메뉴 건너뛰기




Volumn 183, Issue 1, 2005, Pages 9-18

FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress

Author keywords

Cation diffusion facilitators; E. coli; Efflux; Fluorescence quenching; Iron; Zinc

Indexed keywords

CATION TRANSPORT PROTEIN; DYE; EDETIC ACID; FERROUS IRON EFFLUX PROTEIN; IRON 55; IRON BINDING PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 12444299959     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-004-0739-4     Document Type: Article
Times cited : (179)

References (57)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ (2000) A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J Biol Chem 275:19906-19912
    • (2000) J Biol Chem , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 3
    • 0021277078 scopus 로고
    • Calcium efflux from Escherichia coli. Evidence for two systems
    • Ambudkar SV, Zlotnick GW, Rosen BP (1984) Calcium efflux from Escherichia coli. Evidence for two systems. J Biol Chem 259:6142-6146
    • (1984) J Biol Chem , vol.259 , pp. 6142-6146
    • Ambudkar, S.V.1    Zlotnick, G.W.2    Rosen, B.P.3
  • 5
    • 0344578041 scopus 로고    scopus 로고
    • CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34
    • Anton A, Grosse C, Reissmann J, Pribyl T, Nies DH (1999) CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34. J Bacteriol 181:6876-6881
    • (1999) J Bacteriol , vol.181 , pp. 6876-6881
    • Anton, A.1    Grosse, C.2    Reissmann, J.3    Pribyl, T.4    Nies, D.H.5
  • 6
    • 7744220357 scopus 로고    scopus 로고
    • Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans and Escherichia coli
    • in press
    • Anton A, Weltrowski A, Haney CJ, Franke S, Grass G, Rensing C, Nies DH (in press) Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans and Escherichia coli. J Bacteriol
    • J Bacteriol
    • Anton, A.1    Weltrowski, A.2    Haney, C.J.3    Franke, S.4    Grass, G.5    Rensing, C.6    Nies, D.H.7
  • 7
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • Bachmann BJ (1972) Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol Rev 36:525-557
    • (1972) Bacteriol Rev , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 8
    • 0346634896 scopus 로고    scopus 로고
    • Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes
    • Bloss T, Clemens S, Nies DH (2002) Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes. Planta 214:783-791
    • (2002) Planta , vol.214 , pp. 783-791
    • Bloss, T.1    Clemens, S.2    Nies, D.H.3
  • 10
    • 1842530384 scopus 로고    scopus 로고
    • Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB
    • Chao Y, Fu D (2004a) Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB. J Biol Chem 279:12043-12050
    • (2004) J Biol Chem , vol.279 , pp. 12043-12050
    • Chao, Y.1    Fu, D.2
  • 11
    • 2342429689 scopus 로고    scopus 로고
    • Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP
    • Chao Y, Fu D (2004b) Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. J Biol Chem 279:17173-17180
    • (2004) J Biol Chem , vol.279 , pp. 17173-17180
    • Chao, Y.1    Fu, D.2
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97:6640-6645
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0038028683 scopus 로고    scopus 로고
    • Genes encoding proteins of the cation diffusion facilitator family that confer manganese tolerance
    • Delhaize E, Kataoka T, Hebb DM, White RG, Ryan PR (2003) Genes encoding proteins of the cation diffusion facilitator family that confer manganese tolerance. Plant Cell 15:1131-1142
    • (2003) Plant Cell , vol.15 , pp. 1131-1142
    • Delhaize, E.1    Kataoka, T.2    Hebb, D.M.3    White, R.G.4    Ryan, P.R.5
  • 15
    • 0031794474 scopus 로고    scopus 로고
    • Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins
    • Eng BH, Guerinot ML, Eide D, Saier MH Jr (1998) Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins. J Membr Biol 166:1-7
    • (1998) J Membr Biol , vol.166 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier Jr., M.H.4
  • 16
    • 0032582478 scopus 로고    scopus 로고
    • Binding of the fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence
    • Escolar L, Perez-Martin J, de Lorenzo V (1998) Binding of the Fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence. J Mol Biol 283:537-547
    • (1998) J Mol Biol , vol.283 , pp. 537-547
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 17
    • 0036570964 scopus 로고    scopus 로고
    • A review of fluorescence methods for assessing labile iron in cells and biological fluids
    • Esposito BP, Epsztejn S, Breuer W, Cabantchik ZI (2002) A review of fluorescence methods for assessing labile iron in cells and biological fluids. Anal Biochem 304:1-18
    • (2002) Anal Biochem , vol.304 , pp. 1-18
    • Esposito, B.P.1    Epsztejn, S.2    Breuer, W.3    Cabantchik, Z.I.4
  • 18
    • 0035101356 scopus 로고    scopus 로고
    • Genes involved in copper homeostasis in Escherichia coli
    • Grass G, Rensing C (2001) Genes involved in copper homeostasis in Escherichia coli. J Bacteriol 183:2145-2147
    • (2001) J Bacteriol , vol.183 , pp. 2145-2147
    • Grass, G.1    Rensing, C.2
  • 19
    • 0034945014 scopus 로고    scopus 로고
    • ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli
    • Grass G, Fan B, Rosen BP, Franke S, Nies DH, Rensing C (2001a) ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli. J Bacteriol 183:4664-4667
    • (2001) J Bacteriol , vol.183 , pp. 4664-4667
    • Grass, G.1    Fan, B.2    Rosen, B.P.3    Franke, S.4    Nies, D.H.5    Rensing, C.6
  • 20
    • 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, Rensing C (2001b) 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    Rensing, C.6
  • 22
    • 0035486722 scopus 로고    scopus 로고
    • A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria
    • Grunberg K, Wawer C, Tebo BM, Schuler D (2001) A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria. Appl Environ Microbiol 67:4573-4582
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4573-4582
    • Grunberg, K.1    Wawer, C.2    Tebo, B.M.3    Schuler, D.4
  • 24
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell B, Gutteridge JM (1992) Biologically relevant metal ion-dependent hydroxyl radical generation. An update. FEBS Lett 307:108-112
    • (1992) FEBS Lett , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 25
    • 0021699534 scopus 로고
    • Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K12
    • Hantke K (1984) Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K12. Mol Gen Genet 197:337-341
    • (1984) Mol Gen Genet , vol.197 , pp. 337-341
    • Hantke, K.1
  • 26
    • 0037135606 scopus 로고    scopus 로고
    • Functional characterization of a novel mammalian zinc transporter, ZnT6
    • Huang L, Kirschke CP, Gitschier J (2002) Functional characterization of a novel mammalian zinc transporter, ZnT6. J Biol Chem 277:26389-26395
    • (2002) J Biol Chem , vol.277 , pp. 26389-26395
    • Huang, L.1    Kirschke, C.P.2    Gitschier, J.3
  • 27
    • 0022919619 scopus 로고
    • Effects of iron-limitation of Escherichia coli on growth, the respiratory chains and gallium uptake
    • Hubbard JA, Lewandowska KB, Hughes MN, Poole RK (1986) Effects of iron-limitation of Escherichia coli on growth, the respiratory chains and gallium uptake. Arch Microbiol 146:80-86
    • (1986) Arch Microbiol , vol.146 , pp. 80-86
    • Hubbard, J.A.1    Lewandowska, K.B.2    Hughes, M.N.3    Poole, R.K.4
  • 28
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer K, Imlay JA (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci U S A 93:13635-13640
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 29
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange H, Kispal G, Lill R (1999) Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J Biol Chem 274:18989-18996
    • (1999) J Biol Chem , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 31
    • 0030662261 scopus 로고    scopus 로고
    • Characterization of two homologous yeast genes that encode mitochondrial iron transporters
    • Li L, Kaplan J (1997) Characterization of two homologous yeast genes that encode mitochondrial iron transporters. J Biol Chem 272:28485-28493
    • (1997) J Biol Chem , vol.272 , pp. 28485-28493
    • Li, L.1    Kaplan, J.2
  • 32
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse E, Gottesman S (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99:4620-4625
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 34
    • 0021925630 scopus 로고
    • Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals
    • Mergeay M, Nies D, Schlegel HG, Gerits J, Charles P, Van Gijsegem F (1985) Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals. J Bacteriol 162:328-334
    • (1985) J Bacteriol , vol.162 , pp. 328-334
    • Mergeay, M.1    Nies, D.2    Schlegel, H.G.3    Gerits, J.4    Charles, P.5    Van Gijsegem, F.6
  • 36
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies DH (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol Rev 27:313-339
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 37
    • 33644679763 scopus 로고    scopus 로고
    • Essential and toxic effects of elements on microorganisms
    • Anke K, Ihnat M, Stoeppler M (eds) Wiley, Weinheim, p Part II. 1
    • Nies DH (2004) Essential and toxic effects of elements on microorganisms. In: Anke K, Ihnat M, Stoeppler M (eds) Metals and their compounds in the environment. Wiley, Weinheim, p Part II. 1
    • (2004) Metals and Their Compounds in the Environment
    • Nies, D.H.1
  • 38
    • 0033521006 scopus 로고    scopus 로고
    • Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli
    • Nunoshiba T, Obata F, Boss AC, Oikawa S, Mori T, Kawanishi S, Yamamoto K (1999) Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli. J Biol Chem 274:34832-34837
    • (1999) J Biol Chem , vol.274 , pp. 34832-34837
    • Nunoshiba, T.1    Obata, F.2    Boss, A.C.3    Oikawa, S.4    Mori, T.5    Kawanishi, S.6    Yamamoto, K.7
  • 39
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran TV, Culotta VC (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
  • 40
    • 0035903128 scopus 로고    scopus 로고
    • The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
    • Outten FW, Huffman DL, Hale JA, O'Halloran TV (2001) The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem 276:30670-30677
    • (2001) J Biol Chem , vol.276 , pp. 30670-30677
    • Outten, F.W.1    Huffman, D.L.2    Hale, J.A.3    O'Halloran, T.V.4
  • 41
    • 0030953624 scopus 로고    scopus 로고
    • A novel family of ubiquitous heavy metal ion transport proteins
    • Paulsen IT, Saier MH Jr (1997) A novel family of ubiquitous heavy metal ion transport proteins. J Membr Biol 156:99-103
    • (1997) J Membr Biol , vol.156 , pp. 99-103
    • Paulsen, I.T.1    Saier Jr., M.H.2
  • 42
    • 0035859817 scopus 로고    scopus 로고
    • Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense
    • Persans MW, Nieman K, Salt DE (2001) Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense. Proc Natl Acad Sci U S A 98:9995-10000
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9995-10000
    • Persans, M.W.1    Nieman, K.2    Salt, D.E.3
  • 43
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • Pojl E, Haller JC, Mijovilovich A, Meyer-Klaucke W, Garman E, Vasil ML (2003) Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol Microbiol 47:903-915
    • (2003) Mol Microbiol , vol.47 , pp. 903-915
    • Pojl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 44
    • 0035214384 scopus 로고    scopus 로고
    • Nitrate-dependent iron(II) oxidation in paddy soil
    • Ratering S, Schnell S (2001) Nitrate-dependent iron(II) oxidation in paddy soil. Environ Microbiol 3:100-109
    • (2001) Environ Microbiol , vol.3 , pp. 100-109
    • Ratering, S.1    Schnell, S.2
  • 45
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing C, Grass G (2003) Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol Rev 27:197-213
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 46
    • 0020149384 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts
    • Rowley DA, Halliwell B (1982a) Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts. FEBS Lett 142:39-41
    • (1982) FEBS Lett , vol.142 , pp. 39-41
    • Rowley, D.A.1    Halliwell, B.2
  • 47
    • 0020477158 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of thiol compounds
    • Rowley DA, Halliwell B (1982b) Superoxide-dependent formation of hydroxyl radicals in the presence of thiol compounds. FEBS Lett 138:33-36
    • (1982) FEBS Lett , vol.138 , pp. 33-36
    • Rowley, D.A.1    Halliwell, B.2
  • 48
    • 0034672236 scopus 로고    scopus 로고
    • Iron homeostasis: New tales from the crypt
    • Roy CN, Enns CA (2000) Iron homeostasis: new tales from the crypt. Blood 96:4020-4027
    • (2000) Blood , vol.96 , pp. 4020-4027
    • Roy, C.N.1    Enns, C.A.2
  • 50
    • 0036006057 scopus 로고    scopus 로고
    • Ferrous ion transport across chloroplast inner envelope membranes
    • Shingles R, North M, McCarty RE (2002) Ferrous ion transport across chloroplast inner envelope membranes. Plant Physiol 128:1022-1030
    • (2002) Plant Physiol , vol.128 , pp. 1022-1030
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 51
    • 0025141461 scopus 로고
    • Forms of soluble iron in mouse stomach and duodenal lumen: Significance for mucosal uptake
    • Simpson RJ, Peters TJ (1990) Forms of soluble iron in mouse stomach and duodenal lumen: significance for mucosal uptake. Br J Nutr 63:79-89
    • (1990) Br J Nutr , vol.63 , pp. 79-89
    • Simpson, R.J.1    Peters, T.J.2
  • 52
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman R, Yuan DS, Yamaguchi-Iwai Y, Klausner RD, Dancis A (1996) A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271:1552-1557
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2    Yamaguchi-Iwai, Y.3    Klausner, R.D.4    Dancis, A.5
  • 53
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: Protective role of superoxide dismutase
    • Touati D, Jacques M, Tardat B, Bouchard L, Despied S (1995) Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J Bacteriol 177:2305-2314
    • (1995) J Bacteriol , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 56
    • 0033102221 scopus 로고    scopus 로고
    • Overexpression of a novel Arabidopsis gene related to putative zinc-transporter genes from animals can lead to enhanced zinc resistance and accumulation
    • van der Zaal BJ, Neuteboom LW, Pinas JE, Chardonnens AN, Schat H, Verkleij JA, Hooykaas PJ (1999) Overexpression of a novel Arabidopsis gene related to putative zinc-transporter genes from animals can lead to enhanced zinc resistance and accumulation. Plant Physiol 119:1047-1055
    • (1999) Plant Physiol , vol.119 , pp. 1047-1055
    • Van Der Zaal, B.J.1    Neuteboom, L.W.2    Pinas, J.E.3    Chardonnens, A.N.4    Schat, H.5    Verkleij, J.A.6    Hooykaas, P.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.