메뉴 건너뛰기




Volumn 43, Issue 31, 2004, Pages 10018-10028

Selectivity of metal binding and metal-induced stability of Escherichia coli NikP

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; IONS; NICKEL COMPOUNDS; PROTEINS; SPECTROSCOPY;

EID: 3543056937     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049405c     Document Type: Article
Times cited : (83)

References (62)
  • 2
    • 0033120016 scopus 로고    scopus 로고
    • Structure/function relationships in nickel biochemistry
    • Maroney, M. J. (1999) Structure/function relationships in nickel biochemistry, Curr. Opin. Chem. Biol. 3, 188-199.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 188-199
    • Maroney, M.J.1
  • 4
    • 0037392103 scopus 로고    scopus 로고
    • Molecular mechanisms of nickel carcinogenesis: Gene silencing by nickel delivery to the nucleus and gene activation/inactivation by nickel-induced cell signaling
    • Costa, M., Yan, Y., Zhao, D., and Salnikow, K. (2003) Molecular mechanisms of nickel carcinogenesis: gene silencing by nickel delivery to the nucleus and gene activation/inactivation by nickel-induced cell signaling, J. Environ. Monit. 5, 222-223.
    • (2003) J. Environ. Monit. , vol.5 , pp. 222-223
    • Costa, M.1    Yan, Y.2    Zhao, D.3    Salnikow, K.4
  • 5
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L. S., Pennella, M. A., and Giedroc, D. P. (2003) The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance, FEMS Microbiol. Rev. 27, 131-143.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 6
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • Finney, L. A., and O'Halloran, T. V. (2003) Transition metal speciation in the cell: insights from the chemistry of metal ion receptors, Science 300, 931-936.
    • (2003) Science , vol.300 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 8
    • 0038203196 scopus 로고    scopus 로고
    • Nickel uptake and utilization by microorganisms
    • Mulrooney, S. B., and Hausinger, R. P. (2003) Nickel uptake and utilization by microorganisms, FEMS Microbiol. Rev. 27, 239-261.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 239-261
    • Mulrooney, S.B.1    Hausinger, R.P.2
  • 9
    • 0038719677 scopus 로고    scopus 로고
    • The protein complex composed of nickel-binding SrnQ and DNA-binding motif-bearing SrnR of Streptomyces griseus represses sodF transcription in the presence of nickel
    • Kim, J.-S., Kang, S.-O., and Lee, J. K. (2003) The protein complex composed of nickel-binding SrnQ and DNA-binding motif-bearing SrnR of Streptomyces griseus represses sodF transcription in the presence of nickel, J. Biol. Chem. 278, 18455-18463.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18455-18463
    • Kim, J.-S.1    Kang, S.-O.2    Lee, J.K.3
  • 11
    • 0036194664 scopus 로고    scopus 로고
    • A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803
    • López-Maury, L., García-Domínguez, M., Florencio, F. J., and Reyes, J. C. (2002) A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803, Mol. Microbiol. 43, 247-256.
    • (2002) Mol. Microbiol. , vol.43 , pp. 247-256
    • López-Maury, L.1    García-Domínguez, M.2    Florencio, F.J.3    Reyes, J.C.4
  • 12
    • 0032932493 scopus 로고    scopus 로고
    • Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli
    • De Pina, K., Desjardin, V., Mandrand-Berthelot, M.-A., Giordano, G., and Wu, L.-F. (1999) Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli, J. Bacteriol. 181, 670-674.
    • (1999) J. Bacteriol. , vol.181 , pp. 670-674
    • De Pina, K.1    Desjardin, V.2    Mandrand-Berthelot, M.-A.3    Giordano, G.4    Wu, L.-F.5
  • 13
    • 0034733505 scopus 로고    scopus 로고
    • Regulation of high affinity nickel uptake in bacteria
    • Chivers, P. T., and Sauer, R. T. (2000) Regulation of high affinity nickel uptake in bacteria, J. Biol. Chem. 275, 19735-19741.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19735-19741
    • Chivers, P.T.1    Sauer, R.T.2
  • 14
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori
    • Contreras, M., Thiberge, J.-M., Mandrand-Berthelot, M.-A., and Labigne, A. (2003) Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori, Mol. Microbiol. 49, 947-963.
    • (2003) Mol. Microbiol. , vol.49 , pp. 947-963
    • Contreras, M.1    Thiberge, J.-M.2    Mandrand-Berthelot, M.-A.3    Labigne, A.4
  • 15
    • 0022639247 scopus 로고
    • Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity
    • Wu, L. F., and Mandrand-Berthelot, M. A. (1986) Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity, Biochimie 68, 167-179.
    • (1986) Biochimie , vol.68 , pp. 167-179
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 16
    • 0032697047 scopus 로고    scopus 로고
    • NikR is a ribbon-helix-helix DNA-binding protein
    • Chivers, P. T., and Sauer, R. T. (1999) NikR is a ribbon-helix-helix DNA-binding protein, Protein Sci. 8, 2494-2500.
    • (1999) Protein Sci. , vol.8 , pp. 2494-2500
    • Chivers, P.T.1    Sauer, R.T.2
  • 17
    • 0036774881 scopus 로고    scopus 로고
    • NikR repressor: High-affinity nickel binding to the C-terminal domain regulates binding to operator DNA
    • Chivers, P. T., and Sauer, R. T. (2002) NikR repressor: high-affinity nickel binding to the C-terminal domain regulates binding to operator DNA, Chem. Biol. 9, 1141-1148.
    • (2002) Chem. Biol. , vol.9 , pp. 1141-1148
    • Chivers, P.T.1    Sauer, R.T.2
  • 21
    • 0038349048 scopus 로고    scopus 로고
    • Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators
    • Guedon, E., and Helmann, J. D. (2003) Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators, Mol. Microbiol. 48, 495-506.
    • (2003) Mol. Microbiol. , vol.48 , pp. 495-506
    • Guedon, E.1    Helmann, J.D.2
  • 23
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 26
    • 0033572730 scopus 로고    scopus 로고
    • Aqueous coordination chemistry of quinolone-bases fluorescence probes for the biological chemistry of zinc
    • Fahrni, C. J., and O'Halloran, T. V. (1999) Aqueous coordination chemistry of quinolone-bases fluorescence probes for the biological chemistry of zinc, J. Am. Chem. Soc. 121, 11448-11458.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11448-11458
    • Fahrni, C.J.1    O'Halloran, T.V.2
  • 27
    • 0025157183 scopus 로고
    • Uptake and intracellular sequestration of divalent cations in resting and methacholine-stimulated mouse lacrimal acinar cells
    • Kwan, C.-Y., and Putney, J. W. J. (1990) Uptake and intracellular sequestration of divalent cations in resting and methacholine-stimulated mouse lacrimal acinar cells, J. Biol. Chem. 265, 678-684.
    • (1990) J. Biol. Chem. , vol.265 , pp. 678-684
    • Kwan, C.-Y.1    Putney, J.W.J.2
  • 29
    • 0014718113 scopus 로고
    • Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970) Theoretical models for the mechanism of denaturation, Adv. Protein Chem. 24, 1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 30
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 31
    • 0034003762 scopus 로고    scopus 로고
    • Spectroscopic characterization of Co(II)-, Ni(II)-, and Cd(II)-substituted wild-type and non-native retroviral-type zinc finger peptides
    • Chen, X., Chu, M., and Giedroc, D. P. (2000) Spectroscopic characterization of Co(II)-, Ni(II)-, and Cd(II)-substituted wild-type and non-native retroviral-type zinc finger peptides, J. Biol. Inorg. Chem. 5, 93-101.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 93-101
    • Chen, X.1    Chu, M.2    Giedroc, D.P.3
  • 33
    • 0017785176 scopus 로고
    • Biological analogues. On the nature of the binding sites of copper-containing proteins
    • Amundsen, A. R., Whelan, J., and Bosnich, B. (1977) Biological analogues. On the nature of the binding sites of copper-containing proteins, J. Am. Chem. Soc. 99, 6730-6739.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 6730-6739
    • Amundsen, A.R.1    Whelan, J.2    Bosnich, B.3
  • 34
    • 0018225148 scopus 로고
    • Newly synthesized sulfhydryl- and imidazole-containing tripeptides with a specific copper-binding site
    • Sugiura, Y. (1978) Newly synthesized sulfhydryl- and imidazole-containing tripeptides with a specific copper-binding site, Inorg. Chem. 17, 2176-2182.
    • (1978) Inorg. Chem. , vol.17 , pp. 2176-2182
    • Sugiura, Y.1
  • 35
    • 0000515305 scopus 로고
    • Characterization of [dimethyl N,N′-ethylenebis(L-cysteinato)-(2-)- S,S′]copper(II), Cu(SCH2CH(CO2CH3)NHCH2-)2, a stable Cu(II)-aliphatic dithiolate
    • Bharadwaj, P. K., Potenza, J. A., and Schugar, H. J. (1986) Characterization of [dimethyl N,N′-ethylenebis(L-cysteinato)-(2-)-S, S′]copper(II), Cu(SCH2CH(CO2CH3)NHCH2-)2, a stable Cu(II)-aliphatic dithiolate, J. Am. Chem. Soc. 108, 1351-1352.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1351-1352
    • Bharadwaj, P.K.1    Potenza, J.A.2    Schugar, H.J.3
  • 36
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • Bertini, I., and Luchinat, C. (1984) High spin cobalt(II) as a probe for the investigation of metalloproteins, Adv. Inorg. Biochem. 6, 71-111.
    • (1984) Adv. Inorg. Biochem. , vol.6 , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 37
    • 0027425204 scopus 로고
    • Cobalt as probe and label of proteins
    • Maret, W., and Vallee, B. L. (1993) Cobalt as probe and label of proteins, Methods Enzymol. 226, 52-71.
    • (1993) Methods Enzymol. , vol.226 , pp. 52-71
    • Maret, W.1    Vallee, B.L.2
  • 39
    • 0017818322 scopus 로고
    • Preparation and properties of cobalt(II) rubredoxin
    • May, S. W., and Kuo, J.-Y. (1978) Preparation and properties of cobalt(II) rubredoxin, Biochemistry 17, 3333-3338.
    • (1978) Biochemistry , vol.17 , pp. 3333-3338
    • May, S.W.1    Kuo, J.-Y.2
  • 40
    • 0035812424 scopus 로고    scopus 로고
    • Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR
    • Hitomi, Y., Outten, C. E., and O'Halloran, T. V. (2001) Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR, J. Am. Chem. Soc. 123, 8614-8615.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8614-8615
    • Hitomi, Y.1    Outten, C.E.2    O'Halloran, T.V.3
  • 41
    • 2942715463 scopus 로고
    • Kinetics of the ligand substitution reaction of the zinc(II)-4-(2- pyridylazo)-resorcinol complex with (ethylene glycol)bis(2-aminoethyl ether)-N,N,N′,N′-tetraacetic acid
    • Tanaka, M., Funahashi, S., and Shirai, K. (1968) Kinetics of the ligand substitution reaction of the zinc(II)-4-(2-pyridylazo)-resorcinol complex with (ethylene glycol)bis(2-aminoethyl ether)-N,N,N′,N′-tetraacetic acid, Inorg. Chem. 7, 573-578.
    • (1968) Inorg. Chem. , vol.7 , pp. 573-578
    • Tanaka, M.1    Funahashi, S.2    Shirai, K.3
  • 42
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., Neece, S. H., and Ginsburg, A. (1985) The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase, Anal. Biochem. 146, 150-157.
    • (1985) Anal. Biochem. , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 43
    • 0030919897 scopus 로고    scopus 로고
    • Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization
    • Walkup, G. K., and Imperiali, B. (1997) Fluorescent chemosensors for divalent zinc based on zinc finger domains. Enhanced oxidative stability, metal binding affinity, and structural and functional characterization, J. Am. Chem. Soc. 119, 3443-3450.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3443-3450
    • Walkup, G.K.1    Imperiali, B.2
  • 44
    • 0345542210 scopus 로고
    • Spectrophotometric study of the complex equilibria of cadmium(II) ions with 4-(2-pyridylazo)resorcinol (PAR) using the squad-G program and the method of determining Cd(II) ions with PAR
    • Vlčková, S., Jaňář, L., Kubáň, V., and Havel, J. (1982) Spectrophotometric study of the complex equilibria of cadmium(II) ions with 4-(2-pyridylazo)resorcinol (PAR) using the squad-G program and the method of determining Cd(II) ions with PAR, Collect. Czech. Chem. Commun. 47, 1086-1099.
    • (1982) Collect. Czech. Chem. Commun. , vol.47 , pp. 1086-1099
    • Vlčková, S.1    Jaňář, L.2    Kubáň, V.3    Havel, J.4
  • 46
    • 0036301096 scopus 로고    scopus 로고
    • Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: Evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins
    • Busenlehner, L. S., Weng, T.-C., Penner-Hahn, J. E., and Giedroc, D. P. (2002) Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: evolutionary implications for metal ion selectivity of ArsR/ SmtB metal sensor proteins, J. Mol. Biol. 319, 685-701.
    • (2002) J. Mol. Biol. , vol.319 , pp. 685-701
    • Busenlehner, L.S.1    Weng, T.-C.2    Penner-Hahn, J.E.3    Giedroc, D.P.4
  • 47
    • 3543072246 scopus 로고    scopus 로고
    • Metal-selective DNA-binding response of Escherichia coli NikR
    • Bloom, S. B., and Zamble, D. B. (2004) Metal-selective DNA-binding response of Escherichia coli NikR, Biochemistry 43, 10029-10038.
    • (2004) Biochemistry , vol.43 , pp. 10029-10038
    • Bloom, S.B.1    Zamble, D.B.2
  • 49
    • 0034651201 scopus 로고    scopus 로고
    • Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens
    • Wittung-Stafshede, P., Gomes, C. M., and Teixeira, M. (2000) Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens, J. Inorg. Biochem. 78, 35-41.
    • (2000) J. Inorg. Biochem. , vol.78 , pp. 35-41
    • Wittung-Stafshede, P.1    Gomes, C.M.2    Teixeira, M.3
  • 50
    • 0030668204 scopus 로고    scopus 로고
    • The effect of the metal ion on the folding energetics of azurin: A comparison of the native, zinc and apoprotein
    • Leckner, J., Bonander, N., Wittung-Stafshede, P., Malmström, B. G., and Karlsson, G. (1997) The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc and apoprotein, Biochim. Biophys. Acta 1342, 19-27.
    • (1997) Biochim. Biophys. Acta , vol.1342 , pp. 19-27
    • Leckner, J.1    Bonander, N.2    Wittung-Stafshede, P.3    Malmström, B.G.4    Karlsson, G.5
  • 51
    • 0031414716 scopus 로고    scopus 로고
    • Energetics of heme binding to native and denatured states of cytochrome b562
    • Robinson, C. R., Liu, Y., Thomson, J. A., Sturtevant, J. M., and Sligar, S. G. (1997) Energetics of heme binding to native and denatured states of cytochrome b562, Biochemistry 36, 16141-16146.
    • (1997) Biochemistry , vol.36 , pp. 16141-16146
    • Robinson, C.R.1    Liu, Y.2    Thomson, J.A.3    Sturtevant, J.M.4    Sligar, S.G.5
  • 52
    • 0034660451 scopus 로고    scopus 로고
    • No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin
    • Apiyo, D., Guidry, J., and Wittung-Stafshede, P. (2000) No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin, Biochim. Biophys. Acta 1479, 214-224.
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 214-224
    • Apiyo, D.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 53
    • 0035856539 scopus 로고    scopus 로고
    • Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin
    • Pozdnyakova, I., and Wittung-Stafshede, P. (2001) Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin, Biochemistry 40, 13728-13733.
    • (2001) Biochemistry , vol.40 , pp. 13728-13733
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 56
    • 21544440823 scopus 로고
    • Order of stability of metal complexes
    • Irving, H., and Williams, R. J. P. (1948) Order of stability of metal complexes, Nature 162, 746-747.
    • (1948) Nature , vol.162 , pp. 746-747
    • Irving, H.1    Williams, R.J.P.2
  • 57
    • 1842591322 scopus 로고    scopus 로고
    • Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis
    • McCall, K. A., and Fierke, C. A. (2004) Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis, Biochemistry 43, 3979-3986.
    • (2004) Biochemistry , vol.43 , pp. 3979-3986
    • McCall, K.A.1    Fierke, C.A.2
  • 58
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H., and Colón, W. (1997) Kinetic role of early intermediates in protein folding, Curr. Opin. Struct. Biol. 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 59
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove, M. S., and Olson, J. S. (1996) The stability of holomyoglobin is determined by heme affinity, Biochemistry 35, 11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 60
    • 0016624901 scopus 로고
    • (Meister, A., Ed.), John Wiley & Sons, New York
    • Jencks, W. P. (1975) in Advances in Enzymology (Meister, A., Ed.) pp 219-410, John Wiley & Sons, New York.
    • (1975) Advances in Enzymology , pp. 219-410
    • Jencks, W.P.1
  • 61
    • 0041428115 scopus 로고    scopus 로고
    • Designing redox metalloproteins from bottom-up and top-down perspectives
    • Barker, P. D. (2003) Designing redox metalloproteins from bottom-up and top-down perspectives, Curr. Opin. Struct. Biol. 13, 490-499.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 490-499
    • Barker, P.D.1
  • 62
    • 0031885768 scopus 로고    scopus 로고
    • The construction of metal centers in proteins by rational design
    • Hellinga, H., W. (1998) The construction of metal centers in proteins by rational design, Folding Des. 3, R1-R8.
    • (1998) Folding Des. , vol.3
    • Hellinga, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.