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Volumn 126, Issue 1, 1999, Pages 10-18

Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster

Author keywords

Assembly; Escherichia coli; Expression; Ferredoxin; Iron sulfur cluster

Indexed keywords

CYSTEINE; FERREDOXIN; IRON; IRON SULFUR PROTEIN; RECOMBINANT PROTEIN;

EID: 0032868231     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022409     Document Type: Article
Times cited : (178)

References (51)
  • 1
    • 0025360449 scopus 로고
    • Recent developments in the field of iron-sulfur proteins
    • Beinert, H. (1990) Recent developments in the field of iron-sulfur proteins. FASEB J. 4, 2483-2491
    • (1990) FASEB J. , vol.4 , pp. 2483-2491
    • Beinert, H.1
  • 2
    • 77956772373 scopus 로고
    • Structural and functional diversity of ferredoxins and related proteins
    • Cammack, R., ed. Academic Press, San Diego
    • Matsubara, H. and Saeki, K. (1992) Structural and functional diversity of ferredoxins and related proteins in Advances in Inorganic Chemistry: Iron-Sulfur Proteins (Cammack, R., ed.) Vol. 38, pp. 223-280, Academic Press, San Diego
    • (1992) Advances in Inorganic Chemistry: Iron-Sulfur Proteins , vol.38 , pp. 223-280
    • Matsubara, H.1    Saeki, K.2
  • 3
    • 0344834199 scopus 로고
    • Iron-sulphur clusters in enzymes: Themes and variations
    • Cammack, R., ed. Academic Press, San Diego
    • Cammack, R. (1992) Iron-sulphur clusters in enzymes: themes and variations in Advances in Inorganic Chemistry: Iron-Sulfur Proteins (Cammack, R., ed.) Vol. 38, pp. 281-322, Academic Press, San Diego
    • (1992) Advances in Inorganic Chemistry: Iron-Sulfur Proteins , vol.38 , pp. 281-322
    • Cammack, R.1
  • 4
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • Flint, D.H. and Allen, R.M. (1996) Iron-sulfur proteins with nonredox functions. Chem. Rev. 96, 2315-2334
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 5
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R.H., and Münck, E. (1997) Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277, 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 8
    • 0030056113 scopus 로고    scopus 로고
    • Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli
    • Flint, D.H., Tuminello, J.F., and Miller, T.J. (1996) Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli. J. Biol. Chem. 271, 16053-16067
    • (1996) J. Biol. Chem. , vol.271 , pp. 16053-16067
    • Flint, D.H.1    Tuminello, J.F.2    Miller, T.J.3
  • 9
    • 0001158225 scopus 로고
    • Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts
    • Takahashi, Y., Mitsui, A., Hase, T., and Matsubara, H. (1986) Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts. Proc. Natl. Acad. Sci. USA 83, 2434-2437
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2434-2437
    • Takahashi, Y.1    Mitsui, A.2    Hase, T.3    Matsubara, H.4
  • 10
    • 0002949415 scopus 로고
    • Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts
    • Takahashi, Y., Mitsui, A., and Matsubara, H. (1991) Formation of the Fe-S cluster of ferredoxin in lysed spinach chloroplasts. Plant Physiol. 95, 97-103
    • (1991) Plant Physiol. , vol.95 , pp. 97-103
    • Takahashi, Y.1    Mitsui, A.2    Matsubara, H.3
  • 11
    • 0000580463 scopus 로고
    • Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin
    • Takahashi, Y., Mitsui, A., Fujita, Y., and Matsubara, H. (1991) Roles of ATP and NADPH in formation of the Fe-S cluster of spinach ferredoxin. Plant Physiol. 95, 104-110
    • (1991) Plant Physiol. , vol.95 , pp. 104-110
    • Takahashi, Y.1    Mitsui, A.2    Fujita, Y.3    Matsubara, H.4
  • 12
    • 0027494834 scopus 로고
    • Nitrogenase metalloclusters: Structures, organization, and synthesis
    • Dean, D.R., Bolin, J.T., and Zheng, L. (1993) Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 175, 6737-6744
    • (1993) J. Bacteriol. , vol.175 , pp. 6737-6744
    • Dean, D.R.1    Bolin, J.T.2    Zheng, L.3
  • 13
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., White, R.H., Cash, V.L., Jack, R.F., and Dean, D.R. (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90, 2754-2758
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 14
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng, L. and Dean, D.R. (1994) Catalytic formation of a nitrogenase iron-sulfur cluster. J. Biol. Chem. 269, 18723-18726
    • (1994) J. Biol. Chem. , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2
  • 15
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint, D.H. (1996) Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J. Biol. Chem. 271, 16068-16074
    • (1996) J. Biol. Chem. , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 16
    • 0016215747 scopus 로고
    • Role of 3-mercaptopyruvate sulfur-transferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin
    • Taniguchi, T. and Kimura, T. (1974) Role of 3-mercaptopyruvate sulfur-transferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin. Biochim. Biophys. Acta 364, 284-295
    • (1974) Biochim. Biophys. Acta , vol.364 , pp. 284-295
    • Taniguchi, T.1    Kimura, T.2
  • 17
    • 0001633356 scopus 로고
    • Seeking a better job for an under-employed enzyme
    • Cerletti, P. (1986) Seeking a better job for an under-employed enzyme. Trends Biochem. Sci. 11, 369-372
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 369-372
    • Cerletti, P.1
  • 18
    • 0030978491 scopus 로고    scopus 로고
    • A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin
    • Leibrecht, I. and Kessler, D. (1997) A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation of Synechocystis ferredoxin. J. Biol. Chem. 272, 10442-10447
    • (1997) J. Biol. Chem. , vol.272 , pp. 10442-10447
    • Leibrecht, I.1    Kessler, D.2
  • 19
    • 0344366698 scopus 로고
    • Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli
    • Coghlan, V.M. and Vickery, L.E. (1989) Expression of human ferredoxin and assembly of the [2Fe-2S] center in Escherichia coli. Proc. Natl. Acad. Sci. USA 86, 835-839
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 835-839
    • Coghlan, V.M.1    Vickery, L.E.2
  • 20
    • 0001454446 scopus 로고
    • Expression of maize ferredoxin cDNA in Escherichia coli
    • Hase, T., Mizutani, S., and Mukohata, Y. (1991) Expression of maize ferredoxin cDNA in Escherichia coli. Plant Physiol. 97, 1395-1401
    • (1991) Plant Physiol. , vol.97 , pp. 1395-1401
    • Hase, T.1    Mizutani, S.2    Mukohata, Y.3
  • 21
    • 0027952573 scopus 로고
    • Characterization of the genome region encoding an FdxH-type ferredoxin and a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing cyanobacterium Plectonema boryanum PCC 73110
    • Schrautemeier, B., Cassing, A., and Böhme, H. (1994) Characterization of the genome region encoding an FdxH-type ferredoxin and a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing cyanobacterium Plectonema boryanum PCC 73110. J. Bacteriol. 176, 1037-1046
    • (1994) J. Bacteriol. , vol.176 , pp. 1037-1046
    • Schrautemeier, B.1    Cassing, A.2    Böhme, H.3
  • 22
    • 0025828312 scopus 로고
    • A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia coli
    • Grabau, C., Schatt, E., Jouanneau, Y., and Vignais, P.M. (1991) A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia coli. J. Biol. Chem. 266, 3294-3299
    • (1991) J. Biol. Chem. , vol.266 , pp. 3294-3299
    • Grabau, C.1    Schatt, E.2    Jouanneau, Y.3    Vignais, P.M.4
  • 23
    • 0026726780 scopus 로고
    • Expression in Escherichia coli and characterization of a recombinant 7Fe ferredoxin of Rhodobacter capsulatus
    • Jouanneau, Y., Duport, C., Meyer, C., and Gaillard, J. (1992) Expression in Escherichia coli and characterization of a recombinant 7Fe ferredoxin of Rhodobacter capsulatus. Biochem. J. 286, 269-273
    • (1992) Biochem. J. , vol.286 , pp. 269-273
    • Jouanneau, Y.1    Duport, C.2    Meyer, C.3    Gaillard, J.4
  • 24
    • 0027169227 scopus 로고
    • Cloning and expression in Escherichia coli of the gene encoding the [2Fe-2S] ferredoxin from Clostridium pasteurianum
    • Fujinaga, J. and Meyer, J. (1993) Cloning and expression in Escherichia coli of the gene encoding the [2Fe-2S] ferredoxin from Clostridium pasteurianum. Biochem. Biophys. Res. Commun. 192, 1115-1122
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 1115-1122
    • Fujinaga, J.1    Meyer, J.2
  • 25
    • 0028101167 scopus 로고
    • Cloning, sequencing and overexpression of the Desulfovibrio gigas ferredoxin gene in E. coli
    • Chen, B., Menon, N.K., Dervertarnian, L., Moura, J.J.G., and Przybyla, A.E. (1994) Cloning, sequencing and overexpression of the Desulfovibrio gigas ferredoxin gene in E. coli. FEBS Lett. 361, 401-404
    • (1994) FEBS Lett. , vol.361 , pp. 401-404
    • Chen, B.1    Menon, N.K.2    Dervertarnian, L.3    Moura, J.J.G.4    Przybyla, A.E.5
  • 26
    • 0028023872 scopus 로고
    • Cloning, expression, and molecular characterization of the gene encoding an extremely thermostable [4Fe-4S] ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus
    • Heltzel, A., Smith, E.T., Zhou, Z.H., Blarney, J.M., and Adams, M.W. (1994) Cloning, expression, and molecular characterization of the gene encoding an extremely thermostable [4Fe-4S] ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 176, 4790-4793
    • (1994) J. Bacteriol. , vol.176 , pp. 4790-4793
    • Heltzel, A.1    Smith, E.T.2    Zhou, Z.H.3    Blarney, J.M.4    Adams, M.W.5
  • 27
    • 0028143050 scopus 로고
    • Characteristic features of the heterologous functional synthesis in Escherichia coli of a 2[4Fe-4S] ferredoxin
    • Moulis, J.-M., Davasse, V., and Jesus, F.D. (1994) Characteristic features of the heterologous functional synthesis in Escherichia coli of a 2[4Fe-4S] ferredoxin. Biometals 7, 272-278
    • (1994) Biometals , vol.7 , pp. 272-278
    • Moulis, J.-M.1    Davasse, V.2    Jesus, F.D.3
  • 28
    • 0028321562 scopus 로고
    • Cloning and expression of the gene encoding the 7Fe type ferredoxin from a thermophilic hydrogen oxidizing bacterium, Bacillus schlegelii
    • Aono, S., Nakamura, S., Aono, R., and Okura, I. (1994) Cloning and expression of the gene encoding the 7Fe type ferredoxin from a thermophilic hydrogen oxidizing bacterium, Bacillus schlegelii. Biochem. Biophys. Res. Commun. 201, 938-942
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 938-942
    • Aono, S.1    Nakamura, S.2    Aono, R.3    Okura, I.4
  • 29
    • 0027730359 scopus 로고
    • Synthesis, cloning and expression of a synthetic gene for high potential iron protein from Chromatium vinosum
    • Agarwal, A., Tan, J., Eren, M., Tevelev, A., Lui, S.M., and Cowan, J.A. (1993) Synthesis, cloning and expression of a synthetic gene for high potential iron protein from Chromatium vinosum. Biochem. Biophys. Res. Commun. 197, 1357-1362
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1357-1362
    • Agarwal, A.1    Tan, J.2    Eren, M.3    Tevelev, A.4    Lui, S.M.5    Cowan, J.A.6
  • 30
    • 0028091327 scopus 로고
    • Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificance
    • Yano, T., Sled', V.D., Ohnishi, T., and Yagi, T. (1994) Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificance. Biochemistry 1994, 494-499
    • (1994) Biochemistry , vol.1994 , pp. 494-499
    • Yano, T.1    Sled', V.D.2    Ohnishi, T.3    Yagi, T.4
  • 31
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters: Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng, L., Cash, V.L., Flint, D.H., and Dean, D.R. (1998) Assembly of iron-sulfur clusters: identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 35
    • 0007541458 scopus 로고
    • Nucleotide sequence, promoter structure, and expression of the petF1 gene encoding the [2Fe-2S] FdI from the nitrogen-fixing non-heterocystous cyanobacterium Plectonema boryanum PCC 73110
    • Cassing, A., Boehme, H., and Schrautemeier, B. (1995) Nucleotide sequence, promoter structure, and expression of the petF1 gene encoding the [2Fe-2S] FdI from the nitrogen-fixing non-heterocystous cyanobacterium Plectonema boryanum PCC 73110. Plant Physiol. 109, 1499
    • (1995) Plant Physiol. , vol.109 , pp. 1499
    • Cassing, A.1    Boehme, H.2    Schrautemeier, B.3
  • 36
    • 0026704947 scopus 로고
    • Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli
    • Ta, D.T. and Vickery, L.E. (1992) Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli. J. Biol. Chem. 267, 11120-11125
    • (1992) J. Biol. Chem. , vol.267 , pp. 11120-11125
    • Ta, D.T.1    Vickery, L.E.2
  • 37
    • 0024988580 scopus 로고
    • Two distinct ferredoxins from Rhodobacter capsulatus: Complete amino acid sequences and molecular evolution
    • Saeki, K., Suetsugu, Y., Yao, Y., Horio, T., Marrs, B.L., and Matsubara, H. (1990) Two distinct ferredoxins from Rhodobacter capsulatus: complete amino acid sequences and molecular evolution. J. Biochem. 108, 475-482
    • (1990) J. Biochem. , vol.108 , pp. 475-482
    • Saeki, K.1    Suetsugu, Y.2    Yao, Y.3    Horio, T.4    Marrs, B.L.5    Matsubara, H.6
  • 38
    • 0025768497 scopus 로고
    • Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus
    • Saeki, K., Suetsugu, Y., Tokuda, K., Miyatake, Y., Young, D.A., Marrs, B.L., and Matsubara, H. (1991) Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus. J. Biol. Chem. 266, 12889-12895
    • (1991) J. Biol. Chem. , vol.266 , pp. 12889-12895
    • Saeki, K.1    Suetsugu, Y.2    Tokuda, K.3    Miyatake, Y.4    Young, D.A.5    Marrs, B.L.6    Matsubara, H.7
  • 39
    • 0023918263 scopus 로고
    • Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin: Evolutionary implications for bacterial ferredoxins
    • Fukuyama, K., Nagahara, Y., Tsukihara, T., Katsube, Y., Hase, T., and Matsubara, H. (1988) Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin: evolutionary implications for bacterial ferredoxins. J. Mol. Biol. 199, 183-193
    • (1988) J. Mol. Biol. , vol.199 , pp. 183-193
    • Fukuyama, K.1    Nagahara, Y.2    Tsukihara, T.3    Katsube, Y.4    Hase, T.5    Matsubara, H.6
  • 40
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen, N.T., Tamaki, S., Kobayashi, D., and Trollinger, D. (1988) Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70, 191-197
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 41
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genome library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genome library. Cell 50, 495-508
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 43
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. and Walker, J.E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 44
    • 78651153791 scopus 로고
    • Disk electrophoresis II. Method and application to human serum proteins
    • Davis, B.J. (1964) Disk electrophoresis II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121, 404-426
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-426
    • Davis, B.J.1
  • 48
    • 0020582808 scopus 로고
    • Origin of the labile sulfide in the iron-sulfur proteins of Escherichia coli
    • White, R.H. (1983) Origin of the labile sulfide in the iron-sulfur proteins of Escherichia coli. Biochem. Biophys. Res. Commun. 112, 66-72
    • (1983) Biochem. Biophys. Res. Commun. , vol.112 , pp. 66-72
    • White, R.H.1
  • 49
    • 0029278916 scopus 로고
    • Overexpression in Escherichia coli of the fdxA gene encoding Rhodobacter capsulatus ferredoxin II
    • Armengaud, J. and Jouanneau, Y. (1995) Overexpression in Escherichia coli of the fdxA gene encoding Rhodobacter capsulatus ferredoxin II. Protein Express. Purif. 6, 176-184
    • (1995) Protein Express. Purif. , vol.6 , pp. 176-184
    • Armengaud, J.1    Jouanneau, Y.2
  • 50
    • 0030702958 scopus 로고    scopus 로고
    • Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase
    • Chen, S., Zheng, L., Dean, D.R., and Zalkin, H. (1997) Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase. J. Bacteriol. 179, 7587-7590
    • (1997) J. Bacteriol. , vol.179 , pp. 7587-7590
    • Chen, S.1    Zheng, L.2    Dean, D.R.3    Zalkin, H.4


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