Copper, Zinc-Superoxide Dismutase (Cu/Zn SOD) Gene During Embryogenesis of Bombyx mori: Molecular Cloning, Characterization and Expression

  • Hong, Sun-Mee (College of Agriculture and Life Sciences, Kyungpook National University) ;
  • Kang, Seok-Woo (Department of Agricultural Biology, NIAST, RDA) ;
  • Goo, Tae-Won (Department of Agricultural Biology, NIAST, RDA) ;
  • Kim, Nam-Soon (Laboratory of Human Genomics, Genome Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Lee, Jin-Sung (CoreBio Research Institute of Lifescience Biotechonlogy) ;
  • Nho, Si-Kab (College of Agriculture and Life Sciences, Kyungpook National University)
  • 발행 : 2006.09.30

초록

BmCu/Zn SOD was isolated from early embryo of Bombyx mori using microarray analysis. The BmCu/Zn SOD gene was observed during the early embryonic stage with the strongest signal found at the unfertilizaion, fertilization and blastoderm stages. The BmCu/Zn SOD gene encodes a protein of 154 amino acids with a calculated Mr of 15 kDa. The deduced amino acid sequence of BmCu/Zn SOD indicated that the residues that form on the Cu/Zn binding site are conserved and that the sequence is a 60% identity to that of M. domestica. In a phylogenetic tree, Bm SOD was also close to Drosophila SODs rather than other insect SODs. The BmCu/Zn SOD gene exists as a single copy in the genome. Transcripts of BmCu/Zn SOD cDNA were identified by northern blot analysis. The expression of the BmCu/Zn SOD gene was observed weakly in most of larvae, pre-pupae, pupae and adult tissues. Also, the BmCu/Zn SOD gene was observed in early embryonic stage. Although the roles of SODs remains to be further elucidated, the high expression of BmCu/Zn SOD gene at before 24 h post fertilization suggests that this gene is of general importance during early embryogenesis in the Bombyx mod.

키워드

참고문헌

  1. Arhontaki, K., E. Eliopoulos, G. Goulielmos, P. Kastanis, S. Tsakas, M. Loukas and F. Ayala (2002) Functional con­straints of the Cu,Zn superoxide dismutase in species of the Drosophila melanogaster subgroup and phylogenetic analy­sis. J Mol. Evol. 55(6), 745-56 https://doi.org/10.1007/s00239-002-2370-9
  2. Bannister, J. V., W. H. Bannister and G. Rotilio (1987) Aspects of the structure, function, and applications of superoxide dis­mutase. CRC Crit. Rev. Biochem. 22(2), 111-80 https://doi.org/10.3109/10409238709083738
  3. Bermingham-McDonogh, O., E. B. Gralla and J. S. Valentine (1988) The copper, zinc-superoxide dismutase gene of Sac­charomyces cerevisiae: cloning, sequencing, and biological activity. Proc Natl. Acad. Sci. USA. 85(13), 4789-93
  4. Choudhury, S. B., J. W. Lee, G. Davidson, Y. I. Yim, K. Bose, M. L. Sharma, S. O. Kang, D. E. Cabelli and M. J. Maroney (1999) Examination of the nickel site structure and reaction mechanism in Streptomyces seoulensis superoxide dismu­tase. Biochemistry 38(12), 3744-52 https://doi.org/10.1021/bi982537j
  5. Fleming, J. E., J. Miguel, S. F. Cottrell, L. S. Yengoyan and A. C. Economos (1982) Is cell aging caused by respiration-­dependent injury to the mitochondrial genome. Gerontology 28(1), 44-53 https://doi.org/10.1159/000212510
  6. Fridovich, I. (1978) Superoxide dismutases: defence against endogenous superoxide radical. Ciba Found Symp. 65, 77­-93
  7. Fridovich, I. (1995) Superoxide radical and superoxide dismu­tases. Annu. Rev. Biochem. 65, 77-93
  8. Halliwell, B. and J. M. Gutteridge (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219(1), 1-14 https://doi.org/10.1042/bj2190001
  9. Harman, D. (1981) The aging process. Proc Natl. Acad. Sci. USA. 78(11), 7124-8
  10. Imlay, J. A. and S. Linn (1988) DNA damage and oxygen radical toxicity. Science 240(4857), 1302-9 https://doi.org/10.1126/science.3287616
  11. Lewis, W. R. B., Thomas, J., Peter, L., Elliot, M. and Jim, S. (2002) Principles of Development, Oxford
  12. Li, T., X. Huang, R. Zhou, Y. Liu, B. Li, C. Nomura and J. Zhao (2002) Differential expression and localization of Mn and Fe superoxide dismutases in the heterocystous cyano­bacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 184(18), 5096-103 https://doi.org/10.1128/JB.184.18.5096-5103.2002
  13. Puget, K. and A. M. Michelson (1974) Isolation of a new cop­per-containing superoxide dismutase bacteriocuprein. Bio­chem. Biophys. Res. Commun. 58(3), 830-8 https://doi.org/10.1016/S0006-291X(74)80492-4
  14. Rosen, D. R., T. Siddique, D. Patterson, D. A. Figlewicz, P. Sapp, A. Hentati, D. Donaldson, J. Goto, J. P. O'Regan, H. X. Deng and et al. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lat­eral sclerosis. Nature 362(6415), 59-62 https://doi.org/10.1038/362059a0
  15. Seto, N. O., S. Hayashi and G. M. Tener (1990) Overexpres­sion of Cu-Zn superoxide dismutase in Drosophila does not affect life-span. Proc Natl. Acad. Sci. USA. 87(11), 4270-4
  16. Taniguchi, N. (1992) Clinical significances of superoxide dis­mutases: changes in aging, diabetes, ischemia, and cancer. Adv. Clin. Chem. 29: 1-59 https://doi.org/10.1016/S0065-2423(08)60221-8