • Nies, D.H.1
  • 49
    • 84873059719 scopus 로고    scopus 로고
    • The limitations of LB medium. [WWW document].
    • Nikaido, H. (2009) The limitations of LB medium. [WWW document]. URL http://schaechter.asmblog.org/schaechter/2009/11/the-limitations-of-lb-medium.html
    • (2009)
    • Nikaido, H.1
  • 50
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran, T.V., and Culotta, V.C. (2000) Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275: 25057-25060.
    • (2000) J Biol Chem , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 51
    • 0027058149 scopus 로고
    • An ATPase operon involved in copper resistance by Enterococcus hirae
    • Odermatt, A., Suter, H., Krapf, R., and Solioz, M. (1992) An ATPase operon involved in copper resistance by Enterococcus hirae. Ann N Y Acad Sci 671: 484-486.
    • (1992) Ann N Y Acad Sci , vol.671 , pp. 484-486
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 52
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt, A., Suter, H., Krapf, R., and Solioz, M. (1993) Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J Biol Chem 268: 12775-12779.
    • (1993) J Biol Chem , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 53
    • 77955499578 scopus 로고    scopus 로고
    • Copper homeostasis in Salmonella is atypical and copper-CueP is a major periplasmic metal complex
    • Osman, D., Waldron, K.J., Denton, H., Taylor, C.M., Grant, A.J., Mastroeni, P., etal. (2010) Copper homeostasis in Salmonella is atypical and copper-CueP is a major periplasmic metal complex. J Biol Chem 285: 25259-25268.
    • (2010) J Biol Chem , vol.285 , pp. 25259-25268
    • Osman, D.1    Waldron, K.J.2    Denton, H.3    Taylor, C.M.4    Grant, A.J.5    Mastroeni, P.6
  • 55
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C.E., and O'Halloran, T.V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292: 2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 56
    • 0034613337 scopus 로고    scopus 로고
    • Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, CueR
    • Outten, F.W., Outten, C.E., Hale, J., and O'Halloran, T.V. (2000) Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, CueR. J Biol Chem 275: 31024-31029.
    • (2000) J Biol Chem , vol.275 , pp. 31024-31029
    • Outten, F.W.1    Outten, C.E.2    Hale, J.3    O'Halloran, T.V.4
  • 57
    • 0035903128 scopus 로고    scopus 로고
    • The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
    • Outten, F.W., Huffman, D.L., Hale, J.A., and O'Halloran, T.V. (2001) The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem 276: 30670-30677.
    • (2001) J Biol Chem , vol.276 , pp. 30670-30677
    • Outten, F.W.1    Huffman, D.L.2    Hale, J.A.3    O'Halloran, T.V.4
  • 58
    • 67650436140 scopus 로고    scopus 로고
    • Alternative periplasmic copper-resistance mechanisms in Gram negative bacteria
    • Pontel, L.B., and Soncini, F.C. (2009) Alternative periplasmic copper-resistance mechanisms in Gram negative bacteria. Mol Microbiol 73: 212-225.
    • (2009) Mol Microbiol , vol.73 , pp. 212-225
    • Pontel, L.B.1    Soncini, F.C.2
  • 59
    • 35448961704 scopus 로고    scopus 로고
    • GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon
    • Pontel, L.B., Audero, M.E., Espariz, M., Checa, S.K., and Soncini, F.C. (2007) GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon. Mol Microbiol 66: 814-825.
    • (2007) Mol Microbiol , vol.66 , pp. 814-825
    • Pontel, L.B.1    Audero, M.E.2    Espariz, M.3    Checa, S.K.4    Soncini, F.C.5
  • 60
    • 0036718981 scopus 로고    scopus 로고
    • Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2
    • Rapisarda, V.A., Chehín, R.N., De Las Rivas, J., Rodríguez-Montelongo, L., Farías, R.N., and Massa, E.M. (2002) Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2. Arch Biochem Biophys 405: 87-94.
    • (2002) Arch Biochem Biophys , vol.405 , pp. 87-94
    • Rapisarda, V.A.1    Chehín, R.N.2    De Las Rivas, J.3    Rodríguez-Montelongo, L.4    Farías, R.N.5    Massa, E.M.6
  • 61
    • 33745974536 scopus 로고    scopus 로고
    • Biomineralization of gold: biofilms on bacterioform gold
    • Reith, F., Rogers, S.L., McPhail, D.C., and Webb, D. (2006) Biomineralization of gold: biofilms on bacterioform gold. Science 313: 233-236.
    • (2006) Science , vol.313 , pp. 233-236
    • Reith, F.1    Rogers, S.L.2    McPhail, D.C.3    Webb, D.4
  • 63
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing, C., and Grass, G. (2003) Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol Rev 27: 197-213.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 66
    • 33745198005 scopus 로고    scopus 로고
    • The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide
    • Rodriguez-Montelongo, L., Volentini, S.I., Farias, R.N., Massa, E.M., and Rapisarda, V.A. (2006) The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide. Arch Biochem Biophys 451: 1-7.
    • (2006) Arch Biochem Biophys , vol.451 , pp. 1-7
    • Rodriguez-Montelongo, L.1    Volentini, S.I.2    Farias, R.N.3    Massa, E.M.4    Rapisarda, V.A.5
  • 67
    • 39649093183 scopus 로고    scopus 로고
    • Contribution of copper ion resistance to survival of Escherichia coli on metallic copper surfaces
    • Santo, C.E., Taudte, N., Nies, D.H., and Grass, G. (2008) Contribution of copper ion resistance to survival of Escherichia coli on metallic copper surfaces. Appl Environ Microbiol 74: 977-986.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 977-986
    • Santo, C.E.1    Taudte, N.2    Nies, D.H.3    Grass, G.4
  • 68
    • 33846627273 scopus 로고    scopus 로고
    • Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery
    • Schauer, K., Gouget, B., Carriere, M., Labigne, A., and de Reuse, H. (2007) Novel nickel transport mechanism across the bacterial outer membrane energized by the TonB/ExbB/ExbD machinery. Mol Microbiol 63: 1054-1068.
    • (2007) Mol Microbiol , vol.63 , pp. 1054-1068
    • Schauer, K.1    Gouget, B.2    Carriere, M.3    de Labigne, A.4    Reuse, H.5
  • 69
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?
    • Schauer, K., Rodionov, D.A., and de Reuse, H. (2008) New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? Trends Biochem Sci 33: 330-338.
    • (2008) Trends Biochem Sci , vol.33 , pp. 330-338
    • Schauer, K.1    de Rodionov, D.A.2    Reuse, H.3
  • 70
    • 84869070822 scopus 로고    scopus 로고
    • Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicum
    • Serventi, F., Youard, Z.A., Murset, V., Huwiler, S., Buhler, D., Richter, M., etal. (2012) Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicum. J Biol Chem 287: 38812-38823.
    • (2012) J Biol Chem , vol.287 , pp. 38812-38823
    • Serventi, F.1    Youard, Z.A.2    Murset, V.3    Huwiler, S.4    Buhler, D.5    Richter, M.6
  • 71
    • 36749071435 scopus 로고    scopus 로고
    • Escherichia coli physiology in Luria-Bertani broth
    • Sezonov, G., Joseleau-Petit, D., and D'Ari, R. (2007) Escherichia coli physiology in Luria-Bertani broth. J Bacteriol 189: 8746-8749.
    • (2007) J Bacteriol , vol.189 , pp. 8746-8749
    • Sezonov, G.1    Joseleau-Petit, D.2    D'Ari, R.3
  • 72
    • 79960003556 scopus 로고    scopus 로고
    • BioMetals: a historical and personal perspective
    • Silver, S. (2011) BioMetals: a historical and personal perspective. Biometals 24: 379-390.
    • (2011) Biometals , vol.24 , pp. 379-390
    • Silver, S.1
  • 73
    • 0029792315 scopus 로고    scopus 로고
    • Bacterial heavy metal resistance: new surprises
    • Silver, S., and Phung, L.T. (1996) Bacterial heavy metal resistance: new surprises. Annu Rev Microbiol 50: 753-789.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 753-789
    • Silver, S.1    Phung, L.T.2
  • 74
    • 7744237723 scopus 로고    scopus 로고
    • Cuprous oxidase activity of CueO from Escherichia coli
    • Singh, S.K., Grass, G., Rensing, C., and Montfort, W.R. (2004) Cuprous oxidase activity of CueO from Escherichia coli. J Bacteriol 186: 7815-7817.
    • (2004) J Bacteriol , vol.186 , pp. 7815-7817
    • Singh, S.K.1    Grass, G.2    Rensing, C.3    Montfort, W.R.4
  • 76
    • 77957684250 scopus 로고    scopus 로고
    • An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential
    • Stork, M., Bos, M.P., Jongerius, I., de Kok, N., Schilders, I., Weynants, V.E., etal. (2010) An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential. PLoS Pathog 6: e1000969.
    • (2010) PLoS Pathog , vol.6
    • Stork, M.1    Bos, M.P.2    de Jongerius, I.3    Kok, N.4    Schilders, I.5    Weynants, V.E.6
  • 77
    • 79952145187 scopus 로고    scopus 로고
    • Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli
    • Su, C.C., Long, F., Zimmermann, M.T., Rajashankar, K.R., Jernigan, R.L., and Yu, E.W. (2011) Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature 470: 558-563.
    • (2011) Nature , vol.470 , pp. 558-563
    • Su, C.C.1    Long, F.2    Zimmermann, M.T.3    Rajashankar, K.R.4    Jernigan, R.L.5    Yu, E.W.6
  • 78
    • 79959758512 scopus 로고    scopus 로고
    • Point mutations change specificity and kinetics of metal uptake by ZupT from Escherichia coli
    • Taudte, N., and Grass, G. (2010) Point mutations change specificity and kinetics of metal uptake by ZupT from Escherichia coli. Biometals 23: 643-656.
    • (2010) Biometals , vol.23 , pp. 643-656
    • Taudte, N.1    Grass, G.2
  • 79
    • 23644449395 scopus 로고    scopus 로고
    • Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism
    • Teplyakov, A., Obmolova, G., Toedt, J., Galperin, M.Y., and Gilliland, G.L. (2005) Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J Bacteriol 187: 5520-5527.
    • (2005) J Bacteriol , vol.187 , pp. 5520-5527
    • Teplyakov, A.1    Obmolova, G.2    Toedt, J.3    Galperin, M.Y.4    Gilliland, G.L.5
  • 80
    • 0020568974 scopus 로고
    • Plasmid controlled resistance to copper in Escherichia coli
    • Tetaz, T.J., and Luke, R.K.J. (1983) Plasmid controlled resistance to copper in Escherichia coli. J Bacteriol 154: 1263-1268.
    • (1983) J Bacteriol , vol.154 , pp. 1263-1268
    • Tetaz, T.J.1    Luke, R.K.J.2
  • 81
    • 57449097569 scopus 로고    scopus 로고
    • Sandwich hybridization assay for sensitive detection of dynamic changes in mRNA transcript levels in crude Escherichia coli cell extracts in response to copper ions
    • Thieme, D., Neubauer, P., Nies, D.H., and Grass, G. (2008) Sandwich hybridization assay for sensitive detection of dynamic changes in mRNA transcript levels in crude Escherichia coli cell extracts in response to copper ions. Appl Environ Microbiol 74: 7463-7470.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 7463-7470
    • Thieme, D.1    Neubauer, P.2    Nies, D.H.3    Grass, G.4
  • 82
    • 0033170990 scopus 로고    scopus 로고
    • The RND superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng, T.-T., Gratwick, K.S., Kollman, J., Park, D., Nies, D.H., Goffeau, A., and Saier, M.H.J. (1999) The RND superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J Mol Microbiol Biotechnol 1: 107-125.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , pp. 107-125
    • Tseng, T.-T.1    Gratwick, K.S.2    Kollman, J.3    Park, D.4    Nies, D.H.5    Goffeau, A.6    Saier, M.H.J.7
  • 83
    • 80052406205 scopus 로고    scopus 로고
    • Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components
    • Volentini, S.I., Farias, R.N., Rodriguez-Montelongo, L., and Rapisarda, V.A. (2011) Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components. Biometals 24: 827-835.
    • (2011) Biometals , vol.24 , pp. 827-835
    • Volentini, S.I.1    Farias, R.N.2    Rodriguez-Montelongo, L.3    Rapisarda, V.A.4
  • 86
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto, K., and Ishihama, A. (2005) Transcriptional response of Escherichia coli to external copper. Mol Microbiol 56: 215-227.
    • (2005) Mol Microbiol , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 87
    • 36849054013 scopus 로고    scopus 로고
    • CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein
    • Zoropogui, A., Gambarelli, S., and Coves, J. (2008) CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein. Biochem Biophys Res Commun 365: 735-739.
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 735-739
    • Zoropogui, A.1    Gambarelli, S.2    Coves, J.3


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