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Volumn 9, Issue 10, 2014, Pages

Streptomyces coelicolor SC04226 is a nickel binding protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; COBALT; COPPER; MANGANESE; NICKEL; SCO4226 PROTEIN; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 84907698729     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0109660     Document Type: Article
Times cited : (9)

References (48)
  • 1
    • 0037892460 scopus 로고
    • Nickel-dependent chemolithotrophic growth of two Hydrogenomonas strains
    • Bartha R, Ordal EJ (1965) Nickel-dependent chemolithotrophic growth of two Hydrogenomonas strains. J Bacteriol 89: 1015-1019.
    • (1965) J Bacteriol , vol.89 , pp. 1015-1019
    • Bartha, R.1    Ordal, E.J.2
  • 2
    • 0038203196 scopus 로고    scopus 로고
    • Nickel uptake and utilization by microorganisms
    • Mulrooney SB, Hausinger RP (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
  • 3
    • 70350680999 scopus 로고    scopus 로고
    • Nickel homeostasis and nickel regulation: An overview
    • Li Y, Zambie DB (2009) Nickel homeostasis and nickel regulation: an overview. Chem Rev 109: 4617-4643.
    • (2009) Chem Rev , vol.109 , pp. 4617-4643
    • Li, Y.1    Zambie, D.B.2
  • 5
    • 0022202912 scopus 로고
    • Isolation and characterization of Ni-specific T cell clones from patients with Nicontact dermatitis
    • Sinigaglia F, Scheidegger D, Garotta G, Scheper R, Pletscher M, et al. (1985) Isolation and characterization of Ni-specific T cell clones from patients with Nicontact dermatitis. J Immunol 135: 3929-3932.
    • (1985) J Immunol , vol.135 , pp. 3929-3932
    • Sinigaglia, F.1    Scheidegger, D.2    Garotta, G.3    Scheper, R.4    Pletscher, M.5
  • 6
    • 0024937730 scopus 로고
    • Nickel and cobalt resistance of various bacteria isolated from soil and highly polluted domestic and industrial wastes
    • Schmidt T, Schlegel HG (1989) Nickel and cobalt resistance of various bacteria isolated from soil and highly polluted domestic and industrial wastes. FEMS Microbiol Lett 62: 315-328.
    • (1989) FEMS Microbiol Lett , vol.62 , pp. 315-328
    • Schmidt, T.1    Schlegel, H.G.2
  • 7
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs S, Bagchi D (1995) Oxidative mechanisms in the toxicity of metal ions. Free Radical Biol Med 18: 321-336.
    • (1995) Free Radical Biol Med , vol.18 , pp. 321-336
    • Stohs, S.1    Bagchi, D.2
  • 9
    • 4444350490 scopus 로고    scopus 로고
    • Nickel essentiality and homeostasis in aquatic organisms
    • Muyssen BT, Brix K, DeForest D, Janssen C (2004) Nickel essentiality and homeostasis in aquatic organisms. Environ Rev 12: 113-131.
    • (2004) Environ Rev , vol.12 , pp. 113-131
    • Muyssen, B.T.1    Brix, K.2    DeForest, D.3    Janssen, C.4
  • 10
    • 24744437494 scopus 로고    scopus 로고
    • Secondary transporters for nickel and cobalt ions: Theme and variations
    • Eitinger T, Suhr J, Moore L, Smith JAC (2005) Secondary transporters for nickel and cobalt ions: theme and variations. BioMetals 18: 399-405.
    • (2005) BioMetals , vol.18 , pp. 399-405
    • Eitinger, T.1    Suhr, J.2    Moore, L.3    Smith, J.A.C.4
  • 11
    • 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 MA, Giordano G, Wu LF (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
  • 12
    • 0033056216 scopus 로고    scopus 로고
    • Selective transport of divalent cations by transition metal permeases: The Alcaligenes eutrophus HoxN and the Rhodococcus rhodochrous NhlF
    • Degen O, Kobayashi M, Shimizu S, Eitinger T (1999) Selective transport of divalent cations by transition metal permeases: the Alcaligenes eutrophus HoxN and the Rhodococcus rhodochrous NhlF. Arch Microbiol 171: 139-145.
    • (1999) Arch Microbiol , vol.171 , pp. 139-145
    • Degen, O.1    Kobayashi, M.2    Shimizu, S.3    Eitinger, T.4
  • 13
    • 0034733505 scopus 로고    scopus 로고
    • 2+-dependent interaction of NikR with wild-type and mutant operator sites
    • Chivers PT, Sauer RT (2000) Regulation of high affinity nickel uptake in bacteria Ni2+-dependent interaction of NikR with wild-type and mutant operator sites. J Biol Chem 275: 19735-19741.
    • (2000) J Biol Chem , vol.275 , pp. 19735-19741
    • Chivers, P.T.1    Sauer, R.T.2
  • 14
    • 0030612325 scopus 로고    scopus 로고
    • The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase
    • Olson JW, Fu C, Maier RJ (1997) The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase. Mol Microbiol 24: 119-128.
    • (1997) Mol Microbiol , vol.24 , pp. 119-128
    • Olson, J.W.1    Fu, C.2    Maier, R.J.3
  • 15
    • 0028911174 scopus 로고
    • HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer
    • Fu C, Olson JW, Maier RJ (1995) HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer. Proc Natl Acad Sci USA 92: 2333-2337.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2333-2337
    • Fu, C.1    Olson, J.W.2    Maier, R.J.3
  • 16
    • 0034053033 scopus 로고    scopus 로고
    • Dual roles of Bradyrhizobium japonicum nickel in protein in nickel storage and GTP-dependent Ni mobilization
    • Olson JW, Maier RJ (2000) Dual roles of Bradyrhizobium japonicum nickel in protein in nickel storage and GTP-dependent Ni mobilization. J Bacteriol 182: 1702-1705.
    • (2000) J Bacteriol , vol.182 , pp. 1702-1705
    • Olson, J.W.1    Maier, R.J.2
  • 17
    • 24744452563 scopus 로고    scopus 로고
    • Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations
    • Grass G, Fricke B, Nies DH (2005) Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations. BioMetals 18: 437-448.
    • (2005) BioMetals , vol.18 , pp. 437-448
    • Grass, G.1    Fricke, B.2    Nies, D.H.3
  • 18
    • 0035059229 scopus 로고    scopus 로고
    • NreB from Achromobacter xylosoxidans 31A is a nickel-induced transporter conferring nickel resistance
    • Grass G, Fan B, Rosen BP, Lemke K, Schlegel HG, et al. (2001) NreB from Achromobacter xylosoxidans 31A is a nickel-induced transporter conferring nickel resistance. J Bacteriol 183: 2803-2807.
    • (2001) J Bacteriol , vol.183 , pp. 2803-2807
    • Grass, G.1    Fan, B.2    Rosen, B.P.3    Lemke, K.4    Schlegel, H.G.5
  • 19
    • 0033925731 scopus 로고    scopus 로고
    • Primary metabolism and its control in Streptomycetes: A most unusual group of bacteria
    • Hodgson DA (2000) Primary metabolism and its control in Streptomycetes: a most unusual group of bacteria. Adv Microb Physiol 42: 47-238.
    • (2000) Adv Microb Physiol , vol.42 , pp. 47-238
    • Hodgson, D.A.1
  • 20
    • 55549086417 scopus 로고    scopus 로고
    • Streptomyces morphogenetics: Dissecting differentiation in a filamentous bacterium
    • Flärdh K, Buttner MJ (2009) Streptomyces morphogenetics: dissecting differentiation in a filamentous bacterium. Nat Rev Microbiol 7: 36-49.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 36-49
    • Flärdh, K.1    Buttner, M.J.2
  • 21
    • 84867465992 scopus 로고    scopus 로고
    • Specific metal recognition in nickel trafficking
    • Higgins KA, Carr CE, Maroney MJ (2012) Specific metal recognition in nickel trafficking. Biochemistry 51: 7816-7832.
    • (2012) Biochemistry , vol.51 , pp. 7816-7832
    • Higgins, K.A.1    Carr, C.E.2    Maroney, M.J.3
  • 22
    • 33645467335 scopus 로고    scopus 로고
    • Nur, a nickelresponsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor
    • Ahn BE, Cha J, Lee EJ, Han AR, Thompson CJ, et al. (2006) Nur, a nickelresponsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor. Mol Microbiol 59: 1848-1858.
    • (2006) Mol Microbiol , vol.59 , pp. 1848-1858
    • Ahn, B.E.1    Cha, J.2    Lee, E.J.3    Han, A.R.4    Thompson, C.J.5
  • 23
    • 0029778889 scopus 로고    scopus 로고
    • A novel nickel-containing superoxide dismutase from Streptomyces spp
    • Youn H, Kim E, Roe J, Hah Y, Kang S (1996) A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem J 318: 889-896.
    • (1996) Biochem J , vol.318 , pp. 889-896
    • Youn, H.1    Kim, E.2    Roe, J.3    Hah, Y.4    Kang, S.5
  • 24
    • 0029849183 scopus 로고    scopus 로고
    • Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces Coelicolor
    • Kim EJ, Kim HP, Hah YC, Roe JH (1996) Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces Coelicolor. Eur J Biochem 241: 178-185.
    • (1996) Eur J Biochem , vol.241 , pp. 178-185
    • Kim, E.J.1    Kim, H.P.2    Hah, Y.C.3    Roe, J.H.4
  • 26
    • 51149114194 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SC04226 from Streptomyces coelicolor A3 (2)
    • Wang S, He YX, Bao R, Teng YB, Ye BP, et al. (2008) Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SC04226 from Streptomyces coelicolor A3 (2). Acta Crystallogr F 64: 847-850.
    • (2008) Acta Crystallogr F , vol.64 , pp. 847-850
    • Wang, S.1    He, Y.X.2    Bao, R.3    Teng, Y.B.4    Ye, B.P.5
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data. Method Enzymol 276: 307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0002662106 scopus 로고    scopus 로고
    • Denzo and Scalepack
    • M. G Rossmann and E Arnold Netherlands Kluwer Academic
    • Otwinowski Z, Minor W (2001) Denzo and Scalepack. In: M. G Rossmann and E Arnold, editors. International Tables for Crystallography Volume F. Netherlands: Kluwer Academic, pp. 226-235.
    • (2001) International Tables for Crystallography , pp. 226-235
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie A (1999) Integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 55: 1696-1702.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1696-1702
    • Leslie, A.1
  • 31
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30: 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 32
  • 35
  • 36
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383.
    • (2007) Nucleic Acids Res , vol.35 , pp. W375-W383
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 38
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 39
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L, Sander C (1998) Touring protein fold space with Dali/FSSP. Nucleic Acids Res 26: 316-319.
    • (1998) Nucleic Acids Res , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 40
    • 25844521203 scopus 로고    scopus 로고
    • Active site sharing and subterminal hairpin recognition in a new class of DNA transposases
    • Ronning DR, Guynet C, Ton-Hoang B, Perez ZN, Ghirlando R, et al. (2005) Active site sharing and subterminal hairpin recognition in a new class of DNA transposases. Mol Cell 20: 143-154.
    • (2005) Mol Cell , vol.20 , pp. 143-154
    • Ronning, D.R.1    Guynet, C.2    Ton-Hoang, B.3    Perez, Z.N.4    Ghirlando, R.5
  • 41
    • 77953257812 scopus 로고    scopus 로고
    • Structural and mechanistic insights into Helicobacter pylori NikR activation
    • Bahlawane C, Dian C, Muller C, Round A, Fauquant C, et al. (2010) Structural and mechanistic insights into Helicobacter pylori NikR activation. Nucleic Acids Res 38: 3106-3118.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3106-3118
    • Bahlawane, C.1    Dian, C.2    Muller, C.3    Round, A.4    Fauquant, C.5
  • 42
    • 33646138246 scopus 로고    scopus 로고
    • The metal-and DNA-binding activities of Helicobacter pylori NikR
    • Abraham LO, Li Y, Zamble DB (2006) The metal-and DNA-binding activities of Helicobacter pylori NikR. J Inorg Biochem, 100: 1005-1014.
    • (2006) J Inorg Biochem , vol.100 , pp. 1005-1014
    • Abraham, L.O.1    Li, Y.2    Zamble, D.B.3
  • 43
    • 34547130605 scopus 로고    scopus 로고
    • 2+-dependent transcription factor NikR is required for specific DNA binding
    • Benanti EL, Chivers PT (2007) The N-terminal arm of the Helicobacter pylori Ni2+-dependent transcription factor NikR is required for specific DNA binding. J Biol Chem 282: 20365-20375.
    • (2007) J Biol Chem , vol.282 , pp. 20365-20375
    • Benanti, E.L.1    Chivers, P.T.2
  • 46
    • 0038452402 scopus 로고    scopus 로고
    • 2+) in metalloproteins
    • Rulísek L, Vondrásek J (1998) Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins. J Inorg Biochem 71: 115-127.
    • (1998) J Inorg Biochem , vol.71 , pp. 115-127
    • Rulísek, L.1    Vondrásek, J.2
  • 47
    • 77956411916 scopus 로고    scopus 로고
    • Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli
    • Phillips CM, Schreker ER, Stultz CM, Drennan CL (2010) Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli. Biochemistry 49: 7830-7838.
    • (2010) Biochemistry , vol.49 , pp. 7830-7838
    • Phillips, C.M.1    Schreker, E.R.2    Stultz, C.M.3    Drennan, C.L.4
  • 48
    • 0029070195 scopus 로고
    • Protein Hpn: Cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae
    • Gilbert J, Ramakrishna J, Sunderman F, Wright A, Plaut A (1995) Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect Immun 63: 2682-2688.
    • (1995) Infect Immun , vol.63 , pp. 2682-2688
    • Gilbert, J.1    Ramakrishna, J.2    Sunderman, F.3    Wright, A.4    Plaut, A.5


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