메뉴 건너뛰기




Volumn 17, Issue 5, 2006, Pages 303-307

Time-dependent translational response of E. coli to excess Zn(II)

Author keywords

2D gels; Translational response; Zn(II)

Indexed keywords

DIVALENT CATION; ZINC;

EID: 36049005551     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 15744394198 scopus 로고    scopus 로고
    • Bacterial zinc uptake and regulators
    • Hantke K. Bacterial zinc uptake and regulators. Curr Opin Microbiol 2005;8:196-202.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 196-202
    • Hantke, K.1
  • 2
    • 0025060799 scopus 로고
    • 2O of zinc enzymes
    • Vallee BL, Auld DS. Active-site zinc ligands and activated H2O of zinc enzymes. Proc Natl Acad Sci USA 1990;87:220-224.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 220-224
    • Vallee, B.L.1    Auld, D.S.2
  • 3
    • 0025303335 scopus 로고
    • 2O of zinc enzymes
    • Vallee BL, Auld DS. Zinc coordination, function, and structure of zinc enzymes and other proteins. Active-site zinc ligands and activated H2O of zinc enzymes. Biochemistry 1990;29:5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 4
    • 0033828371 scopus 로고    scopus 로고
    • Metal-ion tolerance in Escherichia coli: Analysis of transcriptional profiles by gene-array technology
    • Brocklehurst KR, Morby AP. Metal-ion tolerance in Escherichia coli: Analysis of transcriptional profiles by gene-array technology. Microbiology 2000;146:2277-2282.
    • (2000) Microbiology , vol.146 , pp. 2277-2282
    • Brocklehurst, K.R.1    Morby, A.P.2
  • 5
    • 13244271944 scopus 로고    scopus 로고
    • Genome-wide transcriptional response of chemostat-cultured Escherichia coli to zinc
    • Lee LJ, Barrett JA, Poole RK. Genome-wide transcriptional response of chemostat-cultured Escherichia coli to zinc. J Bacteriol 2005;187:1124-1134.
    • (2005) J Bacteriol , vol.187 , pp. 1124-1134
    • Lee, L.J.1    Barrett, J.A.2    Poole, R.K.3
  • 6
    • 24944583149 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external zinc
    • Yamamoto K, Ishihama A. Transcriptional response of Escherichia coli to external zinc. J Bacteriol 2005;187:6333-6340.
    • (2005) J Bacteriol , vol.187 , pp. 6333-6340
    • Yamamoto, K.1    Ishihama, A.2
  • 8
    • 16544376249 scopus 로고    scopus 로고
    • Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies
    • Sigdel TK, Cilliers R, Gursahaney PR, Crowder MW. Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies. J Biomol Tech 2004;15:199-207.
    • (2004) J Biomol Tech , vol.15 , pp. 199-207
    • Sigdel, T.K.1    Cilliers, R.2    Gursahaney, P.R.3    Crowder, M.W.4
  • 10
    • 0022550466 scopus 로고
    • The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes
    • Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, et al. The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem J 1986;234:593-604.
    • (1986) Biochem J , vol.234 , pp. 593-604
    • Fotheringham, I.G.1    Dacey, S.A.2    Taylor, P.P.3    Smith, T.J.4    Hunter, M.G.5    Finlay, M.E.6
  • 12
    • 0036062240 scopus 로고    scopus 로고
    • PH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli
    • Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, et al. pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli. J Bacteriol 2002;184:4246-4258.
    • (2002) J Bacteriol , vol.184 , pp. 4246-4258
    • Stancik, L.M.1    Stancik, D.M.2    Schmidt, B.3    Barnhart, D.M.4    Yoncheva, Y.N.5
  • 13
    • 8544261105 scopus 로고    scopus 로고
    • Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli
    • Morita T, Kawamoto H, Mizota T, Inada T, Aiba H. Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol Microbiol 2004;54:1063-1075.
    • (2004) Mol Microbiol , vol.54 , pp. 1063-1075
    • Morita, T.1    Kawamoto, H.2    Mizota, T.3    Inada, T.4    Aiba, H.5
  • 14
    • 0034614424 scopus 로고    scopus 로고
    • Serine acetyltransferase from Escherichia coli is a dimer of trimers
    • Hindson VJ, Moody PCE, Rowe AJ, Shaw WV. Serine acetyltransferase from Escherichia coli is a dimer of trimers. J Biol Chem 2000;275:461-466.
    • (2000) J Biol Chem , vol.275 , pp. 461-466
    • Hindson, V.J.1    Moody, P.C.E.2    Rowe, A.J.3    Shaw, W.V.4
  • 15
    • 0026483711 scopus 로고
    • Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
    • Gragerov A, Nudler E, Komissarova N, Gaitanaris G, Gottesman M, Nikiforov V. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci USA 1992;89:10341-10344.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10341-10344
    • Gragerov, A.1    Nudler, E.2    Komissarova, N.3    Gaitanaris, G.4    Gottesman, M.5    Nikiforov, V.6
  • 18
    • 0025736565 scopus 로고
    • Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence
    • Forchhammer K, Bock A. Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence. J Biol Chem 1991;266:6324-6328.
    • (1991) J Biol Chem , vol.266 , pp. 6324-6328
    • Forchhammer, K.1    Bock, A.2
  • 19
    • 0019781166 scopus 로고
    • Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits
    • Fultz PN, Kemper J. Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits. J Bacteriol 1981;148:210-219.
    • (1981) J Bacteriol , vol.148 , pp. 210-219
    • Fultz, P.N.1    Kemper, J.2
  • 20
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998;92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 22
    • 0023567202 scopus 로고
    • Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase
    • Vogel RF, Entian KD, Mecke D. Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase. Arch Microbiol 1987;149:36-42.
    • (1987) Arch Microbiol , vol.149 , pp. 36-42
    • Vogel, R.F.1    Entian, K.D.2    Mecke, D.3
  • 23
    • 0029564145 scopus 로고
    • A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions
    • Wu LF, Mandrand-Berthelot MA. A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions. Biochimie 1995;77:744-750.
    • (1995) Biochimie , vol.77 , pp. 744-750
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 24
    • 0034687819 scopus 로고    scopus 로고
    • Nitrogen regulatory protein C-controlled genes of Escherichia coli: Scavenging as a defense against nitrogen limitation
    • Zimmer DP, Soupene E, Lee HL, Wendisch VF, Khodursky AB, Peter BJ, et al. Nitrogen regulatory protein C-controlled genes of Escherichia coli: Scavenging as a defense against nitrogen limitation. Proc Natl Acad Sci 2000;97:14674-14679.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 14674-14679
    • Zimmer, D.P.1    Soupene, E.2    Lee, H.L.3    Wendisch, V.F.4    Khodursky, A.B.5    Peter, B.J.6
  • 25
    • 0025353846 scopus 로고
    • Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli
    • Adams M, Wagner L, Graddis T, Landick R, Antonucci T, Gibson A, et al. Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli. J Biol Chem 1990;265:11436-11443.
    • (1990) J Biol Chem , vol.265 , pp. 11436-11443
    • Adams, M.1    Wagner, L.2    Graddis, T.3    Landick, R.4    Antonucci, T.5    Gibson, A.6
  • 26
    • 0023038504 scopus 로고
    • Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli
    • Guyer CA, Morgan DG, Staros JV. Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli. J Bacteriol 1986;168:775-779.
    • (1986) J Bacteriol , vol.168 , pp. 775-779
    • Guyer, C.A.1    Morgan, D.G.2    Staros, J.V.3
  • 27
    • 0021347950 scopus 로고
    • Molecular cloning and characterization of genes required for ribose transport and utilization in Escherichia coli K-12
    • Iida A, Harayama S, Iino T, Hazelbauer GL. Molecular cloning and characterization of genes required for ribose transport and utilization in Escherichia coli K-12. J Bacteriol 1984;158:674-682.
    • (1984) J Bacteriol , vol.158 , pp. 674-682
    • Iida, A.1    Harayama, S.2    Iino, T.3    Hazelbauer, G.L.4
  • 28
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten CE, O'Halloran TV. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 2001;292:2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 29
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • Grass G, Franke S, Taudte N, Nies DH, Kucharski LM, Maguire ME, et al. The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J Bacteriol 2005;187:1604-1611.
    • (2005) J Bacteriol , vol.187 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6
  • 30
    • 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. ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli. J Bacteriol 2001;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
  • 31
    • 33748805223 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to TPEN
    • Sigdel TK, Easton JA, Crowder MW. Transcriptional response of Escherichia coli to TPEN. J Bacteriol 2006;188:6709-6713.
    • (2006) J Bacteriol , vol.188 , pp. 6709-6713
    • Sigdel, T.K.1    Easton, J.A.2    Crowder, M.W.3
  • 32
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer SI, Hantke K. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol Microbiol 1998;28:1199-1210.
    • (1998) Mol Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 33
    • 0035896019 scopus 로고    scopus 로고
    • The hydH/G genes from Escherichia coli code for a zinc and lead responsive two-component regulatory system
    • Leonhartsberger S, Huber A, Lottspeich F, Bock A. The hydH/G genes from Escherichia coli code for a zinc and lead responsive two-component regulatory system. J Mol Biol 2001;307:93-105.
    • (2001) J Mol Biol , vol.307 , pp. 93-105
    • Leonhartsberger, S.1    Huber, A.2    Lottspeich, F.3    Bock, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.