cDNA cloning, high-level expression, purification, and characterization of an avian Cu,Zn superoxide dismutase from Peking duck

Protein Expression and Purification

Volumn 25, Issue 3, 2002, Pages 379-388

  Liu, Wei ^a   Zhu, Rong Huan ^a   Li, Gen Pei ^a,b   Wang, Da Cheng ^a,b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Cysteine; Overexpression; Peking duck; Superoxide dismutase; Thermal stability

Indexed keywords

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CIRCULAR DICHROISM; CLONING, MOLECULAR; DNA, COMPLEMENTARY; DUCKS; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUPEROXIDE DISMUTASE;

ANAS PLATYRHYNCHOS; ANAS SP.; AVES; BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; STAPHYLOCOCCUS PHAGE 3A; VECTORS;

EID: 0036408929     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00040-2     Document Type: Article

References (44)

1. J.V. Bannister, W.H. Bannister, G. Rotilio, Aspects of the structure, function, and applications of superoxide dismutase, CRC Crit. Rev. Biochem. 22 (1987) 111-180.
2. J.M. McCord, I. Fridovich, Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J. Biol. Chem. 224 (1969) 6049-6055.
3. I. Fridovich, Superoxide dismutase, Annu. Rev. Biochem. 44 (1975) 147-159.
4. B.A. Freeman, J.D. Crapo, Biology of disease: Free radicals and tissue injury, Lab. Invest. 47 (1982) 412-426.
5. I. Fridovich, Superoxide dismutase, Adv. Enzymol. 58 (1986) 61-97.
6. E.D. Getzo, J.A. Tainer, M.M. Stempien, G.I. Bell, R.A. Hallewell, Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif, Proteins 5 (1989) 322-336.
7. B.J. Bricker, L.B. Tabatabai, B.A. Judge, B.L. Deyoe, J.E. Mayfield, Cloning, expression, and occurrence of the Brucella Cu,Zn superoxide dismutase, Infect. Immun. 58 (1990) 2935-2939.
8. R.A. Hallewell, F.R. Masiarz, R.C. Najarian, J.P. Puma, M.R. Quiroga, A. Randolph, R. Sanchez-Pescador, C.J. Scandella, B. Smith, K.S. Steimer, Human Cu/Zn superoxide dismutase cDNA: Isolation of clones synthesising high levels of active or inactive enzyme from an expression library, Nucleic Acids Res. 13 (1985) 2017-2034.
9. J.R. Hartman, T. Geller, Z. Yavin, D. Bartfeld, D. Kanner, H. Aviv, M. Gorecki, High-level expression of enzymatically active human Cu/Zn superoxide dismutase in Escherichia coli, Proc. Natl. Acad. Sci. USA 83 (1986) 7142-7146.
10. Z. Hong, P.T. LoVerde, M.L. Hammarskjold, D. Rekosh, Schistosoma mansoni: Cloning of a complementary DNA encoding a cytosolic Cu/Zn superoxide dismutase and high-yield expression of the enzymatically active gene product in Escherichia coli, Exp. Parasitol. 75 (1992) 308-322.
11. H. Xiang, W.Z. Wei, H.R. Tan, S.X. Guo, Cloning and expression of human Cu/Zn superoxide dismutase gene in Lactococcus lactis, Chin. J. Biotechnol. 16 (2000) 6-9.
12. R.A. Hallewell, K.C. Imlay, P. Lee, N.M. Fong, C. Gallegos, E.D. Getzo, J.A. Tainer, D.E. Cabelli, P. Tekamp-Olson, G.T. Mullenbach, L.S. Cousens, Thermostabilization of recombinant human and bovine Cu,Zn superoxide dismutases by replacement of free cysteines, Biochem. Biophys. Res. Commun. 181 (1991) 474-480.
13. D.F. McRee, S.M. Redford, E.D. Getzo, J.R. Lepock, R.A. Hallewell, J.A. Tainer, Changes in crystallographic structure and thermostablility of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine, J. Biol. Chem. 265 (1990) 14234-14241.
14. H.Y. Yoo, S.S. Kim, H.M. Rho, Overexpression and simple purification of human superoxide dismutase (SOD1) in yeast and its resistance to oxidative stress, J. Biotechnol. 68 (1999) 29-35.
15. I. Reveillaud, A. Niedzwiecki, K.G. Bensch, J.E. Fleming, Expression of bovine superoxide dismutase in Drosophila melanogaster augments resistance of oxidative stress, Mol. Cell. Biol. 11 (1991) 632-640.
16. I. Ceballos, A. Nicole, P. Briand, G. Grimber, A. Delacourte, S. Flament, J.L. Blouin, M. Thevenin, P. Kamoun, P.M. Sinet, Expression of human Cu,Zn superoxide dismutase gene in transgenic mice: Model for gene dosage effect in Down syndrome, Free Radic. Res. Commun. 12-13 Pt 2 (1991) 581-589.
17. J.L. Stanton, S.D. Wilton, N.G. Laing, Characterization of the chicken Cu,Zn superoxide dismutase gene, DNA Seq. 6 (1996) 357-360.
18. R.A. Weisiger, I. Fridovich, Superoxide dismutase, J. Biol. Chem. 248 (1996) 3582-3592.
19. K.Q. Wang, Z.G. Li, Q.L. Hao, J.L. He, G. Wu, B.S. Chen, H. Xue, J.M. Wang, X.Z. Li, Y.M. Hu, The characteristic transportation of cholesterol by serum lipoproteins and its role in anti-atherogenesis in Beijing Duck, Acta Acad. Med. Sin. 8 (1986) 88-94.
20. P. Ye, B. Chen, S. Wang, Association of polymorphisms of the apolipoprotein B gene with coronary heart disease in Han Chinese, Atherosclerosis 117 (1995) 43-50.
21. H. Esterbauer, G. Wag, H. Puhl, Lipid peroxidation and its role in atherosclerosis, Br. Med. Bull. 49 (1993) 566-576.
22. L.E. Rikans, K.R. Hornbrook, Lipid peroxidation, antioxidant protection and aging, Biochim. Biophys. Acta 1362 (1997) 116-127.
23. P.W. Li, C.F. Xu, N. Wang, G.P. Li, Purification and some properties of charge isomers of copper and zinc superoxide dismutase from Peking duck erythrocytes, Chin. Biochem. J. 11 (1995) 276-280.
24. U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage, Nature 277 (1970) 680-685.
25. S. Marklund, G. Marklund, Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase, Eur. J. Biochem. 47 (1974) 469-474.
26. M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
27. L. Sherman, N. Dafni, J. Lieman-Hurwitz, Y. Groner, Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA, Proc. Natl. Acad. Sci. USA 80 (1983) 5465-5469.
28. K. Arai, S. Iizuka, A. Makita, K. Oikawa, N. Taniguchi, Purification of Cu,Zn-superoxide dismutase from human erythrocytes by immunoaffinity chromatography. Evidence for the presence of isoelectric heterogeneity, J. Immunol. Methods 91 (1986) 139-143.
29. B. Lonnerdal, C.L. Keen, L.S. Hurley, Isoelectric focusing of superoxide dismutase isoenzymes, FEBS Lett. 108 (1976) 51-55.
30. M.E. Schinina, P. Carlini, F. Polticelli, F. Zappacosta, F. Bossa, L. Calabrese, Amino acid sequence of chicken Cu,Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues, Eur. J. Biochem. 237 (1996) 433-439.
31. N. Crosti, P. Sausa, Evidence for tissue-specific electromorphs of Cu/Zn SOD unrelated to genetic control, Biochem. Genet. 18 (1980) 693-696.
32. S. Yano, Multiple isoelectric variants of copper, zinc-superoxide dismutase from rat liver, Arch. Biochem. Biophys. 279 (1990) 60-69.
33. J. Kajihara, M. Enomoto, K. Seya, Y. Sukenage, K. Katoh, Physicochemical properties of charge isomers of recombinant human superoxide dismutas, J. Biochem. (Tokyo) 104 (1988) 638-642.
34. M.E. Schinina, D. Barra, F. Bossa, L. Calabrese, L. Montesano, M.T. Carri, P. Mariottini, F. Amaldi, G. Rotilio, Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis, Arch. Biochem. Biophys. 272 (1989) 507-515.
35. H.E. Parge, R.A. Hallewell, J.A. Tainer, Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase, Proc. Natl. Acad. Sci. USA 89 (1992) 6109-6113.
36. J.A. Tainer, E.D. Getzo, K.M. Beem, J.S. Richardson, D.C. Richardson, Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase, J. Mol. Biol. 160 (1982) 181-217.
37. V. Ravindranath, D.J. Reed, Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress, Biochem. Biophys. Res. Commun. 169 (1990) 1075-1079.
38. V. Ravindranath, T. Seres, T. Moriguchi, J.A. Thormas, R.B. Johnston, S-thiolation of glyceraldhyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes, J. Biol. Chem. 269 (1994) 25010-25015.
39. J.R. Lepock, H.E. Frey, R.A. Hallewell, Contribution of conformational stability and reversibility of unfolding to the increased thermostability of human and bovine superoxide dismutase mutated at free cysteines, J. Biol. Chem. 265 (1990) 21612-21618.
40. M.C. Bonaccorsi di Patti, M.T. Carri, R. Gabbianelli, R. Da Gai, C. Volpe, A. Giartosio, G. Rotilio, A. Battistoni, A free cysteine residue at the dimer interface decreases conformational stability of Xenopus laevis copper,zinc superoxide dismutase, Arch. Biochem. Biophys. 377 (2000) 284-289.
41. C.O. Beauchamp, I. Fridovich, Isozymes of superoxide dismutase from wheat germ, Biochim. Biophys. Acta 317 (1973) 50-64.
42. K. Djinovic, G. Gatti, A. Coda, L. Antolini, G. Pelosi, A. Desideri, M. Falconi, F. Marmocchi, G. Rotilio, M. Bolognesi, Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic refinement at 2.5 resolution, J. Mol. Biol. 225 (1992) 791-809.
43. U. Weser, A. Fretzdor, R. Prinz, Superoxide dismutase in baker's yeast, FEBS Lett. 27 (1972) 267-269.
44. H. Liu, H. Zhu, D.K. Eggers, A.M. Nersissian, K.F. Faull, J.J. Goto, J. Ai, J. Sanders-Loehr, E.B. Gralla, J.S. Valentine, Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper,zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant, Biochemistry 39 (2000) 8125-8132.