메뉴 건너뛰기




Volumn 1434, Issue 2, 1999, Pages 284-295

cDNA cloning, overproduction and characterization of rat adrenodoxin reductase

Author keywords

Adrenodoxin; Adrenodoxin reductase; cDNA cloning; Electron transfer; Escherichia coli; Rat

Indexed keywords

COMPLEMENTARY DNA; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032874492     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00180-6     Document Type: Article
Times cited : (3)

References (49)
  • 1
    • 0001901923 scopus 로고
    • Cytochrome P-450-linked electron transport system in monooxygenase reaction
    • in: T. Omura, Y. Ishimuram and Y. Fujii-Kuriyama (Eds.), Kodansha, Tokyo
    • S. Takemori, T. Yamazaki and S. Ikushiro, Cytochrome P-450-linked electron transport system in monooxygenase reaction, in: T. Omura, Y. Ishimuram and Y. Fujii-Kuriyama (Eds.), Cytochrome P-450, 2nd edn., Kodansha, Tokyo, 1993, pp. 44-63.
    • (1993) Cytochrome P-450, 2nd Edn. , pp. 44-63
    • Takemori, S.1    Yamazaki, T.2    Ikushiro, S.3
  • 2
    • 0019334794 scopus 로고
    • In vitro synthesis of adrenodoxin and adrenodoxin reductase: Existence of a putative large precursor form of adrenodoxin
    • Nabi N., Omura T. In vitro synthesis of adrenodoxin and adrenodoxin reductase: Existence of a putative large precursor form of adrenodoxin. Biochem. Biophys. Res. Commun. 97:1980;680-686.
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 680-686
    • Nabi, N.1    Omura, T.2
  • 4
    • 0015511154 scopus 로고
    • The purification and properties of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria
    • Suhara K., Ikeda Y., Takemori S., Katagiri M. The purification and properties of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria. FEBS Lett. 28:1972;45-47.
    • (1972) FEBS Lett. , vol.28 , pp. 45-47
    • Suhara, K.1    Ikeda, Y.2    Takemori, S.3    Katagiri, M.4
  • 5
    • 0016610284 scopus 로고
    • Purification and crystallization of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria
    • Sugiyama T., Yamano T. Purification and crystallization of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria. FEBS Lett. 52:1975;145-148.
    • (1975) FEBS Lett. , vol.52 , pp. 145-148
    • Sugiyama, T.1    Yamano, T.2
  • 6
    • 0017157781 scopus 로고
    • Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase form bovine adrenocortical mitochondria. I. Physicochemical properties of holo- And apo-NADPH-adrenodoxin reductase and interaction between non-heme iron proteins and the reductase
    • Hiwatashi A., Ichikawa Y., Maruya N., Yamano T., Aki K. Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase form bovine adrenocortical mitochondria. I. Physicochemical properties of holo- and apo-NADPH-adrenodoxin reductase and interaction between non-heme iron proteins and the reductase. Biochemistry. 15:1976;3082-3090.
    • (1976) Biochemistry , vol.15 , pp. 3082-3090
    • Hiwatashi, A.1    Ichikawa, Y.2    Maruya, N.3    Yamano, T.4    Aki, K.5
  • 8
    • 0343052039 scopus 로고    scopus 로고
    • Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase
    • Lapko A., Müller A., Heese O., Ruckpaul K., Heinemann U. Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase. Proteins. 28:1997;289-292.
    • (1997) Proteins , vol.28 , pp. 289-292
    • Lapko, A.1    Müller, A.2    Heese, O.3    Ruckpaul, K.4    Heinemann, U.5
  • 9
    • 0033057396 scopus 로고    scopus 로고
    • The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis
    • Ziegler G.A., Vonrhein C., Hanukoglu I., Schulz G.E. The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis. J. Mol. Biol. 289:1999;981-990.
    • (1999) J. Mol. Biol. , vol.289 , pp. 981-990
    • Ziegler, G.A.1    Vonrhein, C.2    Hanukoglu, I.3    Schulz, G.E.4
  • 10
    • 0023516679 scopus 로고
    • Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex
    • Sagara Y., Takata Y., Miyata T., Hara T., Horiuchi T. Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex. J. Biochem. (Tokyo). 102:1987;1333-1336.
    • (1987) J. Biochem. (Tokyo) , vol.102 , pp. 1333-1336
    • Sagara, Y.1    Takata, Y.2    Miyata, T.3    Hara, T.4    Horiuchi, T.5
  • 12
    • 0025052513 scopus 로고
    • Cloning and sequence of the human adrenodoxin reductase gene
    • Lin D., Shi Y., Miller W.L. Cloning and sequence of the human adrenodoxin reductase gene. Proc. Natl. Acad. Sci. USA. 87:1990;8516-8520.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8516-8520
    • Lin, D.1    Shi, Y.2    Miller, W.L.3
  • 14
    • 0029801008 scopus 로고    scopus 로고
    • A gene encoding a yeast equivalent of mammalian NADPH-adrenodoxin oxidoreductases
    • Lacour T., Dumas B. A gene encoding a yeast equivalent of mammalian NADPH-adrenodoxin oxidoreductases. Gene. 174:1996;289-292.
    • (1996) Gene , vol.174 , pp. 289-292
    • Lacour, T.1    Dumas, B.2
  • 15
    • 0032508616 scopus 로고    scopus 로고
    • Characterization of recombinant adrenodoxin reductase homologue (Arh1p) from yeast: Implication in in vitro cytochrome P45011β monooxygenase system
    • Lacour T., Achstetter T., Dumas B. Characterization of recombinant adrenodoxin reductase homologue (Arh1p) from yeast: Implication in in vitro cytochrome P45011β monooxygenase system. J. Biol. Chem. 273:1998;23984-23992.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23984-23992
    • Lacour, T.1    Achstetter, T.2    Dumas, B.3
  • 16
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport: The role of adrenodoxin as an electron shuttle
    • Lambeth J.D., Seybert D.W., Kamin H. Ionic effects on adrenal steroidogenic electron transport: The role of adrenodoxin as an electron shuttle. J. Biol. Chem. 254:1979;7255-7264.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 17
    • 0018563695 scopus 로고
    • The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex: The implication in ACTH function
    • Kido T., Kimura T. The formation of binary and ternary complexes of cytochrome P-450scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex: The implication in ACTH function. J. Biol. Chem. 254:1979;11806-11815.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 18
    • 0024539032 scopus 로고
    • Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P-450scc reduction reaction
    • Hara T., Kimura T. Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P-450scc reduction reaction. J. Biochem. (Tokyo). 105:1989;601-605.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 601-605
    • Hara, T.1    Kimura, T.2
  • 19
    • 0025998805 scopus 로고
    • Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc
    • Coghlan V.M., Vickery L.E. Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc. J. Biol. Chem. 266:1991;18606-18612.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18606-18612
    • Coghlan, V.M.1    Vickery, L.E.2
  • 20
    • 0026522889 scopus 로고
    • Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino-terminal regions
    • Sagara Y., Hara T., Ariyasu Y., Ando F., Tokunaga N., Horiuchi T. Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino-terminal regions. FEBS Lett. 300:1992;208-212.
    • (1992) FEBS Lett. , vol.300 , pp. 208-212
    • Sagara, Y.1    Hara, T.2    Ariyasu, Y.3    Ando, F.4    Tokunaga, N.5    Horiuchi, T.6
  • 21
    • 0026488375 scopus 로고
    • Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
    • Wada A., Waterman M.R. Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J. Biol. Chem. 267:1992;22877-22882.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22877-22882
    • Wada, A.1    Waterman, M.R.2
  • 22
    • 0027284228 scopus 로고
    • Charge pair interactions stabilizing ferredoxin- ferredoxin reductase complexes: Identification by complementary site-specific mutations
    • Brandt M.E., Vickery L.E. Charge pair interactions stabilizing ferredoxin- ferredoxin reductase complexes: Identification by complementary site-specific mutations. J. Biol. Chem. 268:1993;17126-17130.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17126-17130
    • Brandt, M.E.1    Vickery, L.E.2
  • 23
    • 0027980825 scopus 로고
    • Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer
    • Beckert V., Dettmer R., Bernhardt R. Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer. J. Biol. Chem. 269:1994;2568-2573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2568-2573
    • Beckert, V.1    Dettmer, R.2    Bernhardt, R.3
  • 24
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H., Kraft R., Bernhardt R. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J. Biol. Chem. 269:1994;22557-22564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 25
    • 0029560248 scopus 로고
    • The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function
    • Uhlmann H., Bernhardt R. The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function. J. Biol. Chem. 270:1995;29959-29966.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29959-29966
    • Uhlmann, H.1    Bernhardt, R.2
  • 26
    • 0029824469 scopus 로고    scopus 로고
    • Different effects of carboxy-terminal deletion in the adrenodoxin molecule on cytochrome c and acetylated cytochrome c reductions
    • Sagara Y., Hara T., Ariyasu Y., Kajiyama A., Yasukochi T., Horiuchi T. Different effects of carboxy-terminal deletion in the adrenodoxin molecule on cytochrome c and acetylated cytochrome c reductions. Biol. Pharm. Bull. 19:1996;1401-1406.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 1401-1406
    • Sagara, Y.1    Hara, T.2    Ariyasu, Y.3    Kajiyama, A.4    Yasukochi, T.5    Horiuchi, T.6
  • 28
    • 0030049051 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a full-length cDNA of rat adrenodoxin
    • Sagara Y., Watanabe Y., Kawamura K., Yubisui T. Cloning and sequence analysis of a full-length cDNA of rat adrenodoxin. Biol. Pharm. Bull. 19:1996;39-41.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 39-41
    • Sagara, Y.1    Watanabe, Y.2    Kawamura, K.3    Yubisui, T.4
  • 29
    • 0031764295 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli and characterization of the precise mature form of rat adrenodoxin
    • Sagara Y., Aramaki H. Overproduction in Escherichia coli and characterization of the precise mature form of rat adrenodoxin. Biol. Pharm. Bull. 21:1998;1106-1109.
    • (1998) Biol. Pharm. Bull. , vol.21 , pp. 1106-1109
    • Sagara, Y.1    Aramaki, H.2
  • 30
    • 0027292014 scopus 로고
    • Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization
    • Sagara Y., Wada A., Takata Y., Waterman M.R., Sekimizu K., Horiuchi T. Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization. Biol. Pharm. Bull. 16:1993;627-630.
    • (1993) Biol. Pharm. Bull. , vol.16 , pp. 627-630
    • Sagara, Y.1    Wada, A.2    Takata, Y.3    Waterman, M.R.4    Sekimizu, K.5    Horiuchi, T.6
  • 31
    • 0024592960 scopus 로고
    • Purification and catalytic properties of a cross-linked complex between adrenodoxin reductase and adrenodoxin
    • Hara T., Kimura T. Purification and catalytic properties of a cross-linked complex between adrenodoxin reductase and adrenodoxin. J. Biochem. (Tokyo). 105:1989;594-600.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 594-600
    • Hara, T.1    Kimura, T.2
  • 33
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 19:1982;259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 35
    • 0023395492 scopus 로고
    • Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli
    • Looman A.C., Bodlaender J., Comstock L.J., Eaton D., Jhurani P., deBoer H.A., vanKnippenberg P.H. Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli. EMBO J. 6:1987;2489-2492.
    • (1987) EMBO J. , vol.6 , pp. 2489-2492
    • Looman, A.C.1    Bodlaender, J.2    Comstock, L.J.3    Eaton, D.4    Jhurani, P.5    Deboer, H.A.6    Vanknippenberg, P.H.7
  • 36
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P45017α-hydroxylase in Escherichia coli
    • Barnes H., Arlotto M.P., Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P45017α-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA. 88:1991;5597-5601.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5597-5601
    • Barnes, H.1    Arlotto, M.P.2    Waterman, M.R.3
  • 37
    • 0023571657 scopus 로고
    • High- copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- Or kanamycin-resistance selection
    • Takeshita S., Sato M., Toba M., Masahashi W., Hashimoto-Gotoh T. High- copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- or kanamycin-resistance selection. Gene. 61:1987;63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 38
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains Nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 40
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • Chance B., Williams G.R. The respiratory chain and oxidative phosphorylation. Adv. Enzymol. 17:1956;65-134.
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.R.2
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 12:1984;857-872.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 44
    • 0017089669 scopus 로고
    • 3′ Non-coding region sequences in eukaryotic messenger RNA
    • Proudfoot N.J., Brownlee G.G. 3′ Non-coding region sequences in eukaryotic messenger RNA. Nature. 263:1976;211-214.
    • (1976) Nature , vol.263 , pp. 211-214
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 45
    • 0024516824 scopus 로고
    • CDNA sequence of adrenodoxin reductase: Identification of NADP-binding sites in oxidoreductases
    • Hanukoglu I., Gutfinger T. cDNA sequence of adrenodoxin reductase: Identification of NADP-binding sites in oxidoreductases. Eur. J. Biochem. 180:1989;479-484.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 479-484
    • Hanukoglu, I.1    Gutfinger, T.2
  • 46
    • 0026740820 scopus 로고
    • Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli
    • Brandt M.E., Vickery L.E. Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli. Arch. Biochem. Biophys. 294:1992;735-740.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 735-740
    • Brandt, M.E.1    Vickery, L.E.2
  • 47
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel P.-H., Schmitter J.-M., Dessen P., Fayat G., Blanquet S. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. USA. 86:1989;8247-8251.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8247-8251
    • Hirel, P.-H.1    Schmitter, J.-M.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 48
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:1969;4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 49
    • 0015878083 scopus 로고
    • Studies on adrenal steroid hydroxylases: Complex formation of the hydroxylase components
    • Chu J.-W., Kimura T. Studies on adrenal steroid hydroxylases: Complex formation of the hydroxylase components. J. Biol. Chem. 248:1973;5183-5187.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5183-5187
    • Chu, J.-W.1    Kimura, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.