DOI QR코드

DOI QR Code

Identification of the genes which related cold (low temperature) stress in Bombyx mori

  • Kang, Min-Uk (Department of Analysis & Certification, FACT) ;
  • Choi, Kwang-Ho (Department of Agricultural Biology, NAAS, RDA) ;
  • Park, Kwan-Ho (Department of Agricultural Biology, NAAS, RDA) ;
  • Nho, Si-Kab (College of Agricultural and Life science, Kyungpook National University)
  • Received : 2016.10.20
  • Accepted : 2016.11.04
  • Published : 2016.12.31

Abstract

Stress may be defined as any modification of environmental parameters that leads to a response by biological organisms. Stresses that affect biolpgical structures may be nonthermal, such as ultraviolet radiation, pH, or salinity, or thermal. Temperture is one of the major stresses that all living organism face. The major effects of cold(low emperature) are decrease of membrane fluidity and the stabilization of secondary structures of RNA and DNA in the cells, which may effect the efficiency of translation, transcription, and DNA replication. In this study, we focus on discovering the genes that are expressed by the cold(low temperature) stress in the silkworm. In cold(low temperature) stress test, we found 100% survive from cold stress at $0^{\circ}C$ up to 12h and $-5^{\circ}C$ up to 2h, and then, survive rate was rapidly decrease in silkworm. Thereafter two whole genes have selected by SSH(Suppression subtractive hybridization). (GenBank accession : GQ149511, GQ338156)

Keywords

References

  1. A. Li, D.L. Denlinger (2008) Rapid cold hardening elicits changes in brain protein profiles of the flesh fly, Sarcophaga crassipalpis., Insect Mol Biol. 17(5), 565-572. https://doi.org/10.1111/j.1365-2583.2008.00827.x
  2. B.J. Sinclair, A.G. Gibbs, S.P. Roberts (2007) Gene transcription during exposure to, and recovery from, cold and desiccation stress in Drosophila melanogaster, Insect Molecular Biology 16(4), 435-443. https://doi.org/10.1111/j.1365-2583.2007.00739.x
  3. Clark M.S., Worland M.R. (2008) How insects survive the cold: molecular mechanisms a review., J Comp Physiol B. Nov, 178(8), 917-933. https://doi.org/10.1007/s00360-008-0286-4
  4. Duman, J.G., Bennett, V., Sformo, T., Hochstrasser, R., Barnes, B.M., (2004) Antifreeze proteins in Alaskan insects and spiders. J. Insect Physiol. 50, 259-266. https://doi.org/10.1016/j.jinsphys.2003.12.003
  5. Dhanikachalam V., Kangayam. M. P., Syed. M. Hussaini Q. (2008) Expression of the Heat Shock Protein Genes in Respons Thermal Stress in the Silkworm Bombyx mori Int. J. Indust. Entomol. 16, 21-27
  6. E. Kristiansen, H. Ramlov, P. Hojrup, S.A. Pedersen, L. Hagen, K.E. Zachariassen, (2011) Structural characteristics of a novel antifreeze protein from the longhorn beetle Rhagium inquisitor. Insect Biochemistry and Molecular Biology 41(2), 109-117 https://doi.org/10.1016/j.ibmb.2010.11.002
  7. Goto S.G. (2001), A novel gene that is up-regulated during recovery from cold shock in Drosophila melanogaster. Gene. 270(1-2), 259-264. https://doi.org/10.1016/S0378-1119(01)00465-6
  8. Herve C., Thi Thuy A. N., Conrad C., Dominique M. Thierry H. (2007) Proteomic profiling of a parasitic wasp exposed to constant and fluctuating cold exposure., Insect Biochemistry and Molecular Biology. 37, 1177-1188. https://doi.org/10.1016/j.ibmb.2007.07.004
  9. Joseph P. R., Rebecca M. R., D.L. Denlinger (2010) Isolation of diapause-regulated genes from the flesh fly, Sarcophaga crassipalpis by suppressive subtractive hybridization, Journal of Insect Physiology 56, 603-609 https://doi.org/10.1016/j.jinsphys.2009.12.007
  10. Lee, R.E., Chen, C.-P. and Denlinger, D.L. (1987) A rapid cold-hardening process in insects. Science. 238, 1415-1417. https://doi.org/10.1126/science.238.4832.1415
  11. N. Guz, U. Toprak, A. Dageri, M. Oktay Gurkan, D. L. Denlinger (2014) Identification of a putative antifreeze protein gene that is highly expressed during preparation for winter in the sunn pest, Eurygaste maura. Journal of Insect Physiology. 68, 30-35. https://doi.org/10.1016/j.jinsphys.2014.06.021
  12. Qi Xu, Qi Zou, Huizhen Zheng, Fan Zhang, Bin Tang, Shigui Wan, (2011) Three heat shock proteins from Spodoptera exigua: Gene cloning, characterization and comparative stress response during heat and cold shocks. Comparative Biochemistry and Physiology, Part B 159, 92-102.
  13. Raymond, J.A., DeVries, A.L. (1977) Adsorption inhibition as a mechanism of freezing resistance in polar fishes. Proc. Natl. Acad. Sci. U.S.A. 74, 2589-2593. https://doi.org/10.1073/pnas.74.6.2589
  14. Robert C. R., John C. A., Connie E. S. Jennifer K., Michael E. R., William R. D., K. Vanya E. (2008) Seasonal expressed sequence tags of rainbow smelt (Osmerus mordax) revealed by subtractive hybridization and the identification of two genes up-regulated during winter. Gene. 424, 56-62. https://doi.org/10.1016/j.gene.2008.08.002
  15. Shu-Xia Yi., Richard E. Lee Jr. (2011) Rapid cold-hardening blocks cold-induced apoptosis by inhibiting the activation of pro-caspases in the flesh fly Sarcophaga crassipalpis. Apoptosis 16, 249-255. https://doi.org/10.1007/s10495-010-0570-0
  16. Takumi K., Yukio I. (2009) Chaperonin contributes to cold hardiness of the onion Maggot Delia antiqua through repression of depolymerization of actin at low temperatures. PLoS ONE. 4(12), e8277(1-7)
  17. Yi SX, Moore CW, Lee RE Jr. (2007) Rapid cold-hardening protects Drosophila melanogaster from cold-induced apoptosis. Apoptosis. 12(7), 1183-93. https://doi.org/10.1007/s10495-006-0048-2
  18. Yoriko M., Teruyuki N., Okitsugu Y., Toshinobu Y. (2001) Samui, a novel cold-inducible gene, encoding a protein with a BAG domain similar to silencer of death domains (SODD/BAG-4), isolated from Bombyx diapause eggs. Eur. J. Biochem. 268, 3432-3442 https://doi.org/10.1046/j.1432-1327.2001.02244.x
  19. Zachariassen, K.E., Husby, J.A. (1982) Antifreeze effect of thermal hysteresis agents protects highly supercooled insects. Nature 298, 865-867. https://doi.org/10.1038/298865a0