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Volumn 191, Issue 6, 2009, Pages 519-528

A genetic analysis of in vivo selenate reduction by Salmonella enterica serovar Typhimurium LT2 and Escherichia coli K12

Author keywords

Bacterial respiration; Enteric bacteria; Isothermal titration calorimetry; Molecular chaperone; Molybdo enzymes; Mutagenesis; Selenate reductase; Twin arginine translocation pathway

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CARRIER PROTEIN; CHAPERONE; MOLYBDENUM; OXIDOREDUCTASE; PROTEIN YNFE; PROTEIN YNFF; SELENATE; SELENATE REDUCTASE; SIGNAL PEPTIDE; TWIN ARGININE TRANSPORT SYSTEM; UNCLASSIFIED DRUG;

EID: 67349267351     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-009-0478-7     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 1842297642 scopus 로고    scopus 로고
    • Tellurite reductase activity of nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite
    • C Avazeri RJ Turner J Pommier JH Weiner G Giordano A Vermeglio 1997 Tellurite reductase activity of nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite Microbiology 143 1181 1189 (Pubitemid 27207787)
    • (1997) Microbiology , vol.143 , Issue.4 , pp. 1181-1189
    • Avazeri, C.1    Turner, R.J.2    Pommier, J.3    Weiner, J.H.4    Giordano, G.5    Vermeglio, A.6
  • 3
    • 0036956672 scopus 로고    scopus 로고
    • Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli
    • M Bebien J Kirsch V Mejean A Vermeglio 2002 Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli Microbiology 148 3865 3872 (Pubitemid 36097448)
    • (2002) Microbiology , vol.148 , Issue.12 , pp. 3865-3872
    • Bebien, M.1    Kirsch, J.2    Mejean, V.3    Vermeglio, A.4
  • 4
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • BC Berks 1996 A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22 393 404 (Pubitemid 26373825)
    • (1996) Molecular Microbiology , vol.22 , Issue.3 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • DOI 10.1016/S0065-2911(03)47004-5
    • BC Berks T Palmer F Sargent 2003 The Tat protein translocation pathway and its role in microbial physiology Adv Microb Physiol 47 187 254 (Pubitemid 37214151)
    • (2003) Advances in Microbial Physiology , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 7
    • 0023479171 scopus 로고
    • Involvement of the ntrA gene product in the anaerobic metabolism of Escherichia coli
    • A Birkmann RG Sawers A Böck 1987 Involvement of the ntrA gene product in the anaerobic metabolism of Escherichia coli Mol Gen Genet 210 535 542
    • (1987) Mol Gen Genet , vol.210 , pp. 535-542
    • Birkmann, A.1    Sawers, R.G.2    Böck, A.3
  • 8
    • 56649102164 scopus 로고    scopus 로고
    • Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone
    • G Buchanan J Maillard SB Nabuurs DJ Richardson T Palmer F Sargent 2008 Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone FEBS Lett 582 3979 3984
    • (2008) FEBS Lett , vol.582 , pp. 3979-3984
    • Buchanan, G.1    Maillard, J.2    Nabuurs, S.B.3    Richardson, D.J.4    Palmer, T.5    Sargent, F.6
  • 10
    • 40149097624 scopus 로고    scopus 로고
    • Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis
    • CS Chan 2008 Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis Biochemistry 47 2749 2759
    • (2008) Biochemistry , vol.47 , pp. 2749-2759
    • Chan, C.S.1
  • 11
    • 64049092491 scopus 로고    scopus 로고
    • Differential interactions between Tat-specific redox enzyme peptides and their chaperones
    • CS Chan L Chang KL Rommens RJ Turner 2009 Differential interactions between Tat-specific redox enzyme peptides and their chaperones J Bacteriol 191 2091 2101
    • (2009) J Bacteriol , vol.191 , pp. 2091-2101
    • Chan, C.S.1    Chang, L.2    Rommens, K.L.3    Turner, R.J.4
  • 15
    • 1642575113 scopus 로고    scopus 로고
    • Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli
    • DOI 10.1016/j.bbamem.2003.10.016
    • P Geijer JH Weiner 2004 Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli Biochim Biophys Acta 1660 66 74 (Pubitemid 38125232)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1660 , Issue.1-2 , pp. 66-74
    • Geijer, P.1    Weiner, J.H.2
  • 16
    • 33846464982 scopus 로고    scopus 로고
    • X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase
    • GN George CJ Doonan RA Rothery N Boroumand JH Weiner 2007 X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase Inorg Chem 46 2 4
    • (2007) Inorg Chem , vol.46 , pp. 2-4
    • George, G.N.1    Doonan, C.J.2    Rothery, R.A.3    Boroumand, N.4    Weiner, J.H.5
  • 17
    • 0016274491 scopus 로고
    • Detection of selenium deposits in Escherichia coli by electron microscopy
    • TL Gerrard JN Telford HH Williams 1974 Detection of selenium deposits in Escherichia coli by electron microscopy J Bacteriol 119 1057 1060
    • (1974) J Bacteriol , vol.119 , pp. 1057-1060
    • Gerrard, T.L.1    Telford, J.N.2    Williams, H.H.3
  • 18
    • 0028225059 scopus 로고
    • Oxidation of dimethylselenide to dimethylselenoxide by microsomes from rat liver and lung and by flavin-containing monooxygenase from pig liver
    • DOI 10.1006/abbi.1994.1191
    • DE Goeger HE Ganther 1994 Oxidation of dimethylselenide to dimethylselenoxide by microsomes from rat liver and lung and by flavin-containing monooxygenase from pig liver Arch Biochem Biophys 310 448 451 (Pubitemid 24172691)
    • (1994) Archives of Biochemistry and Biophysics , vol.310 , Issue.2 , pp. 448-451
    • Goeger, D.E.1    Ganther, H.E.2
  • 20
  • 21
    • 1642370336 scopus 로고    scopus 로고
    • Architecture of NarGH Reveals a Structural Classification of Mo-bisMGD Enzymes
    • DOI 10.1016/j.str.2003.11.020
    • M Jormakka D Richardson B Byrne S Iwata 2004 Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes Structure 12 95 104 (Pubitemid 38114809)
    • (2004) Structure , vol.12 , Issue.1 , pp. 95-104
    • Jormakka, M.1    Richardson, D.2    Byrne, B.3    Iwata, S.4
  • 22
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • DOI 10.1146/annurev.biochem.66.1.233
    • C Kisker H Schindelin DC Rees 1997 Molybdenum-cofactor-containing enzymes: structure and mechanism Annu Rev Biochem 66 233 267 (Pubitemid 27274657)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 23
    • 0029900624 scopus 로고    scopus 로고
    • Tungsten in biological systems
    • DOI 10.1016/0168-6445(95)00025-9
    • A Kletzin MW Adams 1996 Tungsten in biological systems FEMS Microbiol Rev 18 5 63 (Pubitemid 26163588)
    • (1996) FEMS Microbiology Reviews , vol.18 , Issue.1 , pp. 5-63
    • Kietzin, A.1    Adams, M.W.W.2
  • 24
    • 0034064383 scopus 로고    scopus 로고
    • Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis
    • T Krafft A Bowen F Theis JM Macy 2000 Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis DNA Seq 10 365 377 (Pubitemid 30308253)
    • (2000) DNA Sequence - Journal of DNA Sequencing and Mapping , vol.10 , Issue.6 , pp. 365-377
    • Krafft, T.1    Bowen, A.2    Theis, F.3    Macy, J.M.4
  • 26
    • 0031038898 scopus 로고    scopus 로고
    • A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: Isolation and identification of the Escherichia coli ubiE gene
    • PT Lee AY Hsu HT Ha CF Clarke 1997 A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene J Bacteriol 179 1748 1754 (Pubitemid 27100466)
    • (1997) Journal of Bacteriology , vol.179 , Issue.5 , pp. 1748-1754
    • Lee, P.T.1    Hsu, A.Y.2    Ha, H.T.3    Clarke, C.F.4
  • 27
    • 0141651638 scopus 로고    scopus 로고
    • The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC)
    • DOI 10.1016/j.abb.2003.08.008
    • SP Lubitz JH Weiner 2003 The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC) Arch Biochem Biophys 418 205 216 (Pubitemid 37159387)
    • (2003) Archives of Biochemistry and Biophysics , vol.418 , Issue.2 , pp. 205-216
    • Lubitz, S.P.1    Weiner, J.H.2
  • 28
    • 36249031611 scopus 로고    scopus 로고
    • Chemical kinetic and molecular genetic study of selenium oxyanion reduction by Enterobacter cloacae SLD1a-1
    • DOI 10.1021/es0712672
    • J Ma DY Kobayashi N Yee 2007 Chemical kinetic and molecular genetic study of selenium oxyanion reduction by Enterobacter cloacae SLD1a-1 Environ Sci Technol 41 7795 7801 (Pubitemid 350133320)
    • (2007) Environmental Science and Technology , vol.41 , Issue.22 , pp. 7795-7801
    • Ma, J.1    Kobayashi, D.Y.2    Yee, N.3
  • 29
    • 58149216603 scopus 로고    scopus 로고
    • Role of menaquinone biosynthesis genes in selenate reduction by Enterobacter cloacae SLD1a-1 and Escherichia coli K12
    • J Ma DY Kobayashi N Yee 2009 Role of menaquinone biosynthesis genes in selenate reduction by Enterobacter cloacae SLD1a-1 and Escherichia coli K12 Environ Microbiol 11 149 158
    • (2009) Environ Microbiol , vol.11 , pp. 149-158
    • Ma, J.1    Kobayashi, D.Y.2    Yee, N.3
  • 32
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • DOI 10.1046/j.1365-2958.2001.02391.x
    • IJ Oresnik CL Ladner RJ Turner 2001 Identification of a twin-arginine leader-binding protein Mol Microbiol 40 323 331 (Pubitemid 32391628)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 33
    • 41149137584 scopus 로고    scopus 로고
    • The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway
    • Y Qiu R Zhang TA Binkowski V Tereshko A Joachimiak A Kossiakoff 2008 The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway Proteins 71 525 533
    • (2008) Proteins , vol.71 , pp. 525-533
    • Qiu, Y.1    Zhang, R.2    Binkowski, T.A.3    Tereshko, V.4    Joachimiak, A.5    Kossiakoff, A.6
  • 34
    • 0029668203 scopus 로고    scopus 로고
    • Gas-phase reactions of dimethyl selenide with ozone and the hydroxyl and nitrate radicals
    • DOI 10.1016/1352-2310(95)00447-5
    • RM Rael EC Tuazon WT Frankenberger 1996 Gas-phase reactions of dimethyl selenide with ozone and the hydroxyl and nitrate radicals Atmospheric Environ 30 1221 1232 (Pubitemid 26082873)
    • (1996) Atmospheric Environment , vol.30 , Issue.8 , pp. 1221-1232
    • Rael, R.M.1    Tuazon, E.C.2    Frankenberger Jr., W.T.3
  • 35
    • 0037448423 scopus 로고    scopus 로고
    • DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
    • DOI 10.1016/S0014-5793(02)03839-5
    • N Ray J Oates RJ Turner C Robinson 2003 DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus FEBS Lett 534 156 160 (Pubitemid 36084534)
    • (2003) FEBS Letters , vol.534 , Issue.1-3 , pp. 156-160
    • Ray, N.1    Oates, J.2    Turner, R.J.3    Robinson, C.4
  • 36
    • 33747372448 scopus 로고    scopus 로고
    • Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions
    • DOI 10.1128/AEM.00568-06
    • H Ridley CA Watts DJ Richardson CS Butler 2006 Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions Appl Environ Microbiol 72 5173 5180 (Pubitemid 44242366)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.8 , pp. 5173-5180
    • Ridley, H.1    Watts, C.A.2    Richardson, D.J.3    Butler, C.S.4
  • 37
    • 0026075272 scopus 로고
    • Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
    • D Sambasivarao JH Weiner 1991 Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation J Bacteriol 173 5935 5943
    • (1991) J Bacteriol , vol.173 , pp. 5935-5943
    • Sambasivarao, D.1    Weiner, J.H.2
  • 38
    • 33947370894 scopus 로고    scopus 로고
    • Constructing the wonders of the bacterial world: Biosynthesis of complex enzymes
    • DOI 10.1099/mic.0.2006/004762-0
    • F Sargent 2007 Constructing the wonders of the bacterial world: biosynthesis of complex enzymes Microbiology 153 633 651 (Pubitemid 46444361)
    • (2007) Microbiology , vol.153 , Issue.3 , pp. 633-651
    • Sargent, F.1
  • 39
    • 0242696464 scopus 로고    scopus 로고
    • Purification and characterization of the selenate reductase from Thauera selenatis
    • DOI 10.1074/jbc.272.38.23765
    • I Schröder S Rech T Krafft JM Macy 1997 Purification and characterization of the selenate reductase from Thauera selenatis J Biol Chem 272 23765 23768 (Pubitemid 27410953)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.38 , pp. 23765-23768
    • Schroder, I.1    Rech, S.2    Krafft, T.3    Macy, J.M.4
  • 41
    • 0031596770 scopus 로고    scopus 로고
    • 2) biosynthesis: Localization and characterization of the menA gene from Escherichia coli
    • K Suvarna D Stevenson R Meganathan ME Hudspeth 1998 Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli J Bacteriol 180 2782 2787 (Pubitemid 28213284)
    • (1998) Journal of Bacteriology , vol.180 , Issue.10 , pp. 2782-2787
    • Suvarna, K.1    Stevenson, D.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 42
    • 29144459865 scopus 로고    scopus 로고
    • Identification of biogenic dimethyl selenodisulfide in the headspace gases above genetically modified Escherichia coli
    • DOI 10.1016/j.ab.2005.10.007, PII S0003269705007256
    • JW Swearingen Jr DP Frankel DE Fuentes CP Saavedra CC Vasquez TG Chasteen 2006 Identification of biogenic dimethyl selenodisulfide in the headspace gases above genetically modified Escherichia coli Anal Biochem 348 115 122 (Pubitemid 41796464)
    • (2006) Analytical Biochemistry , vol.348 , Issue.1 , pp. 115-122
    • Swearingen Jr., J.W.1    Frankel, D.P.2    Fuentes, D.E.3    Saavedra, C.P.4    Vasquez, C.C.5    Chasteen, T.G.6
  • 43
    • 33644862744 scopus 로고    scopus 로고
    • Expression of the ubiE gene of Geobacillus stearothermophilus v in Escherichia coli K-12 mediates the evolution of selenium compounds into the headspace of selenite- and selenate-amended cultures
    • JW Swearingen Jr 2006 Expression of the ubiE gene of Geobacillus stearothermophilus V in Escherichia coli K-12 mediates the evolution of selenium compounds into the headspace of selenite- and selenate-amended cultures Appl Environ Microbiol 72 963 967
    • (2006) Appl Environ Microbiol , vol.72 , pp. 963-967
    • Swearingen Jr, J.W.1
  • 44
    • 0029861620 scopus 로고    scopus 로고
    • Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase
    • DOI 10.1074/jbc.271.44.27339
    • CA Trieber RA Rothery JH Weiner 1996 Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase J Biol Chem 271 27339 27345 (Pubitemid 26367288)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27339-27345
    • Trieber, C.A.1    Rothery, R.A.2    Weiner, J.H.3
  • 46
    • 0031735176 scopus 로고    scopus 로고
    • Selenium metabolism in Escherichia coli
    • DOI 10.1023/A:1009290213301
    • RJ Turner JH Weiner DE Taylor 1998 Selenium metabolism in Escherichia coli Biometals 11 223 227 (Pubitemid 28528732)
    • (1998) BioMetals , vol.11 , Issue.3 , pp. 223-227
    • Turner, R.J.1    Weiner, J.H.2    Taylor, D.E.3
  • 47
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • DOI 10.1139/w03-117
    • RJ Turner AL Papish F Sargent 2004 Sequence analysis of bacterial redox enzyme maturation proteins (REMPs) Can J Microbiol 50 225 238 (Pubitemid 38903410)
    • (2004) Canadian Journal of Microbiology , vol.50 , Issue.4 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 48
    • 0344585331 scopus 로고    scopus 로고
    • Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase
    • DOI 10.1016/S0378-1097(03)00782-1
    • CA Watts H Ridley KL Condie JT Leaver DJ Richardson CS Butler 2003 Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase FEMS Microbiol Lett 228 273 279 (Pubitemid 37456854)
    • (2003) FEMS Microbiology Letters , vol.228 , Issue.2 , pp. 273-279
    • Watts, C.A.1    Ridley, H.2    Condie, K.L.3    Leaver, J.T.4    Richardson, D.J.5    Butler, C.S.6
  • 50
    • 0027165748 scopus 로고
    • Mutants of Escherichia coli affected in respiration: The cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate: octaprenyltransferase
    • G Wu HD Williams F Gibson RK Poole 1993 Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase J Gen Microbiol 139 1795 1805 (Pubitemid 23258606)
    • (1993) Journal of General Microbiology , vol.139 , Issue.8 , pp. 1795-1805
    • Wu, G.1    Williams, H.D.2    Gibson, F.3    Poole, R.K.4
  • 51
    • 33947434064 scopus 로고    scopus 로고
    • Se(VI) reduction and the precipitation of Se(0) by the facultative bacterium Enterobacter cloacae SLD1a-1 are regulated by FNR
    • DOI 10.1128/AEM.02542-06
    • N Yee J Ma A Dalia T Boonfueng DY Kobayashi 2007 Se(VI) reduction and the precipitation of Se(0) by the facultative bacterium Enterobacter cloacae SLD1a-1 are regulated by FNR Appl Environ Microbiol 73 1914 1920 (Pubitemid 46449075)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.6 , pp. 1914-1920
    • Yee, N.1    Ma, J.2    Dalia, A.3    Boonfueng, T.4    Kobayashi, D.Y.5


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