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Volumn 10, Issue 6, 2000, Pages 365-377

Cloning and sequencing of the genes encoding the periplasmic-cytochrome b-containing selenate reductase of Thauera selenatis

Author keywords

Anaerobic respiration; Chaperone proteins; Iron sulfur proteins; Molybdenum containing enzymes; Soluble cytochrome b

Indexed keywords

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CYTOPLASM; DNA FRAGMENT; ELECTRON TRANSFER; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE PRODUCT; GENE SEQUENCING; MOLECULAR CLONING; MUTAGENESIS; OLIGONUCLEOTIDE; OPEN READING FRAME; OPERON; SELENATE REDUCTASE; TRANSPOSON;

EID: 0034064383     PISSN: 19401736     EISSN: 19401744     Source Type: Journal    
DOI: 10.3109/10425170009015604     Document Type: Article
Times cited : (82)

References (53)
  • 1
    • 0021912130 scopus 로고
    • Construction of broad-host-range cosmid cloning vectors: Identification of genes necessary for growth of Methylobacterium organophilum on methanol
    • Allen L. N. and Hanson R. S. (1985). Construction of broad-host-range cosmid cloning vectors: Identification of genes necessary for growth of Methylobacterium organophilumon methanol. J. Bacteriol. 161, 955-962. (Pubitemid 15137385)
    • (1985) Journal of Bacteriology , vol.161 , Issue.3 , pp. 955-962
    • Allen, L.N.1    Hanson, R.S.2
  • 3
    • 0025788382 scopus 로고
    • Nitrate-inducible formate dehydrogenase in Escherichia coli K-12: 1. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine
    • Berg B. L., Li J., Heider J. and Stewart V. (1991). Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine. J. Biol. Chetn. 266, 22380-22385. (Pubitemid 21908664)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.33 , pp. 22380-22385
    • Berg, B.L.1    Li, J.2    Heider, J.3    Stewart, V.4
  • 4
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks B. C., Ferguson S. J., Moir J. W. B. and Richardson D. J. (1995). Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232, 97-173.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 5
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks B. C. (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
  • 6
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • Bilous P. T., Cole S. T., Anderson W. F. and Weiner J. H. (1988). Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2, 785-795.
    • (1988) Mol. Microbiol. , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 7
    • 0024713468 scopus 로고
    • Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the a and b subunits in iron binding and electron transfer
    • Blasco F., Iobbi C., Giordano G, Chippaux M. and Bonnefoy V. (1989). Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the a and b subunits in iron binding and electron transfer. Mol. Gen. Genet. 218, 249-256.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 249-256
    • Blasco, F.1    Iobbi, C.2    Giordano, G.3    Chippaux, M.4    Bonnefoy, V.5
  • 8
    • 0025368948 scopus 로고
    • Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon
    • Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V. and Chippaux M. (1990). Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. Mol. Gen. Genet. 222, 104-111. (Pubitemid 20219866)
    • (1990) Molecular and General Genetics , vol.222 , Issue.1 , pp. 104-111
    • Blasco, F.1    Iobbi, C.2    Ratouchniak, J.3    Bonnefoy, V.4    Chippaux, M.5
  • 9
    • 0031979433 scopus 로고    scopus 로고
    • NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli
    • DOI 10.1046/j.1365-2958.1998.00795.x
    • Blasco F., Dos Santos J.-P., Magalon A., Frixon C., Guigliarelli B., Santini C.-L. and Giordano G (1998). NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli. Mol. Microbiol. 28, 435-447. (Pubitemid 28218391)
    • (1998) Molecular Microbiology , vol.28 , Issue.3 , pp. 435-447
    • Blasco, F.1    Dos Santos, J.-P.2    Magalon, A.3    Frixon, C.4    Guigliarelli, B.5    Santini, C.-L.6    Giordano, G.7
  • 10
    • 0027519504 scopus 로고
    • Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes
    • Blattner F. R., Burland V., Plunkett III G., Sofia H. J. and Daniels D. L. (1993). Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 21, 5408-5417. (Pubitemid 23348606)
    • (1993) Nucleic Acids Research , vol.21 , Issue.23 , pp. 5408-5417
    • Blattner, F.R.1    Burland, V.2    Plunkett III, G.3    Sofia, H.J.4    Daniels, D.L.5
  • 11
    • 84931997607 scopus 로고
    • Zur Eliminierung von Trubungsfehlern bei der Eiweissbestimmung mit der Biuretmethode
    • Bode C., Goebell H. and Stahler E. (1968). Zur Eliminierung von Trubungsfehlern bei der Eiweissbestimmung mit der Biuretmethode. Z. Klin. Chem. Klin. Biochem. 6, 418-422.
    • (1968) Z. Klin. Chem. Klin. Biochem. , vol.6 , pp. 418-422
    • Bode, C.1    Goebell, H.2    Stahler, E.3
  • 12
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • DOI 10.1074/jbc.273.29.18003
    • Bogsch E. G., Sargent F., Stanley N. R., Berks B. C., Robinson C. and Palmer T. (1998). An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273, 18003-18006. (Pubitemid 28334711)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.29 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 13
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm R., Sauter M. and Böck A. (1990). Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. A, 231-243.
    • (1990) Mol. Microbiol. A , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 14
    • 0025912548 scopus 로고
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
    • Bokranz M., Gutmann M., Körtner C., Kojro E., Fahrenholz F., Lauterbach F. and Kröger A. (1991). Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. Arch. Microbiol. 156, 119-128.
    • (1991) Arch. Microbiol. , vol.156 , pp. 119-128
    • Bokranz, M.1    Gutmann, M.2    Körtner, C.3    Kojro, E.4    Fahrenholz, F.5    Lauterbach, F.6    Kröger, A.7
  • 15
    • 0017584161 scopus 로고
    • Construction and characterization of new cloning vehicles. II. A multipurpose cloning system
    • Bolivar F., Rodriguez R. L., Greene P. J., Betlach M. C., Heyneker H. L., Boyer H. W., Crosa J. H. and Falkow S. (1977). Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene 2, 95-113. (Pubitemid 9021046)
    • (1977) Gene , vol.2 , Issue.2 , pp. 95-113
    • Bolivar, F.1    Rodriguez, R.L.2    Greene, P.J.3
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the b subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest and lowest potential [4Fe-4S] clusters
    • Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G. and Blasco F. (1996). Complete coordination of the four Fe-S centers of the b subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest and lowest potential [4Fe-4S] clusters. Biochemistry 35, 4828-4836.
    • (1996) Biochemistry , vol.35 , pp. 4828-4836
    • Guigliarelli, B.1    Magalon, A.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Blasco, F.7
  • 20
    • 0030036323 scopus 로고    scopus 로고
    • Dimethylsulfide: Acceptor oxidoreductase from Rhodobacter sulfidophilus - The purified enzyme contains b-type haem and a pterin molybdenum cofactor
    • Hanlon S. P., Toh T.-H., Solomon P. S., Holt R. A. and McEwan A. G. (1996). Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor. Eur. J. Biochem. 239, 391-396. (Pubitemid 26246545)
    • (1996) European Journal of Biochemistry , vol.239 , Issue.2 , pp. 391-396
    • Hanlon, S.P.1    Toh, T.-H.2    Solomon, P.S.3    Holt, R.A.4    McEwan, A.G.5
  • 21
    • 0029078973 scopus 로고
    • Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism
    • Heinzinger N. K., Fujimoto S. Y., Clark M. A., Moreno M. S. and Barrett E. L. (1995). Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism. J. Bacteriol. 177, 2813-2820.
    • (1995) J. Bacteriol. , vol.177 , pp. 2813-2820
    • Heinzinger, N.K.1    Fujimoto, S.Y.2    Clark, M.A.3    Moreno, M.S.4    Barrett, E.L.5
  • 22
    • 0029153686 scopus 로고
    • The anaerobic life of Bacillus subtilis: Cloning of the genes encoding the respiratory nitrate reductase system
    • Hoffmann T., Troup B., Szabo A., Hungerer C. and Jahn D. (1995). The anaerobic life of Bacillus subtilis: Cloning of the genes encoding the respiratory nitrate reductase system. FEMS Microbiol. Lett. 131, 219-225.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 219-225
    • Hoffmann, T.1    Troup, B.2    Szabo, A.3    Hungerer, C.4    Jahn, D.5
  • 23
    • 0016667182 scopus 로고
    • A simple method for the preparation of large quantities of pure plasmid DNA
    • Humphreys GO., Willshaw G. A. and Anderson E. S. (1975). A simple method for the preparation of large quantities of pure plasmid DNA. Biochim. Biophys. Acta 383, 457-463.
    • (1975) Biochim. Biophys. Acta , vol.383 , pp. 457-463
    • Humphreys, G.O.1    Willshaw, G.A.2    Anderson, E.S.3
  • 24
    • 0028290650 scopus 로고
    • A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria
    • DOI 10.1111/j.1365-2958.1994.tb01004.x
    • Hussain H., Grove J., Griffiths L., Busby S. and Cole J. (1994). A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. Mol. Microbiol. 12, 153-163. (Pubitemid 24197453)
    • (1994) Molecular Microbiology , vol.12 , Issue.1 , pp. 153-163
    • Hussain, H.1    Grove, J.2    Griffiths, L.3    Busby, S.4    Cole, J.5
  • 25
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard J. W. and Kendall D. A. (1994). Signal peptides: Exquisitely designed transport promoters. Mol. Microbiol. 13, 765-773. (Pubitemid 24272197)
    • (1994) Molecular Microbiology , vol.13 , Issue.5 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 26
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • DOI 10.1146/annurev.biochem.66.1.233
    • Kisker C., Schindelin H. and Rees D. C. (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
  • 27
  • 28
    • 0030760622 scopus 로고    scopus 로고
    • Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli
    • DOI 10.1074/jbc.272.39.24266
    • Liu X. and DeMoss J. A. (1997). Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli. J. Biol. Chem. 272, 24266-24271. (Pubitemid 27418628)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.39 , pp. 24266-24271
    • Liu, X.1    DeMoss, J.A.2
  • 29
    • 0024742507 scopus 로고
    • Selenate reduction by a Pseudomonas species: A new mode of anaerobic respiration
    • Macy J. M., Michel T. A. and Kirsch D. G. (1989). Selenate reduction by a Pseudomonas species: A new mode of anaerobic respiration. FEMS Microbiol. Lett. 61, 195-198.
    • (1989) FEMS Microbiol. Lett. , vol.61 , pp. 195-198
    • Macy, J.M.1    Michel, T.A.2    Kirsch, D.G.3
  • 30
    • 0027408903 scopus 로고
    • Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration
    • Macy J. M., Rech S., Auling G., Dorsch M., Stackebrandt E. and Sly L. I. (1993). Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration. Int. J. Syst. Bacteriol. 43, 135-142. (Pubitemid 23023162)
    • (1993) International Journal of Systematic Bacteriology , vol.43 , Issue.1 , pp. 135-142
    • Macy, J.M.1    Rech, S.2    Auling, G.3    Dorsch, M.4    Stackebrandt, E.5    Sly, L.I.6
  • 31
    • 0030845184 scopus 로고    scopus 로고
    • Heme axial ligation by the highly conserved his residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A (NarGHI)
    • DOI 10.1074/jbc.272.41.25652
    • Magalon A., Lemesle-Meunier D., Rothery R. A., Frixon C., Weiner J. H. and Blasco F. (1997). Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (Narl) of Escherichia coli nitrate reductase A (NarGHI). J. Biol. Chem. 272, 25652-25658. (Pubitemid 27438881)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25652-25658
    • Magalon, A.1    Lemesle-Meunier, D.2    Rothery, R.A.3    Frixon, C.4    Weiner, J.H.5    Blasco, F.6
  • 32
    • 0028198987 scopus 로고
    • TMAO anaerobic respiration in Escherichia coli: Involvement of the tor operon
    • DOI 10.1111/j.1365-2958.1994.tb00393.x
    • Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M. and Pascal M. C. (1994). TMAO anaerobic respiration in Escherichia coli: Involvement of the tor operon. Mol. Microbiol. 11, 1169-1179. (Pubitemid 24201632)
    • (1994) Molecular Microbiology , vol.11 , Issue.6 , pp. 1169-1179
    • Mejean, V.1    Lobbi-Nivol, C.2    Lepelletier, M.3    Giordano, G.4    Chippaux, M.5    Pascal, M.-C.6
  • 33
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Miller J. H. (1972). Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1972) Experiments in Molecular genetics.
    • Miller, J.H.1
  • 34
    • 0000489370 scopus 로고
    • Selenate reduction to elemental selenium by anaerobic bacteria in sediments and culture: Biogeochemical significance of a novel, sulfate-independent respiration
    • Oremland R. S., Hollibaugh J. T., Maest A. S., Presser T. S., Miller L. G. and Culbertson C. W. (1989). Selenate reduction to elemental selenium by anaerobic bacteria in sediments and culture: Biogeochemical significance of a novel, sulfate-independent respiration. Appl. Environ. Microbiol. 55, 2333-2343.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2333-2343
    • Oremland, R.S.1    Hollibaugh, J.T.2    Maest, A.S.3    Presser, T.S.4    Miller, L.G.5    Culbertson, C.W.6
  • 36
    • 0025304436 scopus 로고
    • Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli
    • Pierson D. E. and Campbell A. (1990). Cloning and nucleotide sequence of bisC., the structural gene for biotin sulfoxide reductase in Escherichia coli. J. Bacteriol. 172, 2194-2198. (Pubitemid 20112050)
    • (1990) Journal of Bacteriology , vol.172 , Issue.4 , pp. 2194-2198
    • Pierson, D.E.1    Campbell, A.2
  • 37
    • 0027219606 scopus 로고
    • Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
    • Plunkett III G., Burland V., Daniels D. L. and Blattner F. R. (1993). Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 21, 3391-3398. (Pubitemid 23241470)
    • (1993) Nucleic Acids Research , vol.21 , Issue.15 , pp. 3391-3398
    • Plunkett III, G.1    Burland, V.2    Daniels, D.L.3    Blattner, F.R.4
  • 38
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A. P. (1993). The complete general secretory pathway of gram-negative bacteria. Microbiol. Rev. 57, 50-108. (Pubitemid 23078438)
    • (1993) Microbiological Reviews , vol.57 , Issue.1 , pp. 50-108
    • Pugsley, A.P.1
  • 39
    • 0026526443 scopus 로고
    • The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes
    • Rech S. A. and Macy J. M. (1992). The terminal reductases for selenate and nitrate respiration in Thauera selenatis are two distinct enzymes. J. Bacteriol. 174, 7316-7320.
    • (1992) J. Bacteriol. , vol.174 , pp. 7316-7320
    • Rech, S.A.1    Macy, J.M.2
  • 42
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • DOI 10.1093/emboj/17.1.101
    • Santini C.-L., Ize B., Chanal A., Miiller M., Giordano G. and Wu L.-F. (1998). A novel Sec-independent periplasmic translocation pathway in Escherichia coli. EMBO J. 17, 101-112. (Pubitemid 28041052)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 101-112
    • Santini, C.-L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.-F.6
  • 43
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • DOI 10.1093/emboj/17.13.3640
    • Sargent F., Bogsch E. G., Stanley N. R., Wexler M., Robinson C., Berks B. C. and Palmer T. (1998). Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17, 3640-3650. (Pubitemid 28327382)
    • (1998) EMBO Journal , vol.17 , Issue.13 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 44
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin H., Kisker C., Hilton J., Rajagopalan K. V. and Rees D. C. (1996). Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination. Science 272, 1615-1621. (Pubitemid 26200018)
    • (1996) Science , vol.272 , Issue.5268 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 45
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution
    • DOI 10.1006/jmbi.1996.0555
    • Schneider F., Löwe J., Huber R., Schindelin H., Kisker C. and Knäblein J. (1996). Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. J. Mol. Biol. 263, 53-69. (Pubitemid 26361512)
    • (1996) Journal of Molecular Biology , vol.263 , Issue.1 , pp. 53-69
    • Schneider, F.1    Lowe, J.2    Huber, R.3    Schindelin, H.4    Kisker, C.5    Knablein, J.6
  • 46
    • 0242696464 scopus 로고    scopus 로고
    • Purification and characterization of the selenate reductase from Thauera selenatis
    • DOI 10.1074/jbc.272.38.23765
    • Schröder I., Rech S., Krafft T. and Macy J. M. (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
  • 47
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon R., Priefer U. and Pühler A. (1983). A broad host range mobilization system for in vitro genetic engineering: Transposon mutagenesis in gram negative bacteria. Bio/technology 1:784-791. (Pubitemid 14239484)
    • (1983) Bio/Technology , vol.1 , Issue.9 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 48
    • 0023988313 scopus 로고
    • Narl region of the Escherichia coli nitrate reductase (nar) operon contains two genes
    • Sodergren E. J. and DeMoss J. A. (1988). narl region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J. Bacteriol. 170, 1721-1729.
    • (1988) J. Bacteriol. , vol.170 , pp. 1721-1729
    • Sodergren, E.J.1    DeMoss, J.A.2
  • 49
    • 0029912192 scopus 로고    scopus 로고
    • Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase
    • DOI 10.1074/jbc.271.9.4620
    • Trieber C. A., Rothery R. A. and Weiner J. H. (1996). Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase. J. Biol. Chem. 271, 4620-4626. (Pubitemid 26074939)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.9 , pp. 4620-4626
    • Triebert, C.A.1    Rothery, R.A.2    Weiner, J.H.3
  • 51
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • DOI 10.1016/S0092-8674(00)81149-6
    • Weiner J. H., Bilous P. T., Shaw G. M., Lubitz S. P., Frost L., Thomas G. H., Cole J. A. and Turner R. J. (1998). A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93, 93-101. (Pubitemid 28173555)
    • (1998) Cell , vol.93 , Issue.1 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5    Thomas, G.H.6    Cole, J.A.7    Turner, R.J.8
  • 52
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • DOI 10.1016/0378-1119(85)90120-9
    • Yanisch-Perron C., Vieira J. and Messing J. (1985). Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33, 103-119. (Pubitemid 15122816)
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 53
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli
    • Zinoni F., Birkmarm A., Stadtman T. C. and Bock A. (1986). Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 4650-4654. (Pubitemid 16075459)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.13 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Bock, A.4


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