메뉴 건너뛰기




Volumn 459, Issue 3, 2014, Pages 525-538

Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans

Author keywords

Copper chaperone; Cytochrome c oxidase; Morphological development; Streptomyces

Indexed keywords

BINDING PROTEIN; CHAPERONE; COPPER; COPPER PROTEIN; CUPROUS ION; CYSTEINE; CYTOCHROME C OXIDASE; EXTRACYTOPLASMIC COPPER CHAPERONE LIKE PROTEIN; METALLOCHAPERONE; UNCLASSIFIED DRUG;

EID: 84898650541     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140017     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 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. U.S.A. 106, 8344-8349
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 3
    • 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
    • Ohalloran, T.V.1    Culotta, V.C.2
  • 5
    • 0035798652 scopus 로고    scopus 로고
    • Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase
    • Arnesano, F., Banci, L., Bertini, I., Cantini, F., Ciofi-Baffoni, S., Huffman, D. L. and O?Halloran, T. V. (2001) Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J. Biol. Chem. 276, 41365-41376
    • (2001) J. Biol. Chem. , vol.276 , pp. 41365-41376
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5    Huffman, D.L.6    Ohalloran, T.V.7
  • 6
    • 33644696300 scopus 로고    scopus 로고
    • A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: The interplay of domains
    • DOI 10.1074/jbc.M506219200
    • Banci, L., Bertini, I., Cantini, F., Chasapis, C. T., Hadjiliadis, N. and Rosato, A. (2005) A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains. J. Biol. Chem. 280, 38259-38263 (Pubitemid 43853722)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38259-38263
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Chasapis, C.T.4    Hadjiliadis, N.5    Rosato, A.6
  • 11
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase
    • DOI 10.1074/jbc.M404747200
    • Horng, Y. C., Cobine, P. A., Maxfield, A. B., Carr, H. S. and Winge, D. R. (2004) Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase. J. Biol. Chem. 279, 35334-35340 (Pubitemid 39100532)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35334-35340
    • Horng, Y.-C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 12
    • 0025071742 scopus 로고
    • Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. Denitrificans protein encoded by ORF3
    • Tzagoloff, A., Capitanio, N., Nobrega, M. P. and Gatti, D. (1990) Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3. EMBO J. 9, 2759-2764
    • (1990) EMBO J. , vol.9 , pp. 2759-2764
    • Tzagoloff, A.1    Capitanio, N.2    Nobrega, M.P.3    Gatti, D.4
  • 13
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase
    • DOI 10.1074/jbc.275.1.619
    • Hiser, L., Di Valentin, M., Hamer, A. G. and Hosler, J. P. (2000) Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase. J. Biol. Chem. 275, 619-623 (Pubitemid 30039026)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 14
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.34.20531
    • Glerum, D. M., Shtanko, A. and Tzagoloff, A. (1996) SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271, 20531-20535 (Pubitemid 26281827)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20531-20535
    • Moira Glerum, D.1    Shtanko, A.2    Tzagoloff, A.3
  • 15
    • 0033025125 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase
    • DOI 10.1007/s002940050438
    • Rentzsch, A., Krummeck-Weiss, G., Hofer, A., Bartuschka, A., Ostermann, K. and Rodel, G. (1999) Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Curr. Genet. 35, 103-108 (Pubitemid 29141252)
    • (1999) Current Genetics , vol.35 , Issue.2 , pp. 103-108
    • Rentzsch, A.1    Krummeck-Weiss, G.2    Hofer, A.3    Bartuschka, A.4    Ostermann, K.5    Rodel, G.6
  • 16
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein
    • Nittis, T., George, G. N. and Winge, D. R. (2001) Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J. Biol. Chem. 276, 42520-42526
    • (2001) J. Biol. Chem. , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 17
    • 79959306944 scopus 로고    scopus 로고
    • Seeking the determinants of the elusive functions of Sco proteins
    • Banci, L., Bertini, I., Cavallaro, G. and Ciofi-Baffoni, S. (2011) Seeking the determinants of the elusive functions of Sco proteins. FEBS J. 278, 2244-2262
    • (2011) FEBS J. , vol.278 , pp. 2244-2262
    • Banci, L.1    Bertini, I.2    Cavallaro, G.3    Ciofi-Baffoni, S.4
  • 20
    • 84860653311 scopus 로고    scopus 로고
    • The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa3-type and the cbb3-type cytochrome c oxidases
    • Thompson, A. K., Gray, J., Liu, A. and Hosler, J. P. (2012) The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa3-type and the cbb3-type cytochrome c oxidases. Biochim. Biophys. Acta 1817, 955-964
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 955-964
    • Thompson, A.K.1    Gray, J.2    Liu, A.3    Hosler, J.P.4
  • 22
    • 0025889035 scopus 로고
    • Genetic manipulation of Streptomyces: Integrating vectors and gene replacement
    • Kieser, T. and Hopwood, D. A. (1991) Genetic manipulation of Streptomyces: integrating vectors and gene replacement. Methods Enzymol. 204, 430-458
    • (1991) Methods Enzymol. , vol.204 , pp. 430-458
    • Kieser, T.1    Hopwood, D.A.2
  • 23
    • 0030867564 scopus 로고    scopus 로고
    • Stimulatory effect of copper on antibiotic production and morphological differentiation in Streptomyces tanashiensis
    • Ueda, K., Tomaru, Y., Endoh, K. and Beppu, T. (1997) Stimulatory effect of copper on antibiotic production and morphological differentiation in Streptomyces tanashiensis. J. Antibiot. (Tokyo) 50, 693-695 (Pubitemid 27401707)
    • (1997) Journal of Antibiotics , vol.50 , Issue.8 , pp. 693-695
    • Ueda, K.1    Tomaru, Y.2    Endoh, K.3    Beppu, T.4
  • 26
    • 84877761743 scopus 로고    scopus 로고
    • Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein
    • Blundell, K. L. I. M., Wilson, M. T., Svistunenko, D. A., Vijgenboom, E. and Worrall, J. A. R. (2013) Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein. Open Biol. 3, 120163
    • (2013) Open Biol. , vol.3 , pp. 120163
    • Blundell, K.L.I.M.1    Wilson, M.T.2    Svistunenko, D.A.3    Vijgenboom, E.4    Worrall, J.A.R.5
  • 27
    • 77951990361 scopus 로고    scopus 로고
    • Copper mining in Streptomyces: Enzymes, natural products and development
    • Worrall, J. A. R. and Vijgenboom, E. (2010) Copper mining in Streptomyces: enzymes, natural products and development. Nat. Prod. Rep. 27, 742-756
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 742-756
    • Worrall, J.A.R.1    Vijgenboom, E.2
  • 28
    • 0034666433 scopus 로고    scopus 로고
    • Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis
    • Mattatall, N. R., Jazairi, J. and Hill, B. C. (2000) Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J. Biol. Chem. 275, 28802-28809
    • (2000) J. Biol. Chem. , vol.275 , pp. 28802-28809
    • Mattatall, N.R.1    Jazairi, J.2    Hill, B.C.3
  • 29
    • 79951552770 scopus 로고    scopus 로고
    • The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: Evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco
    • Siluvai, G. S., Nakano, M., Mayfield, M. and Blackburn, N. J. (2011) The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco. J. Biol. Inorg. Chem. 16, 285-297
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 285-297
    • Siluvai, G.S.1    Nakano, M.2    Mayfield, M.3    Blackburn, N.J.4
  • 30
    • 84879962033 scopus 로고    scopus 로고
    • The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein
    • Blundell, K. L. I. M., Wilson, M. T., Vijgenboom, E. and Worrall, J. A. R. (2013) The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein. Dalton Trans. 42, 10608-10616
    • (2013) Dalton Trans. , vol.42 , pp. 10608-10616
    • Blundell, K.L.I.M.1    Wilson, M.T.2    Vijgenboom, E.3    Worrall, J.A.R.4
  • 32
    • 0020505048 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase
    • Green, G. N. and Gennis, R. B. (1983) Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. J. Bacteriol. 154, 1269-1275 (Pubitemid 13099040)
    • (1983) Journal of Bacteriology , vol.154 , Issue.3 , pp. 1269-1275
    • Green, G.N.1    Gennis, R.B.2
  • 33
    • 0024729626 scopus 로고
    • Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis
    • Mueller, J. P. and Taber, H. W. (1989) Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis. J. Bacteriol. 171, 4967-4978
    • (1989) J. Bacteriol. , vol.171 , pp. 4967-4978
    • Mueller, J.P.1    Taber, H.W.2
  • 34
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • DOI 10.1093/nar/gkg563
    • Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R. D. and Bairoch, A. (2003) ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31, 3784-3788 (Pubitemid 37442246)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 35
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • DOI 10.1093/nar/gkh371
    • Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673 (Pubitemid 38997420)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Whitmore, L.1    Wallace, B.A.2
  • 36
    • 44349084237 scopus 로고    scopus 로고
    • Transfer of copper between bis(thiosemicarbazone) ligands and intracellular copper-binding proteins. Insights into mechanisms of copper uptake and hypoxia selectivity
    • Xiao, Z., Donnelly, P. S., Zimmermann, M. and Wedd, A. G. (2008) Transfer of copper between bis(thiosemicarbazone) ligands and intracellular copper-binding proteins. Insights into mechanisms of copper uptake and hypoxia selectivity. Inorg. Chem. 47, 4338-4347
    • (2008) Inorg. Chem. , vol.47 , pp. 4338-4347
    • Xiao, Z.1    Donnelly, P.S.2    Zimmermann, M.3    Wedd, A.G.4
  • 37
    • 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
    • DOI 10.1021/ja0390350
    • 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 (Pubitemid 38380713)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.10 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 38
    • 79953211568 scopus 로고    scopus 로고
    • Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: Detection probes and affinity standards
    • Xiao, Z., Brose, J., Schimo, S., Ackland, S. M., La Fontaine, S. and Wedd, A. G. (2011) Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards. J. Biol. Chem. 286, 11047-11055
    • (2011) J. Biol. Chem. , vol.286 , pp. 11047-11055
    • Xiao, Z.1    Brose, J.2    Schimo, S.3    Ackland, S.M.4    La Fontaine, S.5    Wedd, A.G.6
  • 42
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • DOI 10.1107/S0907444906022116
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011 (Pubitemid 44337374)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 43
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • DOI 10.1038/8263
    • Perrakis, A., Morris, R. and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463 (Pubitemid 29218016)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 48
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of betaI-and betaII-proteins
    • Sreerama, N. and Woody, R. W. (2003) Structural composition of betaI-and betaII-proteins. Protein Sci. 12, 384-388
    • (2003) Protein Sci. , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 49
    • 77957927380 scopus 로고    scopus 로고
    • NmerA of tn501 mercuric ion reductase: Structural modulation of the pKa values of the metal binding cysteine thiols
    • Ledwidge, R., Hong, B., Dotsch, V. and Miller, S. M. (2010) NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols. Biochemistry 49, 8988-8998
    • (2010) Biochemistry , vol.49 , pp. 8988-8998
    • Ledwidge, R.1    Hong, B.2    Dotsch, V.3    Miller, S.M.4
  • 50
    • 79952265848 scopus 로고    scopus 로고
    • Copper trafficking mechanism of CXXC-containing domains: Insight from the pH-dependence of their Cu(I) affinities
    • Badarau, A. and Dennison, C. (2011) Copper trafficking mechanism of CXXC-containing domains: insight from the pH-dependence of their Cu(I) affinities. J. Am. Chem. Soc. 133, 2983-2988
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2983-2988
    • Badarau, A.1    Dennison, C.2
  • 52
    • 80051996196 scopus 로고    scopus 로고
    • Thermodynamics of copper and zinc distribution in the cyanobacterium Synechocystis PCC 6803
    • Badarau, A. and Dennison, C. (2011) Thermodynamics of copper and zinc distribution in the cyanobacterium Synechocystis PCC 6803. Proc. Natl. Acad. Sci. U.S.A. 108, 13007-13012
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 13007-13012
    • Badarau, A.1    Dennison, C.2
  • 53
    • 77953946552 scopus 로고    scopus 로고
    • Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of Wilson disease protein
    • Rodriguez-Granillo, A., Crespo, A., Estrin, D. A. and Wittung-Stafshede, P. (2010) Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of Wilson disease protein. J. Phys. Chem. B. 114, 3698-3706
    • (2010) J. Phys. Chem. B. , vol.114 , pp. 3698-3706
    • Rodriguez-Granillo, A.1    Crespo, A.2    Estrin, D.A.3    Wittung-Stafshede, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.