Table of Contents Author Guidelines Submit a Manuscript
International Journal of Genomics
Volume 2017, Article ID 7243973, 14 pages
https://doi.org/10.1155/2017/7243973
Research Article

Genome-Wide Identification and Transcriptional Expression Analysis of Cucumber Superoxide Dismutase (SOD) Family in Response to Various Abiotic Stresses

1School of Sciences, Jiangxi Agricultural University, Nanchang, Jiangxi, China
2School of Agriculture, Jiangxi Agricultural University, Nanchang, Jiangxi, China
3Key Laboratory of Crop Physiology, Ecology and Genetic Breeding, Ministry of Education, Jiangxi Agricultural University, Nanchang, Jiangxi, China
4National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural University, Wuhan, China

Correspondence should be addressed to Shiqiang Liu; moc.361@603nh_qsl

Received 25 February 2017; Revised 7 May 2017; Accepted 6 June 2017; Published 20 July 2017

Academic Editor: Graziano Pesole

Copyright © 2017 Yong Zhou et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. G. R. Cramer, K. Urano, S. Delrot, M. Pezzotti, and K. Shinozaki, “Effects of abiotic stress on plants: a systems biology perspective,” BMC Plant Biology, vol. 11, p. 163, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. J. You and Z. Chan, “ROS regulation during abiotic stress responses in crop plants,” Frontiers in Plant Science, vol. 6, p. 1092, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. L. A. Del Rio, “ROS and RNS in plant physiology: an overview,” Journal of Experimental Botany, vol. 66, pp. 2827–2837, 2015. View at Publisher · View at Google Scholar · View at Scopus
  4. R. Mittler, S. Vanderauwera, M. Gollery, and F. Van Breusegem, “Reactive oxygen gene network of plants,” Trends in Plant Science, vol. 9, pp. 490–498, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. J. J. Yan, L. Zhang, R. Q. Wang et al., “The sequence characteristics and expression models reveal superoxide dismutase involved in cold response and fruiting body development in Volvariella volvacea,” International Journal of Molecular Sciences, vol. 17, pp. 34–46, 2016. View at Publisher · View at Google Scholar · View at Scopus
  6. K. Feng, J. Yu, Y. Cheng et al., “The SOD gene family in tomato: identification, phylogenetic relationships, and expression patterns,” Frontiers in Plant Science, vol. 7, p. 1279, 2016. View at Publisher · View at Google Scholar · View at Scopus
  7. I. A. Abreu and D. E. Cabelli, “Superoxide dismutases-a review of the metal-associated mechanistic variations,” Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1804, pp. 263–274, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. K. Asada, K. Yoshikawa, M. Takahashi, Y. Maeda, and K. Enmanji, “Superoxide dismutases from a blue-green alga, Plectonema boryanum,” Journal of Biological Chemistry, vol. 250, pp. 2801–2807, 1975. View at Google Scholar
  9. M. Pilon, K. Ravet, and W. Tapken, “The biogenesis and physiological function of chloroplast superoxide dismutases,” Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol. 1807, pp. 989–998, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. X. Feng, Z. Lai, Y. Lin, G. Lai, and C. Lian, “Genome-wide identification and characterization of the superoxide dismutase gene family in Musa acuminata cv. Tianbaojiao (AAA group),” BMC Genomics, vol. 16, p. 823, 2015. View at Publisher · View at Google Scholar · View at Scopus
  11. R. G. Alscher, N. Erturk, and L. S. Heath, “Role of superoxide dismutases (SODs) in controlling oxidative stress in plants,” Journal of Experimental Botany, vol. 53, pp. 1331–1341, 2002. View at Publisher · View at Google Scholar
  12. I. M. Moller, “Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species,” Annual Review of Plant Physiology and Plant Molecular Biolog, vol. 52, pp. 561–591, 2001. View at Publisher · View at Google Scholar
  13. A. F. Miller, “Superoxide dismutases: ancient enzymes and new insights,” FEBS Letters, vol. 586, pp. 585–595, 2012. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Wuerges, J. W. Lee, Y. I. Yim, H. S. Yim, S. O. Kang, and K. Djinovic Carugo, “Crystal structure of nickel-containing superoxide dismutase reveals another type of active site,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, pp. 8569–8574, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. H. D. Youn, E. J. Kim, J. H. Roe, Y. C. Hah, and S. O. Kang, “A novel nickel-containing superoxide dismutase from Streptomyces spp,” Biochemical Journal, vol. 318, Part 3, pp. 889–896, 1996. View at Publisher · View at Google Scholar
  16. B. Wang, U. Luttge, and R. Ratajczak, “Specific regulation of SOD isoforms by NaCl and osmotic stress in leaves of the C3 halophyte Suaeda salsa L.,” Journal of Plant Physiology, vol. 161, pp. 285–293, 2004. View at Publisher · View at Google Scholar · View at Scopus
  17. V. Srivastava, M. K. Srivastava, K. Chibani et al., “Alternative splicing studies of the reactive oxygen species gene network in Populus reveal two isoforms of high-isoelectric-point superoxide dismutase,” Plant Physiology, vol. 149, pp. 1848–1859, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. W. Feng, W. Hongbin, L. Bing, and W. Jinfa, “Cloning and characterization of a novel splicing isoform of the iron-superoxide dismutase gene in rice (Oryza sativa L.),” Plant Cell Reports, vol. 24, pp. 734–742, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Sunkar, A. Kapoor, and J. K. Zhu, “Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by downregulation of miR398 and important for oxidative stress tolerance,” Plant Cell, vol. 18, pp. 2051–2065, 2006. View at Publisher · View at Google Scholar · View at Scopus
  20. D. V. Dugas and B. Bartel, “Sucrose induction of Arabidopsis miR398 represses two Cu/Zn superoxide dismutases,” Plant Molecular Biology, vol. 67, pp. 403–417, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. S. H. Lee, N. Ahsan, K. W. Lee et al., “Simultaneous overexpression of both CuZn superoxide dismutase and ascorbate peroxidase in transgenic tall fescue plants confers increased tolerance to a wide range of abiotic stresses,” Journal of Plant Physiology, vol. 164, pp. 1626–1638, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. J. J. Molina-Rueda, C. J. Tsai, and E. G. Kirby, “The Populus superoxide dismutase gene family and its responses to drought stress in transgenic poplar overexpressing a pine cytosolic glutamine synthetase (GS1a),” PLoS One, vol. 8, article e56421, 2013. View at Google Scholar
  23. F. Z. Wang, Q. B. Wang, S. Y. Kwon, S. S. Kwak, and W. A. Su, “Enhanced drought tolerance of transgenic rice plants expressing a pea manganese superoxide dismutase,” Journal of Plant Physiology, vol. 162, pp. 465–472, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Wang, X. Zhao, Z. Xiao, X. Yin, T. Xing, and G. Xia, “A wheat superoxide dismutase gene TaSOD2 enhances salt resistance through modulating redox homeostasis by promoting NADPH oxidase activity,” Plant Molecular Biology, vol. 91, pp. 115–130, 2016. View at Publisher · View at Google Scholar · View at Scopus
  25. X. Jing, P. Hou, Y. Lu et al., “Overexpression of copper/zinc superoxide dismutase from mangrove Kandelia candel in tobacco enhances salinity tolerance by the reduction of reactive oxygen species in chloroplast,” Frontiers in Plant Science, vol. 6, p. 23, 2015. View at Publisher · View at Google Scholar · View at Scopus
  26. N. P. Negi, D. C. Shrivastava, V. Sharma, and N. B. Sarin, “Overexpression of CuZnSOD from Arachis hypogaea alleviates salinity and drought stress in tobacco,” Plant Cell Reports, vol. 34, pp. 1109–1126, 2015. View at Publisher · View at Google Scholar · View at Scopus
  27. Y. H. Kim, S. Lim, S. H. Han et al., “Expression of both CuZnSOD and APX in chloroplasts enhances tolerance to sulfur dioxide in transgenic sweet potato plants,” Comptes Rendus Biologies, vol. 338, pp. 307–313, 2015. View at Publisher · View at Google Scholar · View at Scopus
  28. A. Perl, R. Perl-Treves, S. Galili et al., “Enhanced oxidative-stress defense in transgenic potato expressing tomato Cu, Zn superoxide dismutases,” Theoretical and Applied Genetics, vol. 85, pp. 568–576, 1993. View at Publisher · View at Google Scholar · View at Scopus
  29. X. Luo, J. Wu, Y. Li et al., “Synergistic effects of GhSOD1 and GhCAT1 overexpression in cotton chloroplasts on enhancing tolerance to methyl viologen and salt stresses,” PLoS One, vol. 8, article e54002, 2013. View at Publisher · View at Google Scholar · View at Scopus
  30. L. Hu and S. Liu, “Genome-wide analysis of the MADS-box gene family in cucumber,” Genome, vol. 55, pp. 245–256, 2012. View at Publisher · View at Google Scholar · View at Scopus
  31. L. Hu, Y. Yang, L. Jiang, and S. Liu, “The catalase gene family in cucumber: genome-wide identification and organization,” Genetics and Molecular Biology, vol. 39, pp. 408–415, 2016. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Zhou, L. Liu, W. Huang et al., “Overexpression of OsSWEET5 in rice causes growth retardation and precocious senescence,” PLoS One, vol. 9, article e94210, 2014. View at Publisher · View at Google Scholar · View at Scopus
  33. S. Gotz, J. M. Garcia-Gomez, J. Terol et al., “High-throughput functional annotation and data mining with the Blast2GO suite,” Nucleic Acids Research, vol. 36, pp. 3420–3435, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. B. Dehury, K. Sarma, R. Sarmah et al., “In silico analyses of superoxide dismutases (SODs) of rice (Oryza sativa L.),” Journal of Plant Biochemistry and Biotechnology, vol. 22, pp. 150–156, 2013. View at Publisher · View at Google Scholar · View at Scopus
  35. E. Filiz and H. Tombuloğlu, “Genome-wide distribution of superoxide dismutase (SOD) gene families in Sorghum bicolor,” Turkish Journal of Biology, vol. 39, pp. 49–59, 2015. View at Publisher · View at Google Scholar · View at Scopus
  36. J. Zhang, B. Li, Y. Yang et al., “Genome-wide characterization and expression profiles of the superoxide dismutase gene family in Gossypium,” International Journal of Genomics, vol. 2016, Article ID 8740901, 11 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  37. M. W. Parker and C. C. F. Blake, “Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures,” FEBS Letters, vol. 229, pp. 377–382, 1988. View at Publisher · View at Google Scholar · View at Scopus
  38. C. H. Huang, W. Y. Kuo, C. Weiss, and T. L. Jinn, “Copper chaperone-dependent and -independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis,” Plant Physiology, vol. 158, pp. 737–746, 2012. View at Publisher · View at Google Scholar · View at Scopus
  39. X. Feng, F. Chen, W. Liu et al., “Molecular characterization of MaCCS, a novel copper chaperone gene involved in abiotic and hormonal stress responses in Musa acuminata cv. Tianbaojiao,” International Journal of Molecular Sciences, vol. 17, p. 441, 2016. View at Publisher · View at Google Scholar · View at Scopus
  40. D. J. Kliebenstein, R. A. Monde, and R. L. Last, “Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization,” Plant Physiology, vol. 118, pp. 637–650, 1998. View at Publisher · View at Google Scholar
  41. Y. L. Lin and Z. X. Lai, “Superoxide dismutase multigene family in longan somatic embryos: a comparison of CuZn-SOD, Fe-SOD, and Mn-SOD gene structure, splicing, phylogeny, and expression,” Molecular Breeding, vol. 32, pp. 595–615, 2013. View at Publisher · View at Google Scholar · View at Scopus
  42. K. Nath, S. Kumar, R. S. Poudyal et al., “Developmental stage-dependent differential gene expression of superoxide dismutase isoenzymes and their localization and physical interaction network in rice (Oryza sativa L.),” Genes & Genomics, vol. 36, pp. 45–55, 2014. View at Publisher · View at Google Scholar · View at Scopus
  43. W. Wang, M. Xia, J. Chen et al., “Genome-wide analysis of superoxide dismutase gene family in Gossypium raimondii and G. arboreum,” Plant Gene, vol. 6, pp. 18–29, 2016. View at Publisher · View at Google Scholar · View at Scopus
  44. R. C. Fink and J. G. Scandalios, “Molecular evolution and structure―function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases,” Archives of Biochemistry and Biophysics, vol. 399, pp. 19–36, 2002. View at Publisher · View at Google Scholar · View at Scopus
  45. G. Xu, C. Guo, H. Shan, and H. Kong, “Divergence of duplicate genes in exon-intron structure,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, pp. 1187–1192, 2012. View at Publisher · View at Google Scholar · View at Scopus
  46. J. Kurepa, M. V. Montagu, and D. Inzé, “Expression of sodCp and sodB genes in Nicotiana tabacum: effects of light and copper excess,” Journal of Experimental Botany, vol. 48, pp. 2007–2014, 1997. View at Publisher · View at Google Scholar
  47. E. W. Tsang, C. Bowler, D. Herouart et al., “Differential regulation of superoxide dismutases in plants exposed to environmental stress,” Plant Cell, vol. 3, pp. 783–792, 1991. View at Publisher · View at Google Scholar
  48. A. S. Gupta, J. L. Heinen, A. S. Holaday, J. J. Burke, and R. D. Allen, “Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, pp. 1629–1633, 1993. View at Publisher · View at Google Scholar · View at Scopus