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Volumn 87, Issue 3, 2013, Pages 466-477

The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves P1B-type ATPase copper efflux and periplasmic CueP

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COPPER BINDING PROTEIN; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; COPPER ZINC SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 84873060682     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12107     Document Type: Article
Times cited : (83)

References (49)
  • 1
    • 77951228745 scopus 로고    scopus 로고
    • The multi-copper-ion oxidase CueO of Salmonella enterica serovar Typhimurium is required for systemic virulence
    • Achard, M.E.S., Tree, J.J., Holden, J.A., Simpfendorfer, K.R., Wijburg, O.L.C., Strugnell, R.A., etal. (2010) The multi-copper-ion oxidase CueO of Salmonella enterica serovar Typhimurium is required for systemic virulence. Infect Immun 78: 2312-2319.
    • (2010) Infect Immun , vol.78 , pp. 2312-2319
    • Achard, M.E.S.1    Tree, J.J.2    Holden, J.A.3    Simpfendorfer, K.R.4    Wijburg, O.L.C.5    Strugnell, R.A.6
  • 2
    • 46649107577 scopus 로고    scopus 로고
    • Regulatory and structural differences in the Cu,Zn-superoxide dismutases of Salmonella enterica and their significance for virulence
    • Ammendola, S., Pasquali, P., Pacello, F., Rotilio, G., Castor, M., Libby, S.J., etal. (2008) Regulatory and structural differences in the Cu, Zn-superoxide dismutases of Salmonella enterica and their significance for virulence. J Biol Chem 283: 13688-13699.
    • (2008) J Biol Chem , vol.283 , pp. 13688-13699
    • Ammendola, S.1    Pasquali, P.2    Pacello, F.3    Rotilio, G.4    Castor, M.5    Libby, S.J.6
  • 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
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C., and 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
  • 7
  • 8
    • 33947129778 scopus 로고    scopus 로고
    • Salmonella, the host and disease: a brief review
    • Coburn, B., Grassl, G.A., and Finlay, B.B. (2007) Salmonella, the host and disease: a brief review. Immunol Cell Biol 85: 112-118.
    • (2007) Immunol Cell Biol , vol.85 , pp. 112-118
    • Coburn, B.1    Grassl, G.A.2    Finlay, B.B.3
  • 9
    • 72049112816 scopus 로고    scopus 로고
    • Interaction between cyanobacterial copper chaperone Atx1 and zinc homeostasis
    • Dainty, S.J., Patterson, C.J., Waldron, K.J., and Robinson, N.J. (2010) Interaction between cyanobacterial copper chaperone Atx1 and zinc homeostasis. J Biol Inorg Chem 15: 77-85.
    • (2010) J Biol Inorg Chem , vol.15 , pp. 77-85
    • Dainty, S.J.1    Patterson, C.J.2    Waldron, K.J.3    Robinson, N.J.4
  • 10
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 11
    • 0009543864 scopus 로고    scopus 로고
    • Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase
    • De Groote, M.A., Ochsner, U.A., Shiloh, M.U., Nathan, C., McCord, J.M., Dinauer, M.C., etal. (1997) Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase. Proc Natl Acad Sci USA 94: 13997-14001.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13997-14001
    • De Groote, M.A.1    Ochsner, U.A.2    Shiloh, M.U.3    Nathan, C.4    McCord, J.M.5    Dinauer, M.C.6
  • 14
    • 0011736531 scopus 로고
    • Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent
    • Fields, P.I., Swanson, R.V., Haidaris, C.G., and Heffron, F. (1986) Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proc Natl Acad Sci USA 83: 5189-5193.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5189-5193
    • Fields, P.I.1    Swanson, R.V.2    Haidaris, C.G.3    Heffron, F.4
  • 15
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli
    • Franke, S., Grass, G., Rensing, C., and Nies, D.H. (2003) Molecular analysis of the copper-transporting efflux system CusCFBA of 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
  • 20
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • Huffman, D.L., and O'Halloran, T.V. (2000) Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J Biol Chem 275: 18611-18614.
    • (2000) J Biol Chem , vol.275 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 21
    • 0034913058 scopus 로고    scopus 로고
    • Function, structure, and mechanism of intracellular copper trafficking proteins
    • Huffman, D.L., and O'Halloran, T.V. (2001) Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem 70: 677-701.
    • (2001) Annu Rev Biochem , vol.70 , pp. 677-701
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 22
    • 77950638212 scopus 로고    scopus 로고
    • Protecting against antimicrobial effectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium
    • Kim, B., Richards, S.M., Gunn, J.S., and Slauch, J.M. (2010) Protecting against antimicrobial effectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium. J Bacteriol 192: 2140-2149.
    • (2010) J Bacteriol , vol.192 , pp. 2140-2149
    • Kim, B.1    Richards, S.M.2    Gunn, J.S.3    Slauch, J.M.4
  • 23
    • 3843084999 scopus 로고    scopus 로고
    • Differences in enzymatic properties allow SodCI but not SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium strain 14028
    • Krishnakumar, R., Craig, M., Imlay, J.A., and Slauch, J.M. (2004) Differences in enzymatic properties allow SodCI but not SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium strain 14028. J Bacteriol 186: 5230-5238.
    • (2004) J Bacteriol , vol.186 , pp. 5230-5238
    • Krishnakumar, R.1    Craig, M.2    Imlay, J.A.3    Slauch, J.M.4
  • 24
    • 34250348371 scopus 로고    scopus 로고
    • Structural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar Typhimurium
    • Krishnakumar, R., Kim, B., Mollo, E.A., Imlay, J.A., and Slauch, J.M. (2007) Structural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar Typhimurium. J Bacteriol 189: 4343-4352.
    • (2007) J Bacteriol , vol.189 , pp. 4343-4352
    • Krishnakumar, R.1    Kim, B.2    Mollo, E.A.3    Imlay, J.A.4    Slauch, J.M.5
  • 25
    • 34748859338 scopus 로고    scopus 로고
    • Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy
    • Loftin, I.R., Franke, S., Blackburn, N.J., and McEvoy, M.M. (2007) Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Sci 16: 2287-2293.
    • (2007) Protein Sci , vol.16 , pp. 2287-2293
    • Loftin, I.R.1    Franke, S.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 28
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund, S., and Marklund, G. (1974) Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47: 469-474.
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 29
    • 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
  • 30
    • 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
  • 31
    • 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
  • 32
    • 32044441204 scopus 로고    scopus 로고
    • Individual metal ligands play distinct functional roles in the zinc sensor Staphylococcus aureus CzrA
    • Pennella, M.A., Arunkumar, A.I., and Giedroc, D.P. (2006) Individual metal ligands play distinct functional roles in the zinc sensor Staphylococcus aureus CzrA. J Mol Biol 356: 1124-1136.
    • (2006) J Mol Biol , vol.356 , pp. 1124-1136
    • Pennella, M.A.1    Arunkumar, A.I.2    Giedroc, D.P.3
  • 34
    • 0034665626 scopus 로고    scopus 로고
    • Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene
    • Pesce, A., Battistoni, A., Stroppolo, M.E., Polizio, F., Nardini, M., Kroll, J.S., etal. (2000) Functional and crystallographic characterization of Salmonella typhimurium Cu, Zn superoxide dismutase coded by the sodCI virulence gene. J Mol Biol 302: 465-478.
    • (2000) J Mol Biol , vol.302 , pp. 465-478
    • Pesce, A.1    Battistoni, A.2    Stroppolo, M.E.3    Polizio, F.4    Nardini, M.5    Kroll, J.S.6
  • 35
    • 25444517605 scopus 로고    scopus 로고
    • A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm
    • Pittman, M.S., Robinson, H.C., and Poole, R.K. (2005) A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm. J Biol Chem 280: 32254-32261.
    • (2005) J Biol Chem , vol.280 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 36
    • 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
  • 37
    • 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
  • 41
    • 80855132841 scopus 로고    scopus 로고
    • Either periplasmic tethering or protease resistance is sufficient to allow a SodC to protect Salmonella enterica serovar Typhimurium from phagocytic superoxide
    • Rushing, M.D., and Slauch, J.M. (2011) Either periplasmic tethering or protease resistance is sufficient to allow a SodC to protect Salmonella enterica serovar Typhimurium from phagocytic superoxide. Mol Microbiol 82: 952-963.
    • (2011) Mol Microbiol , vol.82 , pp. 952-963
    • Rushing, M.D.1    Slauch, J.M.2
  • 43
    • 0032167580 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase from Photobacterium leiognathi is an hyperefficient enzyme
    • Stroppolo, M.E., Sette, M., O'Neill, P., Polizio, F., Cambria, M.T., and Desideri, A. (1998) Cu, Zn superoxide dismutase from Photobacterium leiognathi is an hyperefficient enzyme. Biochemistry 37: 12287-12292.
    • (1998) Biochemistry , vol.37 , pp. 12287-12292
    • Stroppolo, M.E.1    Sette, M.2    O'Neill, P.3    Polizio, F.4    Cambria, M.T.5    Desideri, A.6
  • 45
    • 0035827547 scopus 로고    scopus 로고
    • Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803
    • Tottey, S., Rich, P.R., Rondet, S.A.M., and Robinson, N.J. (2001) Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803. J Biol Chem 276: 19999-20004.
    • (2001) J Biol Chem , vol.276 , pp. 19999-20004
    • Tottey, S.1    Rich, P.R.2    Rondet, S.A.M.3    Robinson, N.J.4
  • 48
    • 0242627233 scopus 로고    scopus 로고
    • Let's Sco1, Oxidase! Let's Sco!
    • Winge, D.R. (2003) Let's Sco1, Oxidase! Let's Sco! Structure 11: 1313-1314.
    • (2003) Structure , vol.11 , pp. 1313-1314
    • Winge, D.R.1
  • 49
    • 1642404510 scopus 로고    scopus 로고
    • C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking
    • Xiao, Z., Loughlin, F., George, G.N., Howlett, G.J., and Wedd, A.G. (2004) C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J Am Chem Soc 126: 3081-3090.
    • (2004) J Am Chem Soc , vol.126 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5


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