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Volumn 84, Issue 6, 2012, Pages 1139-1149

Role in metal homeostasis of CtpD, a Co 2+ transporting P1B4-ATPase of Mycobacterium smegmatis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COBALT; NICKEL; PROTEIN CTPD; SUPEROXIDE; UNCLASSIFIED DRUG; ZINC;

EID: 84865199126     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08082.x     Document Type: Article
Times cited : (48)

References (46)
  • 1
    • 0141987910 scopus 로고    scopus 로고
    • Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases
    • Argüello, J.M. (2003) Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases. J Membr Biol 195: 93-108.
    • (2003) J Membr Biol , vol.195 , pp. 93-108
    • Argüello, J.M.1
  • 2
    • 34248633103 scopus 로고    scopus 로고
    • The structure and function of heavy metal transport P1BATPases
    • Argüello, J.M., Eren, E., and González-Guerrero, M. (2007) The structure and function of heavy metal transport P1BATPases. Biometals 20: 233-248.
    • (2007) Biometals , vol.20 , pp. 233-248
    • Argüello, J.M.1    Eren, E.2    González-Guerrero, M.3
  • 3
    • 81255142801 scopus 로고    scopus 로고
    • Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence
    • Argüello, J.M., González-Guerrero, M., and Raimunda, D. (2011) Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence. Biochemistry 50: 9940-9949.
    • (2011) Biochemistry , vol.50 , pp. 9940-9949
    • Argüello, J.M.1    González-Guerrero, M.2    Raimunda, D.3
  • 4
    • 84859972108 scopus 로고    scopus 로고
    • Metal transport across biomembranes: emerging models for a distinct chemistry
    • Argüello, J.M., González-Guerrero, M., and Raimunda, D. (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    González-Guerrero, M.2    Raimunda, D.3
  • 5
    • 3142632027 scopus 로고    scopus 로고
    • Chimeras of P1-type ATPases and their tran-scriptional regulators: contributions of a cytosolic aminoterminal domain to metal specificity
    • Borrelly, G.P.M., Rondet, S.A.M., Tottey, S., and Robinson, N.J. (2004) Chimeras of P1-type ATPases and their tran-scriptional regulators: contributions of a cytosolic aminoterminal domain to metal specificity. Mol Microbiol 53: 217-227.
    • (2004) Mol Microbiol , vol.53 , pp. 217-227
    • Borrelly, G.P.M.1    Rondet, S.A.M.2    Tottey, S.3    Robinson, N.J.4
  • 6
    • 80053049896 scopus 로고    scopus 로고
    • Mycobacterial P-1-type ATPases mediate resistance to zinc poisoning in human macrophages
    • Botella, H., Peyron, P., Levillain, F., Poincloux, R., Poquet, Y., Brandli, I., et al. (2011) Mycobacterial P-1-type ATPases mediate resistance to zinc poisoning in human macrophages. Cell Host Microbe 10: 248-259.
    • (2011) Cell Host Microbe , vol.10 , pp. 248-259
    • Botella, H.1    Peyron, P.2    Levillain, F.3    Poincloux, R.4    Poquet, Y.5    Brandli, I.6
  • 7
    • 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
  • 10
    • 84856368815 scopus 로고    scopus 로고
    • The Biological Chemistry of the Elements: The Inorganic Chemistry of Life
    • Oxford: Oxford University Press.
    • Fraústro da Silva, J.J.R., and Williams, R.J.P. (2001) The Biological Chemistry of the Elements: The Inorganic Chemistry of Life. Oxford: Oxford University Press.
    • (2001)
    • Fraústro da Silva, J.J.R.1    Williams, R.J.P.2
  • 11
    • 0036041795 scopus 로고    scopus 로고
    • A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis
    • Gaballa, A., and Helmann, J.D. (2002) A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Mol Microbiol 45: 997-1005.
    • (2002) Mol Microbiol , vol.45 , pp. 997-1005
    • Gaballa, A.1    Helmann, J.D.2
  • 12
    • 43149096496 scopus 로고    scopus 로고
    • Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites
    • González-Guerrero, M., and Argüello, J.M. (2008) Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites. Proc Natl Acad Sci USA 105: 5992-5997.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5992-5997
    • González-Guerrero, M.1    Argüello, J.M.2
  • 13
    • 57649148770 scopus 로고    scopus 로고
    • Structure of the two transmembrane Cu+ transport sites of the Cu+-ATPases
    • González-Guerrero, M., Eren, E., Rawat, S., Stemmler, T.L., and Argüello, J.M. (2008) Structure of the two transmembrane Cu+ transport sites of the Cu+-ATPases. J Biol Chem 283: 29753-29759.
    • (2008) J Biol Chem , vol.283 , pp. 29753-29759
    • González-Guerrero, M.1    Eren, E.2    Rawat, S.3    Stemmler, T.L.4    Argüello, J.M.5
  • 14
    • 78649536013 scopus 로고    scopus 로고
    • Distinct functional roles of homologous Cu+ efflux ATPases in Pseudomonas aeruginosa
    • González-Guerrero, M., Raimunda, D., Cheng, X., and Argüello, J.M. (2010) Distinct functional roles of homologous Cu+ efflux ATPases in Pseudomonas aeruginosa. Mol Microbiol 78: 1246-1258.
    • (2010) Mol Microbiol , vol.78 , pp. 1246-1258
    • González-Guerrero, M.1    Raimunda, D.2    Cheng, X.3    Argüello, J.M.4
  • 15
    • 33749348163 scopus 로고    scopus 로고
    • Identification and characterization of a major Zn(II) resistance determinant of Mycobacterium smegmatis
    • Grover, A., and Sharma, R. (2006) Identification and characterization of a major Zn(II) resistance determinant of Mycobacterium smegmatis. J Bacteriol 188: 7026-7032.
    • (2006) J Bacteriol , vol.188 , pp. 7026-7032
    • Grover, A.1    Sharma, R.2
  • 16
    • 0031046749 scopus 로고    scopus 로고
    • Zinc site redesign in T4 gene 32 protein: structure and stability of cobalt(II) complexes formed by wild-type and metal ligand substitution mutants
    • Guo, J., and Giedroc, D. (1997) Zinc site redesign in T4 gene 32 protein: structure and stability of cobalt(II) complexes formed by wild-type and metal ligand substitution mutants. Biochemistry 36: 730-742.
    • (1997) Biochemistry , vol.36 , pp. 730-742
    • Guo, J.1    Giedroc, D.2
  • 18
    • 0026716643 scopus 로고
    • Membrane protein structure prediction: hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992) Membrane protein structure prediction: hydrophobicity analysis and the positive-inside rule. J Mol Biol 225: 487-494.
    • (1992) J Mol Biol , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 19
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., Boon-Chieng, S., and Mitaku, S. (1998) SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14: 378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 21
    • 33947357684 scopus 로고    scopus 로고
    • Recombineering in Mycobacterium tuberculosis
    • van Kessel, J.C., and Hatfull, G.F. (2007) Recombineering in Mycobacterium tuberculosis. Nat Methods 4: 147-152. Kim, Y.Y., Choi, H., Segami, S., Cho, H.T., Martinoia, E., Maeshima, M., and Lee, Y. (2009) AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis. Plant J 58: 737-753.
    • (2007) Nat Methods , vol.4 , pp. 147-152
    • van Kessel, J.C.1    Hatfull, G.F.2
  • 22
    • 66349100468 scopus 로고    scopus 로고
    • AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis
    • Kim, Y.Y., Choi, H., Segami, S., Cho, H.T., Martinoia, E., Maeshima, M., and Lee, Y. (2009) AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis. Plant J 58: 737-753.
    • (2009) Plant J , vol.58 , pp. 737-753
    • Kim, Y.Y.1    Choi, H.2    Segami, S.3    Cho, H.T.4    Martinoia, E.5    Maeshima, M.6    Lee, Y.7
  • 23
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • 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.
    • (1979) Anal Biochem , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 24
    • 31044446123 scopus 로고    scopus 로고
    • Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity
    • Liu, J., Dutta, S.J., Stemmler, A.J., and Mitra, B. (2006) Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity. Biochemistry 45: 763-772.
    • (2006) Biochemistry , vol.45 , pp. 763-772
    • Liu, J.1    Dutta, S.J.2    Stemmler, A.J.3    Mitra, B.4
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-DDC(T)) method
    • Livak, K.J., and Schmittgen, T.D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-DDC(T)) method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
  • 27
    • 0142103656 scopus 로고    scopus 로고
    • 2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain
    • 2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain. J Biol Chem 278: 40534-40541.
    • (2003) J Biol Chem , vol.278 , pp. 40534-40541
    • Mana-Capelli, S.1    Mandal, A.K.2    Argüello, J.M.3
  • 28
    • 0036510741 scopus 로고    scopus 로고
    • Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus
    • Mandal, A.K., Cheung, W.D., and Argüello, J.M. (2002) Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus. J Biol Chem 277: 7201-7208.
    • (2002) J Biol Chem , vol.277 , pp. 7201-7208
    • Mandal, A.K.1    Cheung, W.D.2    Argüello, J.M.3
  • 30
    • 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
  • 31
    • 0030203863 scopus 로고    scopus 로고
    • Tree View: an application to display phylogenetic trees on personal computers
    • Page, R.D.M. (1996) Tree View: an application to display phylogenetic trees on personal computers. Comput Appl Biosci 12: 357-358.
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 32
    • 79959979258 scopus 로고    scopus 로고
    • The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function
    • Raimunda, D., González-Guerrero, M., Leeber, B.W., and Argüello, J.M. (2011) The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function. Biometals 24: 467-475.
    • (2011) Biometals , vol.24 , pp. 467-475
    • Raimunda, D.1    González-Guerrero, M.2    Leeber, B.W.3    Argüello, J.M.4
  • 34
    • 33846040629 scopus 로고    scopus 로고
    • TransportDB: a comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels
    • Ren, Q., Chen, K., and Paulsen, I.T. (2007) TransportDB: a comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels. Nucleic Acids Res 35: D274-D279.
    • (2007) Nucleic Acids Res , vol.35
    • Ren, Q.1    Chen, K.2    Paulsen, I.T.3
  • 35
    • 79961103204 scopus 로고    scopus 로고
    • A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model
    • Rosadini, C.V., Gawronski, J.D., Raimunda, D., Argüello, J.M., and Akerley, B.J. (2011) A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model. Infect Immun 79: 3366-3376.
    • (2011) Infect Immun , vol.79 , pp. 3366-3376
    • Rosadini, C.V.1    Gawronski, J.D.2    Raimunda, D.3    Argüello, J.M.4    Akerley, B.J.5
  • 36
    • 0033520471 scopus 로고    scopus 로고
    • Cobalt-dependent transcriptional switching by a dualeffector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase
    • Rutherford, J.C., Cavet, J.S., and Robinson, N.J. (1999) Cobalt-dependent transcriptional switching by a dualeffector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase. J Biol Chem 274: 25827-25832.
    • (1999) J Biol Chem , vol.274 , pp. 25827-25832
    • Rutherford, J.C.1    Cavet, J.S.2    Robinson, N.J.3
  • 37
    • 0001760677 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • NY: Cold Spring Harbor Laboratory Press.
    • Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1989) Cold Spring Harbor
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 38
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti, C.M., and Rubin, E.J. (2003) Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci USA 100: 12989-12994.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 39
    • 70350146566 scopus 로고    scopus 로고
    • CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34
    • Scherer, J., and Nies, D.H. (2009) CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34. Mol Microbiol 73: 601-621.
    • (2009) Mol Microbiol , vol.73 , pp. 601-621
    • Scherer, J.1    Nies, D.H.2
  • 40
    • 33646153414 scopus 로고    scopus 로고
    • HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions
    • Seigneurin-Berny, D., Gravot, A., Auroy, P., Mazard, C., Kraut, A., Finazzi, G., et al. (2006) HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions. J Biol Chem 281: 2882-2892.
    • (2006) J Biol Chem , vol.281 , pp. 2882-2892
    • Seigneurin-Berny, D.1    Gravot, A.2    Auroy, P.3    Mazard, C.4    Kraut, A.5    Finazzi, G.6
  • 41
    • 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
  • 42
    • 0027968068 scopus 로고
    • Clustal-W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positionspecific 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, positionspecific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 0037059855 scopus 로고    scopus 로고
    • Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells
    • Tsivkovskii, R., Eisses, J.F., Kaplan, J.H., and Lutsenko, S. (2002) Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells. J Biol Chem 277: 976-983.
    • (2002) J Biol Chem , vol.277 , pp. 976-983
    • Tsivkovskii, R.1    Eisses, J.F.2    Kaplan, J.H.3    Lutsenko, S.4
  • 44
    • 12444344631 scopus 로고    scopus 로고
    • Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system
    • Wagner, D., Maser, J., Lai, B., Cai, Z., Barry, C.E., 3rd, Honer Zu Bentrup, K., et al. (2005) Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system. J Immunol 174: 1491-1500.
    • (2005) J Immunol , vol.174 , pp. 1491-1500
    • Wagner, D.1    Maser, J.2    Lai, B.3    Cai, Z.4    Barry III, C.E.5    Honer Zu Bentrup, K.6
  • 46
    • 71749115454 scopus 로고    scopus 로고
    • A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity
    • White, C., Lee, J., Kambe, T., Fritsche, K., and Petris, M.J. (2009) A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity. J Biol Chem 284: 33949-33956.
    • (2009) J Biol Chem , vol.284 , pp. 33949-33956
    • White, C.1    Lee, J.2    Kambe, T.3    Fritsche, K.4    Petris, M.J.5


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