Skip to main content
Log in

Molecular Cloning, Expression Analysis, and Preliminarily Functional Characterization of the Gene Encoding Protein Disulfide Isomerase from Jatropha curcas

  • Published:
Applied Biochemistry and Biotechnology Aims and scope Submit manuscript

Abstract

Reactive oxygen species (ROS) in plants, arising from various environmental stresses, impair the thiol-contained proteins that are susceptible to irregular oxidative formation of disulfide bonds, which might be alleviated by a relatively specific modifier called protein disulfide isomerase (PDI). From our previous data of the transcriptome and digital gene expression of cold-hardened Jatropha curcas, a PDI gene was proposed to be cold-relevant. In this study, its full-length cDNA (JcPDI) was cloned, with the size of 1649 bp containing the entire open reading frame (ORF) of 1515 bp. This ORF encodes a polypeptide of 504 amino acids with theoretical molecular weight of 56.6 kDa and pI value of 4.85. One N-terminal signal peptide (−MASKGSIWSCMFLFSLI VAISAGEG-) and the C-terminal anchoring sequence motif (−KDEL-) specific to the endoplasmic reticulum, as well as two thioredoxin domains (−CGHC-), are also found by predictions. Through semi-quantitative RT-PCR, the expression of JcPDI was characterized to be tissue-differential strongly in leaves and roots, but weakly in stems, and of cold-induced alternations. Furthermore, JcPDI overexpression in yeast could notably enhance the cold resistance of host cells. Conclusively, these results explicitly suggested a considerable association of JcPDI to cold response and a putative application potential for its correlated genetic engineering.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

References

  1. Fairless, D. (2007). Biofuel: the little shrub that could maybe. Nature, 449, 652–655.

    Article  Google Scholar 

  2. Yang, C. Y., Fang, Z., Li, B., & Long, Y. F. (2012). Review and prospects of Jatropha biodiesel industry in China. Renewable and Sustainable Energy Reviews, 16, 2178–2190.

    Article  CAS  Google Scholar 

  3. Openshaw, L. (2000). A review of Jatropha curcas: an oil plant of unfulfilled promise. Biomass and Bioenergy, 19, 1–15.

    Article  Google Scholar 

  4. Lin, J., Zhou, X., Tang, K. X., & Chen, F. (2004). A survey of the studies on the resources of Jatropha curcas L. Journal of Tropical and Subtropical Botany, 12, 285–290.

    CAS  Google Scholar 

  5. Khan, H. A., & Mutus, B. (2014). Protein disulfide isomerase a multifunctional protein with multiple physiological roles. Frontiers in Chemistry. doi:10.3389/fchem.2014.00070.

    Google Scholar 

  6. Appenzeller-Herzog, C., & Ellgaard, L. (2008). In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and doxidized forms. Antioxidants and Redox Signaling, 10, 55–64.

    Article  CAS  Google Scholar 

  7. Nardai, G., Braun, L., Csala, M., Mile, V., Csermely, P., Benedetti, A., Mandl, J., & Banhegyi, G. (2001). Protein disulfide isomerase and protein thiol-dependent dehydroascorbate reduction and aseorbate accumulation in the lumen of the endoplasmic reticulum. Journal of Biological Chemistry, 276, 8825–8828.

    Article  CAS  Google Scholar 

  8. Wang, H. B., Zou, Z. R., Wang, S. S., & Gong, M. (2013). Global analysis of transcriptome responses and gene expression profiles to cold stress of Jatropha curcas L. PLoS One, 12, e82817.

    Article  Google Scholar 

  9. Wang, H. B., Zou, Z. R., Wang, S. S., & Gong, M. (2014). Deep sequencing-based transcriptome analysis of the oil-bearing plant Physic Nut (Jatropha curcas L.) under cold stress. Plant Omics Journal, 7, 178–187.

    Google Scholar 

  10. Li, Z. G., & Gong, M. (2011). Effects of different chemical disinfectant on seed germination and seedling growth of Jatropha curcas L. Seed, 30(4–7), 12.

    Google Scholar 

  11. Ao, P. X., Li, Z. G., Fan, D. M., & Gong, M. (2013). Involvement of antioxidant defense system in chill hardening-induced chilling tolerance in Jatropha Curcas seedlings. Acta Physiologiae Plantarum, 35, 153–160.

    Article  CAS  Google Scholar 

  12. Ao, P. X., Li, Z. G., & Gong, M. (2013). Involvement of compatible solutes in chill hardening-induced chilling tolerance in Jatropha curcas seedlings. Acta Physiologiae Plantarum, 35, 3457–3464.

    Article  CAS  Google Scholar 

  13. Jaspers, P., & Kangasjarvi, J. (2010). Reactive oxygen species in abiotic stress signaling. Physiologia Plantarum, 138, 405–413.

    Article  CAS  Google Scholar 

  14. Han, X. H., Wang, Y. H., Liu, X., Jiang, L., Ren, Y. L., Liu, F., Peng, C., Li, J. J., Jin, X. M., Wu, F. Q., Wang, J. L., Guo, X. P., Zhang, X., Cheng, Z. J., & Wan, J. M. (2012). The failure to express a protein disulphide isomerase-like protein results in a floury endosperm and an endoplasmic reticulum stress response in rice. Journal of Experimental Botany, 63, 121–130.

    Article  CAS  Google Scholar 

  15. Houston, N. L., Fan, C., Xiang, J. Q., Schulze, J. M., Jung, R., & Boston, R. S. (2005). Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiology, 137, 762–778.

    Article  CAS  Google Scholar 

  16. Lu, D. P., & Christopher, D. A. (2008). Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZIP60 modulates the response in Arabidopsis thaliana. Molecular Genetics and Genomics, 280, 199–210.

    Article  CAS  Google Scholar 

  17. Selles, B., Jacquot, J. P., & Rouhier, N. (2011). Comparative genomic study of protein disulfide isomerases from photosynthetic organisms. Genomics, 97, 37–50.

    Article  CAS  Google Scholar 

  18. Ondzighi, C. A., Christopher, D. A., Cho, E. J., Cho, E. J., Chang, S. C., & Staehelin, L. A. (2008). Arabidopsis protein disulfide isomerase-5 inhibits cysteine proteases during trafficking to vacuoles before programmed cell death of the endothelium in developing seeds. Plant Cell, 20, 2205–2220.

    Article  CAS  Google Scholar 

  19. Huang, D. J., Chen, H. J., & Lin, Y. H. (2005). Isolation and expression of protein disulfide isomerase cDNA from sweet potato (Ipomoea batatas L. Lam ‘Tainong 57’) storage roots. Plant Science, 169, 776–784.

    Article  CAS  Google Scholar 

  20. Liu, Y. H., Wang, X. T., Shi, Y. S., Huang, Y. Q., Song, Y. C., Wang, T. Y., & Li, Y. (2009). Expression and characterization of a protein disulfide isomerases in maize (Zea mays L.). Chinese Journal of Biochemistry and Molecular Biology, 25, 229–234.

    Article  CAS  Google Scholar 

  21. Chen, Y. A., Chi, W. C., Huang, T. L., Lin, C. Y., Quynh Nguyeh, T. T., Hsiung, Y. C., Chia, L. C., & Huang, H. J. (2012). Mercury-induced biochemical and proteomic changes in rice roots. Plant Physiology and Biochemistry, 55, 23–32.

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by several grants from the National Foundations of Natural Sciences, China (No. 31260064, 31460059, 31460179) and the Education Bureau of Yunnan Province (No. ZD2010004).

Ethical statement

This research did not include vertebrate studies or animal experiments and field studies, without any ethical risks. Our academic lab does not locate in the protected area, and no specific permissions are required.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Ming Gong.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Wang, H., Zou, Z. & Gong, M. Molecular Cloning, Expression Analysis, and Preliminarily Functional Characterization of the Gene Encoding Protein Disulfide Isomerase from Jatropha curcas . Appl Biochem Biotechnol 176, 428–439 (2015). https://doi.org/10.1007/s12010-015-1585-3

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12010-015-1585-3

Keywords

Navigation