Cloning and Characterization of the Cu,Zn Superoxide Dismutase (SOD1) cDNA from the Spider, Araneus ventricosus

  • Choi Young Soo (College of Natural Resources and Life Science, Dong-A University) ;
  • Choo Young Moo (College of Natural Resources and Life Science, Dong-A University) ;
  • Li Jianhong (College of Natural Resources and Life Science, Dong-A University, Department of Plant Protection, College of Plant Science and Technology, Hyazhong Agricultural University) ;
  • Sohn Hung Dae (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin Byung Rae (College of Natural Resources and Life Science, Dong-A University)
  • Published : 2005.03.01

Abstract

A Cu,Zn superoxide dismutase (SOD1) cDNA was cloned from the spider, Araneus ventricosus. The A. ventricosus SOD1 (AvSOD1) cDNA contains an open reading frame of 495 bp encoding 165 amino acid polypeptide with a predicted molecular mass of 17,114 Da and pI of 6.55, and possesses the typical metal binding ligands of six histidines and one aspartic acid common to SOD1s. The deduced amino acid sequence of the AvSOD1 cDNA showed $51\%$ identity to Ceratitis capitata SOD1, and $50\%$ to SOD1 sequences of both Drosophila melanogaster and Chymomyza amoena. Northern blot analysis revealed the presence of AvSOD1 transcripts in all tissues examined.

Keywords

References

  1. Borders, C. J., J. E. Saunders, D. M. Blech and I. Fridovich (1985) Essentially of the active site arginine residue for the normal catalytic activity of CU, Zn superoxide dismutase. Biochem. J. 230, 771-776
  2. Chary, P., D. Dillon, A. L. Schroeder and D. O. Natvig (1994) Superoxide dismutase (sod-1) null mutants of Neurospora crassa: oxidative stress sensitivity, spontaneous mutation rate and response to mutagens. Genetics 137, 723-730
  3. Chaturvedi, S., A. J. Hamilton, P. Hobby, G. Zhu, C. V. Lowry and V. Chaturvedi (2001) Molecular cloning, phylogenetic analysis and three-dimensional modeling of CU, Zn superoxide dismutase (CnSOD1) from three varieties of Cryptococcus neofonnans. Gene 268, 41-51 https://doi.org/10.1016/S0378-1119(01)00408-5
  4. Chung, E. H., K. S. Lee, J. H. Han, H. D. Sohn and B. R. Jin (2001) Analysis of expressed sequence tags of the spider, Araneus ventricosus. Int. J. Indust. Entomol. 3, 191-199
  5. Crapo, J. D., T. Oury, C. Rabouille, J. W. Slot and L. Y. Chang (1992) Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc. Natl. Acad. Sci. USA 89, 10405-10409 https://doi.org/10.1073/pnas.89.21.10405
  6. Dalton, T. P., H. G. Shertzer and A. Puga (1999) Regulation of gene expression by reactive oxygen. Annu. Rev. Pharmacol. Toxicol. 39, 67-101 https://doi.org/10.1146/annurev.pharmtox.39.1.67
  7. Fabrizio, P., L. Liou, V. N. Moy, A. Diaspro, J. S. Valentine, E. B. Gralla and V. D. Longo (2003) SOD2 functions downstream of Sch9 to extend longevity in yeast. Genetics 163, 35-46
  8. Fridovich, I. (1986) Superoxide dismutases. Adv. Enzymol. ReI. Areas Mol. BioI. 58, 61-97
  9. Fridovich, I. (1995) Superoxide radical and superoxide dismutase. Ann. Rev. Biochem. 64, 97-112 https://doi.org/10.1146/annurev.bi.64.070195.000525
  10. Jamieson, D. J., S. L. Rivers and D. W. Stephen (1994) Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress. Microbiology 140, 3277-3283 https://doi.org/10.1099/13500872-140-12-3277
  11. Kwiatowski, J. M., D. Skarecky and F. J. Ayala (1992a) Structure and sequence of the CU, Zn Sod gene in the Mediterranean fruit-fly Ceratitis capitata: Intron insertion/deletion and evolution of the gene. Mol. Phylogenet. Evol. 1, 72-82 https://doi.org/10.1016/1055-7903(92)90037-H
  12. Kwiatowski, J. M., D. Skarecky, M. Burgos and F. J. Ayala (1992b) Structure and sequence of the CU, Zn superoxide dismutase gene of Chymomyza amoena: phylogeny of the genus and codon-use evolution. Insect Mol. Biol. 1, 3-13 https://doi.org/10.1111/j.1365-2583.1993.tb00072.x
  13. Malinowski, D. P. and I. Fridovich (1979) Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry 18, 5909-5917 https://doi.org/10.1021/bi00593a023
  14. McCord, J. M. and I. Fridovich (1969) The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. J. BioI. Chem. 244, 6056-6063
  15. McMaster, G. K. and G. G. Carmichael (1977) Analysis of single-and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc. Natl. Acad. Sci. USA 74, 4835-4838 https://doi.org/10.1073/pnas.74.11.4835
  16. Mount, D. W. (1996) Reprogramming transcription. Nature 383, 763-764 https://doi.org/10.1038/383763a0
  17. Orr, W. C. and R. S. Sohol (1994) Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263, 1128-1130 https://doi.org/10.1126/science.8108730
  18. Parker, J. D., K. M. Parker, B. H. Sohol, R. S. Sohol and L. Keller (2004) Decreased expression of Cu-Zn superoxide dismutase 1 in ants with extreme lifespan. Proc. Natl. Acad. Sci. USA 101, 3486-4389 https://doi.org/10.1073/pnas.0400222101
  19. Parker, M. W., F. Bossa, D. Barra, W. H. Bannister and J. V. Bannister (1986) Structural and evolutionary relationships between the eukaryotic superoxide dismutase; in Superoxide and superoxide dismutase in chemistry, biology and medicine. Rotilio, G. (ed.), pp. 237-245, Elsevier Sci. Publ., Amsterdam
  20. Parkes, T. L., A. J. Elia, D. Dickinson, A. J. Hilliker, J. P. Phillips and G. L. Boulianne (1998) Extension of Drosophila lifespan by overexpression of human SOD 1 in motomeurons. Nat. Genet. 19, 171-174 https://doi.org/10.1038/534
  21. Sohol, R. S., A. Agarwal, S. Agarwal and W. C. Orr (1995) Simultaneous overexpression of copper- and zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster. J. Biol. Chem. 270, 15671-15674 https://doi.org/10.1074/jbc.270.26.15671
  22. Sturtz, L. A., K. Diekert, L. T. Jenden, R. Lill and V. C. Culotta (2001) A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. J. Biol. Chem. 276, 38084-38089
  23. Sun, J. and J. Tower (1999) FLP recombinase-mediated induction of Cu/Zn-superoxide dismutase transgene expression can extend the life span of adult Drosophila melanogaster flies. Mol. Cell. BioI. 19, 216-228
  24. Swofford, D. L. (2000) PAUP*. Phylogenetic Analysis Using Parsimony (*and Other Methods), Version 4.0. Sinauer Sunderland. MA
  25. Tainer, J. A., E. D. Getzoff, K. M. Beem, J. S. Richardson and D. C. Richardson (1982) Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160, 181-217 https://doi.org/10.1016/0022-2836(82)90174-7