DOI QR코드

DOI QR Code

Isolation and Characterization of Glycolate Oxidase Gene from Panax ginseng C. A. Meyer

  • Parvin, Shohana (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Pulla, Rama Krishna (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Kim, Yu-Jin (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Sathiyaraj, Gayathri (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Jung, Seok-Kyu (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Khorolragchaa, Altanzul (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • In, Jun-Gyo (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University) ;
  • Yang, Deok-Chun (Korean Ginseng Center for Most Valuable Products and Ginseng Genetic Resource Bank, Kyung Hee University)
  • 발행 : 2009.12.31

초록

The oxidation of glycolate to glyoxylate, a key step in plant photorespiration, is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15). To investigate the altered gene expression and the role of GOX in ginseng plant defense system, a cDNA clone containing a GOX gene designated as PgGOX was isolated and sequenced from Panax ginseng. The cDNA was 692 nucleotides long and have an open reading frame of 552 bp with a deduced amino acid sequence of 183 residues. A GenBank BlastX search revealed that the deduced amino acid of PgGOX shares a high degree homology with the Glycine max (95% identity). In the present study we analyzed the expression of PgGOX under various environmental stresses at different times using real time-PCR. The results showed that the expressions of PgGOX increased after various treatments involving salt, light, cold, ABA, SA, and copper treatment.

키워드

참고문헌

  1. Macheroux P, Massey V, Thiele DJ. Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization. Biochemistry 30: 4612-4619 (1991). https://doi.org/10.1021/bi00232a036
  2. Sharkey TD. Estimating the rate of photorespiration in leaves. Physiologia Plantaurm 73: 147-152 (1988). https://doi.org/10.1111/j.1399-3054.1988.tb09205.x
  3. Boldt R, Edner C, Kolukisaoglu U, Hagemann M, Weckwerth W, Wienkoop S, Morgenthal K and Bauwe H. D-Glycerate 3-kinase, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family. Plant Cell 17: 2413-2420 (2005). https://doi.org/10.1105/tpc.105.033993
  4. Keys AJ. The re-assimilation of ammonia produced by photorespiration and the nitrogen economy of C3 higher plants. Photosynthesis Research 87: 165-175 (2006). https://doi.org/10.1007/s11120-005-9024-x
  5. Rachmilevitch S, Cousins AB and Bloom AJ. Nitrate assimilation in plant shoots depends on photorespiration. Proc Natl Acad Sci USA 101: 11506-11510 (2004). https://doi.org/10.1073/pnas.0404388101
  6. Moreno JI, Martin R, Castresana C. Arabidopsis SHMT1, a serine hydroxyl methyltransferase that functions in the photo respiratory pathway influences resistance to biotic and abiotic stress. Plant Journal 41: 451-463 (2005). https://doi.org/10.1111/j.1365-313X.2004.02311.x
  7. Verslues PE, Kim, YS, Zhu JK. Altered ABA, proline and hydrogen peroxide in an Arabidopsis glutamate: glyoxylate aminotransferase mutant. Plant Molecular Biology 64: 205- 217 (2007). https://doi.org/10.1007/s11103-007-9145-z
  8. Somerville CR. An early Arabidopsis demonstration: resolving a few issues concerning photorespiration. Plant Physiology 125: 20-24 (2001). https://doi.org/10.1104/pp.125.1.20
  9. Holger F, Telma ES, Estela MV, Ulf-Ingo F, Veronica GM. Generation of hydrogen peroxide in chloroplasts of Arabidopsis overexpressing glycolate oxidase as an inducible system to study oxidative stress. Plant Physiology 148: 719-729 (2008). https://doi.org/10.1104/pp.108.126789
  10. Simon B, Ali N, Yair H, Micha V. Transcriptional and posttranscriptional regulation of the glycolate oxidase gene in tobacco seedlings. Plant Molecular Biology 45: 399-407 (2001). https://doi.org/10.1023/A:1010688804719
  11. Goyal A. Effects of water stress on glycolate metabolism in the leaves of rice seedlings (Oryza sativa). Physiol Plantarum 69: 289-294 (1987). https://doi.org/10.1111/j.1399-3054.1987.tb04289.x
  12. Kim JH and Nah SY. Effects of ginsenoside $Rg_3$ epimers on swine coronary artery contractions. J Ginseng Res. 29(3): 119-125 (2005). https://doi.org/10.5142/JGR.2005.29.3.119
  13. Kook S, Han HK, Kim GH, Choi K. The anti-hepatotoxic effect of ginseng in rats: meta–-analysis. J Ginseng Res. 32(2): 161-170 (2008). https://doi.org/10.5142/JGR.2008.32.2.161
  14. Kim YJ, Ham AR, Shim JS, Lee JH, Jung DY, In JG, Lee BS, Yang DC. Isolation and characterization of trepene synthase gene from Panax ginseng. J Ginseng Res. 32(2): 114-119 (2008). https://doi.org/10.5142/JGR.2008.32.2.114
  15. Parvin S, Pulla RK, Shim JS, Kim YJ, Jung DY, Yang DC. Isolation and Characterization of Cinnamoyl-CoA Reductase Gene from Panax ginseng C. A. Meyer. J Ginseng Res. 32(3): 232-237 (2008). https://doi.org/10.5142/JGR.2008.32.3.232
  16. Morris PC, Kumar A, Bowles DJ, Cuming AC. Osmotic stress and abscisic acid regulate the expression of the Em gene of wheat. Eur J Biochem. 190: 625-30(1990). https://doi.org/10.1111/j.1432-1033.1990.tb15618.x
  17. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 157: 105-32 (1982). https://doi.org/10.1016/0022-2836(82)90515-0
  18. Gould SJ, Keller GA, Subramani S. Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase. J Cell Biol. 105: 2923-2931 (1987). https://doi.org/10.1083/jcb.105.6.2923
  19. Ow DW, Wood KV, DeLuca M, DeWet JR, Helinski DR, Howell SH. Transient and stable expression of the firefly luciferase gene in plant cells and transgenic plants. Science 234: 856-859 (1986). https://doi.org/10.1126/science.234.4778.856
  20. Borst P. Peroxisome biogenesis revisited. Biochim Biophys Acta 1008: 1-13 (1989).
  21. Smith SM, Leaver CJ. Glyoxysomal malate synthase of cucumber: molecular cloning of a cDNA and regulation of enzyme synthesis during germination. Plant Physiol. 81: 762-767 (1986). https://doi.org/10.1104/pp.81.3.762
  22. Kindl H. 3-Oxidation of fatty acids by specific organelles. In: Stumpf PK, Conn EE (ed), The Biochemistry of Plants, Academic Press, London 31-52 (1987).
  23. Beeching JR, Northcote DH. Nucleic acid (cDNA) and amino acid sequences of isocitrate lyase from castor bean. Plant Mol Biol. 8: 471-475 (1987). https://doi.org/10.1007/BF00017992
  24. Greenler JM, Sloan JS, Schwartz BW, Becker WM. Isolation, characterization and sequence analysis of a full length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber. Plant Mol Biol. 13: 139-150 (1989). https://doi.org/10.1007/BF00016133
  25. Shin K, Mary AC, Inna A, Davina B, Monica F, Elizabeth John C, Cushman C. Transcript profiling of salinity stress responses by large-scale expressed sequence tag analysis in Mesembryanthemum crystallinum. Gene 341: 83-92 (2004). https://doi.org/10.1016/j.gene.2004.06.037
  26. Park YS, Jin YH, Kim YC, Choi JD, Cho NJ. Effects of light on spinach glycolate oxidase gene expression. J Biochem Mol Biol. 28: 271-274 (1995).
  27. Bertoni GP, Becker WM. Effects of light fluence and wavelength on expression of the gene encoding cucumber hydroxypyruvate reductase. Plant Physiol. 103: 933-941 (1993). https://doi.org/10.1104/pp.103.3.933
  28. Tchang F, Lecharny A, Mazliak P. Photo stimulation of hydroxypyruvate reductase activity in peroxisomes of Pharbitisnil seedlings. I. Action spectrum. Plant Cell Physiol. 25: 1033-1037 (1984).
  29. Verniquet F, Gaillard J, Neuburger M, Douce R. Rapid inactivation of plant aconitase by hydrogen peroxide. Biochem J. 276: 643-648 (1991).
  30. Thimm O, Essigmann B, Kloska S, Altmann T, Buckhou TJ. Response of Arabidopsis to iron deficiency stress as revealed by microarray analysis. Plant Physiology 127: 1030-1043 (2001). https://doi.org/10.1104/pp.010191
  31. Mahour K, Saxena PN. Scavenging strategy of Panax ginseng against formed free radicals under stress of mercuric chloride in Ratus novegicus. J Ginseng Res. 32(2): 150-154 (2008). https://doi.org/10.5142/JGR.2008.32.2.150

피인용 문헌

  1. Transcript profiling of antioxidant genes during biotic and abiotic stresses in Panax ginseng C. A. Meyer vol.38, pp.4, 2011, https://doi.org/10.1007/s11033-010-0421-7
  2. Classification and characterization of putative cytochrome P450 genes from Panax ginseng C. A. Meyer vol.76, pp.12, 2011, https://doi.org/10.1134/S000629791112008X
  3. Influence of potassium nitrate on antioxidant level and secondary metabolite genes under cold stress in Panax ginseng vol.59, pp.3, 2012, https://doi.org/10.1134/S1021443712030041
  4. Overexpression of geraniol 10-hydroxylase from Panax ginseng conferred enhanced resistance to Pseudomonas syringae in Arabidopsis vol.81, pp.2, 2017, https://doi.org/10.1007/s10725-016-0207-6