메뉴 건너뛰기




Volumn 288, Issue 1, 2013, Pages 69-78

The mechanism of Cu+ transport ATPases: Interaction with CU + chaperones and the role of transient metal-binding sites

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEOGLOBUS FULGIDUS; ATP-ASE ACTIVITY; ATPASES; COMPLEMENTATION; ION PATHS; LEGIONELLA PNEUMOPHILA; LIGAND EXCHANGES; MEMBRANE PROTEINS; METAL RELEASE; METAL-BINDING SITES; THIOL GROUPS; TRANSMEMBRANE SEGMENTS; TRANSMEMBRANES;

EID: 84872072402     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.420810     Document Type: Article
Times cited : (66)

References (44)
  • 2
    • 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
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • DOI 10.2174/0929867053764635
    • Valko, M., Morris, H., and Cronin, M. T. (2005) Metals, toxicity and oxidative stress. Curr. Med. Chem. 12, 1161-1208 (Pubitemid 40655271)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.10 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.D.3
  • 4
    • 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
  • 5
    • 77953471147 scopus 로고    scopus 로고
    • Human copper transporters. Mechanism, role in human diseases and therapeutic potential
    • Gupta, A., and Lutsenko, S. (2009) Human copper transporters. Mechanism, role in human diseases and therapeutic potential. Future Med. Chem. 1, 1125-1142
    • (2009) Future Med. Chem. , vol.1 , pp. 1125-1142
    • Gupta, A.1    Lutsenko, S.2
  • 6
    • 56149117733 scopus 로고    scopus 로고
    • Copper homeostasis in bacteria
    • Osman, D., and Cavet, J. S. (2008) Copper homeostasis in bacteria. Adv. Appl. Microbiol. 65, 217-247
    • (2008) Adv. Appl. Microbiol. , vol.65 , pp. 217-247
    • Osman, D.1    Cavet, J.S.2
  • 7
    • 70350029582 scopus 로고    scopus 로고
    • Copper transport in mammalian cells. Special care for a metal with special needs
    • Kaplan, J. H., and Lutsenko, S. (2009) Copper transport in mammalian cells. Special care for a metal with special needs. J. Biol. Chem. 284, 25461-25465
    • (2009) J. Biol. Chem. , vol.284 , pp. 25461-25465
    • Kaplan, J.H.1    Lutsenko, S.2
  • 8
    • 25844489990 scopus 로고    scopus 로고
    • 1B-ATPases - An ancient family of transition metal pumps with diverse functions in plants
    • DOI 10.1016/j.tplants.2005.08.008, PII S1360138505002050
    • Williams, L. E., and Mills, R. F. (2005) P(1B)-ATPases. An ancient family of transition metal pumps with diverse functions in plants. Trends Plant Sci. 10, 491-502 (Pubitemid 41395271)
    • (2005) Trends in Plant Science , vol.10 , Issue.10 , pp. 491-502
    • Williams, L.E.1    Mills, R.F.2
  • 9
    • 0035117191 scopus 로고    scopus 로고
    • Copper delivery by metallochaperone proteins
    • Rosenzweig, A. C. (2001) Copper delivery by metallochaperone proteins. Acc. Chem. Res. 34, 119-128
    • (2001) Acc. Chem. Res. , vol.34 , pp. 119-128
    • Rosenzweig, A.C.1
  • 11
    • 84859972108 scopus 로고    scopus 로고
    • Metal transport across biomembranes. Emerging models for a distinct chemistry
    • Argüello, J. M., Raimunda, D., and González-Guerrero, M. (2012) Metal transport across biomembranes. Emerging models for a distinct chemistry. J. Biol. Chem. 287, 13510-13517
    • (2012) J. Biol. Chem. , vol.287 , pp. 13510-13517
    • Argüello, J.M.1    Raimunda, D.2    González-Guerrero, M.3
  • 13
    • 72049117359 scopus 로고    scopus 로고
    • Structural organization of human Cu-transporting ATPases. Learning from building blocks
    • Barry, A. N., Shinde, U., and Lutsenko, S. (2010) Structural organization of human Cu-transporting ATPases. Learning from building blocks. J. Biol. Inorg. Chem. 15, 47-59
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 47-59
    • Barry, A.N.1    Shinde, U.2    Lutsenko, S.3
  • 19
    • 0036175362 scopus 로고    scopus 로고
    • Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures
    • DOI 10.1101/gr.196802
    • Arnesano, F., Banci, L., Bertini, I., Ciofi-Baffoni, S., Molteni, E., Huffman, D. L., and O'Halloran, T. V. (2002) Metallochaperones and metal-transporting ATPases. A comparative analysis of sequences and structures. Genome Res. 12, 255-271 (Pubitemid 34162992)
    • (2002) Genome Research , vol.12 , Issue.2 , pp. 255-271
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Ciofi-Baffoni, S.4    Molteni, E.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 20
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • Boal, A. K., and Rosenzweig, A. C. (2009) Structural biology of copper trafficking. Chem. Rev. 109, 4760-4779
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 21
    • 0141431021 scopus 로고    scopus 로고
    • +-ATPase CopA
    • DOI 10.1021/bi034806y
    • Mandal, A. K., and Argüello, J. M. (2003) Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu+-ATPase CopA. Biochemistry 42, 11040-11047 (Pubitemid 37174396)
    • (2003) Biochemistry , vol.42 , Issue.37 , pp. 11040-11047
    • Mandal, A.K.1    Arguello, J.M.2
  • 22
    • 33746750825 scopus 로고    scopus 로고
    • Role of metal-binding domains of the copper pump from Archaeoglobus fulgidus
    • DOI 10.1016/j.bbrc.2006.07.012, PII S0006291X06015476
    • Rice, W. J., Kovalishin, A., and Stokes, D. L. (2006) Role of metal-binding domains of the copper pump from Archaeoglobus fulgidus. Biochem. Biophys. Res. Commun. 348, 124-131 (Pubitemid 44163491)
    • (2006) Biochemical and Biophysical Research Communications , vol.348 , Issue.1 , pp. 124-131
    • Rice, W.J.1    Kovalishin, A.2    Stokes, D.L.3
  • 23
    • 0037033056 scopus 로고    scopus 로고
    • Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase
    • DOI 10.1074/jbc.M208490200
    • Fan, B., and Rosen, B. P. (2002) Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. 277, 46987-46992 (Pubitemid 36159204)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 46987-46992
    • Fan, B.1    Rosen, B.P.2
  • 25
    • 44649182134 scopus 로고    scopus 로고
    • Structure of a Copper Pump Suggests a Regulatory Role for Its Metal-Binding Domain
    • DOI 10.1016/j.str.2008.02.025, PII S0969212608001512
    • Wu, C. C., Rice, W. J., and Stokes, D. L. (2008) Structure of a copper pump suggests a regulatory role for its metal-binding domain. Structure 16, 976-985 (Pubitemid 351778383)
    • (2008) Structure , vol.16 , Issue.6 , pp. 976-985
    • Wu, C.-C.1    Rice, W.J.2    Stokes, D.L.3
  • 26
    • 0035910261 scopus 로고    scopus 로고
    • 1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • 1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner. J. Biol. Chem. 276, 2234-2242
    • (2001) J. Biol. Chem. , vol.276 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3
  • 28
    • 0033153380 scopus 로고    scopus 로고
    • Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution
    • DOI 10.1016/S0969-2126(99)80082-3
    • Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Structure 7, 605-617 (Pubitemid 29277414)
    • (1999) Structure , vol.7 , Issue.6 , pp. 605-617
    • Rosenzweig, A.C.1    Huffman, D.L.2    Hou, M.Y.3    Wernimont, A.K.4    Pufahl, R.A.5    O'Halloran, T.V.6
  • 30
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • DOI 10.1074/jbc.C000172200
    • 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 (Pubitemid 30422815)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T. L., and Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2, 28-36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 37
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein. Expr. Purif. 41, 207-234
    • (2005) Protein. Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 39
    • 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
  • 40
    • 0028945240 scopus 로고
    • A quantitative test for copper using bicinchoninic acid
    • Brenner, A. J., and Harris, E. D. (1995) A quantitative test for copper using bicinchoninic acid. Anal. Biochem. 226, 80-84
    • (1995) Anal. Biochem. , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 41
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • DOI 10.1016/0003-2697(79)90115-5
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100, 95-97 (Pubitemid 10157636)
    • (1979) Analytical Biochemistry , vol.100 , Issue.1 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 42
    • 77954687479 scopus 로고    scopus 로고
    • Cellular copper distribution. A mechanistic systems biology approach
    • Banci, L., Bertini, I., Cantini, F., and Ciofi-Baffoni, S. (2010) Cellular copper distribution. A mechanistic systems biology approach. Cell. Mol. Life Sci. 67, 2563-2589
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 2563-2589
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4
  • 44
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont, A. K., Huffman, D. L., Lamb, A. L., O'Halloran, T. V., and Rosenzweig, A. C. (2000) Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 7, 766-771
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.