Identification of GST Interacted Proteins under PRSV Infected Papaya Using Affinity Purification–mass Spectrometry
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Published:
Jul 21, 2020
Keywords:
Carica papaya Glutathione S-transferase AP-MS Protein-protein interactions
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Abstract
Glutathione S-transferases (GSTs) are multifunctional proteins involved in stress metabolism, which play major roles in biotic and abiotic stress responses. GSTs have found in all organisms which is a major phase II detoxification enzymes found in the cytosol. GSTs regulate peroxidase and isomerase activities, they protect cells against H(2)O(2)-induced cell death. Papaya rigsport virus (PRSV) is one of main biotic agent that cause damage in papaya. The disease symptoms are mosaic, chrolosis, ring spot and stunt, all the symptoms are the early stage of cell death. The main point of this research to investigate protein interaction of the PRSV interacted plant proteins and GSTs recombinant protein using the classical Affinity-purification-mass spectrometry (AP-MS) approache. The GST protein was heterologous expressed in E.coli system and the pull down assay was applied to expore the protein interacted complexs after that the protein complexs were indentified by LC-MS/ MS. CTC1, Protein CCA1 isoform X1, Tetratricopeptide repeat (TPR)-like superfamily protein, PHD finger protein ALFIN-LIKE 9 and Fructose-bisphosphate aldolase-lysine N-methyltransferase proteins were identified. The interacted five proteins were predicted the protein network by STITCH program, the result show they associated with oxidative stress response mechanism. However, this is the basic intensive information that could develop to manufacture PRSV resistance variety in the future.
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Sawwa, A., Yingchutrakul, Y., Roytrakul, S., Siriwan, W., & Chowpongpang, S. (2020). Identification of GST Interacted Proteins under PRSV Infected Papaya Using Affinity Purification–mass Spectrometry. Applied Science and Engineering Progress, 13(3), 224–232. Retrieved from https://ph02.tci-thaijo.org/index.php/ijast/article/view/241542
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References
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[30] K. A. Boltz, K. Leehy, X. Song, A. D. Nelson, and D. E. Shippen, “ATR cooperates with CTC1 and STN1 to maintain telomeres and genome integrity in Arabidopsis,” Molecular Biology of the Cell, vol. 23, pp. 1558–1568, Feb. 2012.
[31] J. R. Lee, X. Xie, K.Yang, J. Zhang, S. Y. Lee, and D. E. Shippen,“Dynamic interactions of Arabidopsis TEN1: Stabilizing telomeres in response to heat stress,” The Plant Cell, vol. 28, no. 9, pp. 2212–2224, Sep. 2016.
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[37] Q. Wang, J. Liu, Y. Wang, Y. Zhao, H. Jiang, and B. Cheng, “Systematic analysis of the maize PHD-finger gene family reveals a subfamily involved in abiotic stress response,” International Journal of Molecular Sciences, vol. 16, no. 10, pp. 23517–23544, Oct. 2015.
[38] M. Kuhn, C. Mering, M. Campillos, L. J. Jensen, and P. Bork, “STITCH: Interaction networks of chemicals and proteins,” Nucleic Acids Research, vol. 36, pp. D684–D688, Dec. 2008.
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[41] J. Fang, A. Lin, W. Qiu, H. Cai, M. Umar, R. Chen, and R. Ming, “Transcriptome profiling revealed stress-induced and disease resistance genes up-regulated in PRSV resistant transgenic papaya,” Frontiers in Plant Science, vol. 7, p. 855, Jun. 2016.
[2] S. U. Chalak, S. N. Hasbnis, and V. S. Supe, “Papaya ringspot disease management: A review,” Journal of Pharmacognosy and Phytochemistry, vol. 6, no. 5, pp. 1911–1914, Aug. 2017.
[3] S. D. Yeh and D. Gonsalves, “Practices and perspective of control of Papaya ringspot virus by cross protection,” in Advances in Disease Vector, New York: Springer, 1994, pp. 237–257.
[4] D. Gonsalves, J. Y. Suzuki, S. Tripathi, and S. A. Ferreira, “Papaya ringspot virus,” in Encyclopedia of Virology. 3rd ed., Amsterdam, Netherlands: Elsevier Ltd., 2008, pp. 1–8.
[5] S. Sakuanrungsirikul, N. Sarindu, V. Prasartsee, S. Chaikiatiyos, R. Siriyan, M. Sriwatanakul, P. Lekananon, C. Kitprasert, P. Boonsong, P. Kosiyachinda, G. Fermin, and D. Gonsalves, “Update on the development of virus-resistant papaya: Virus-resistant transgenic papaya for people in rural communities of Thailand,” Food and Nutrition Bulletin, vol. 26, no. 4, pp. 422–426, Dec. 2005.
[6] E. Nutricati, A. Miceli, F. Blando, and L. De Bellis, “Characterization of two Arabidopsis thaliana glutathione S-transferases,” Plant Cell Reports, vol. 25, pp. 997–1005, Sep. 2006.
[7] S. Mohsenzadeh, M. Esmaeili, F. Moosavi, M. Shahrtash, B. Saffari, and H. Mohabatkar, “Plant glutathione S-transferase classification, structure and evolution,” African Journal of Biotechnology, vol. 10, no. 42, pp. 8160–8165, Aug. 2011.
[8] E. Chronopoulou, N. Georgakis, I. Nianiou-Obeidat, P. Madesis, F. Perperopoulou, F. Pouliou, E. Vasilopoulou, E. Ioannou, F. S. Ataya, and N. E. Labrou, “Plant glutathione transferases in abiotic stress response and herbicide resistance,” in Glutathione in Plant Growth, Development, and Stress Tolerance. New York: Springer, 2017, pp. 215–233.
[9] S. Kumar and P. K. Trivedi, “Glutathione S-transferases: Role in combating abiotic stresses including arsenic detoxification in plants,” Frontiers in Plant Science, vol. 9, p. 751, Jun. 2018.
[10] P. Braun, A. Sebastien, V. L. Jelle, D. J. Geert, and L. Claire, “Plant protein interactomes,” Annual Review of Plant Biology, vol. 64, no. 1, pp. 161–187, Jan. 2013.
[11] A. Bauer and B. Kuter, “Affinity purificationmass spectrometry. Powerful tools for the characterization of protein complexes,” European Journal of Biochemistry, vol. 270, no. 4, pp. 570– 578, Feb. 2003.
[12] W. H. Dunham, M. Mullin, and A. C. Gingras, “Affinity-purification coupled to mass spectrometry: Basic principles and strategies,” Proteomics, vol. 12, no. 10, pp. 1576–1590, May. 2012.
[13] J. H. Morris, G. M. Knudsen, E. Verschueren, J. R. Johnson, P. Cimermancic, A. L. Greninger, and A. R. Pico, “Affinity purification-mass spectrometry and network analysis to understand proteinprotein interactions,” Nature Protocol, vol. 9, no. 11, pp. 2539–2554, Oct. 2014.
[14] Y. Zhang, P. Gao, and J. S. Yuan, “Plant proteinprotein interaction network and interactome,” Current Genomics, vol. 11, no. 1, pp. 40–46, Mar. 2010.
[15] Y. Fukao, “Protein-protein interactions in plants,” Plant and Cell Physiology, vol. 53, pp. 617–625, Apr. 2012.
[16] F. U. Joachim, “Protein interaction networks in plants,” Planta, vol. 224, pp. 771–781, Mar. 2006.
[17] J. Chumpookam, H. L. Lin, and C. C. Shiesh, “Effect of smoke-water on seed germination and seedling growth of papaya (Carica papaya cv. Tainung no. 2),” HortScience, vol. 47, pp. 741–744, Jun. 2012.
[18] H. G. Pennington, D. M. Gheorghe, A. Damerum, C. Pliego, P. D. Spanu, R. Cramer, and L. V. Bindschedler, “Interactions between the powdery mildew effector BEC1054 and barley proteins identify candidate host targets,” Journal of Proteome Research, vol. 4, pp. 826–839, Feb. 2016.
[19] D. Szklarczyk, A. Santos, C. Mering, L. J. Jensen, P. Bork, and M. Kuhn, “STITCH 5: Augmenting protein–chemical interaction networks with tissue and affinity data,” Nucleic Acids Research, vol. 44, pp. 380–384, Nov. 2016.
[20] S. Harper and D. W. Speicher, “Purification of proteins fused to glutathione S-tranferase,” Methods in Molecular Biology, vol. 681, pp. 259–280, Feb. 2011.
[21] R. Edwards, D. P. Dixon, and V. Walbot, “Plant glutathione S-transferases: Enzymes with multiple functions in sickness and in health,” Trends Plant Science, vol. 5, pp. 193–198, May 2000.
[22] E. Chronopoulou, N. Georgakis, I. Nianiou, P. Madesis, F. Perperopoulou, F. Pouliou, E. Vasilopoulou, E. Loannou, F. S. Ataya, and N. Labrou, “Plant glutathione transferases in abiotic stress response and herbicide resistance,” in Glutathione in Plant Growth, Development, and Stress Tolerance. New York: Springer, 2017, pp. 215–233.
[23] H. Gong, Y. Jiao, W. Hu, and E. Pua, “Expression of glutation-S-transferase and its role in plant growth and development in vivo and shoot morphogenesis in vitro,” Plant Molecular Biology, vol. 57, pp. 53–66, Jan. 2005.
[24] T. Kiyosue, K. Yamaguchi-Shinozaki, and K. Shinozaki, “Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible genes that encode putative glutathione S-transferase in Arabidopsis thaliana L,” FEBS Letters, vol. 335, pp. 189–192, Dec. 1993.
[25] L. Loyall, K. Uchida, S. Braun, M. Furuya, and H. Frohnmeyer, “Glutathione and a UV lightinduced glutathione S-transferase are involved in signaling to chalcone synthase in cell cultures,” Plant Cell, vol. 12, pp. 1939–1950, Oct. 2000.
[26] J. V. Anderson and D. G. Davis, “Abiotic stress alters transcript profiles and activity of glutathione S-transferase, glutathione peroxidase, and glutathione reductase in Euphorbia esula,” Physiologia Plantarum, vol. 120, pp. 421–433, Feb. 2004.
[27] J. Zhou and P. B. Goldsbrough, “An Arabidopsis gene with homology to glutathione S-transferase is regulated by ethylene,” Plant Molecular Biology, vol. 22, pp. 517–523, Mar. 1993.
[28] N. Zeytuni and R. Zarivach, “Structural and functional discussion of the Tetra-Trico-Peptide repeat, a protein interaction module,” Structure, vol. 20, no. 3, pp. 397–405, Mar. 2012.
[29] M. Mininno, S. Brugière, V. Pautre, A. Gilgen, S. Ma, M. Ferro, M. Tardif, C. Alban, and S. Ravanel, “Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants,” The Journal of Biological Chemistry, vol. 287, no. 25, pp. 21034–21044, Apr. 2012.
[30] K. A. Boltz, K. Leehy, X. Song, A. D. Nelson, and D. E. Shippen, “ATR cooperates with CTC1 and STN1 to maintain telomeres and genome integrity in Arabidopsis,” Molecular Biology of the Cell, vol. 23, pp. 1558–1568, Feb. 2012.
[31] J. R. Lee, X. Xie, K.Yang, J. Zhang, S. Y. Lee, and D. E. Shippen,“Dynamic interactions of Arabidopsis TEN1: Stabilizing telomeres in response to heat stress,” The Plant Cell, vol. 28, no. 9, pp. 2212–2224, Sep. 2016.
[32] Y. Wang and W. Chai, “Pathogenic CTC1 mutations cause global genome instabilities under replication stress,” Nucleic Acids Research, vol. 46, no. 8, pp. 3981–3992, May 2018.
[33] L. Chen, J. Majerska, and J. Lingner, “Molecular basis of telomere syndrome caused by CTC1 mutations,” Genes and Development, vol. 27, pp. 2099–2108, Sep. 2013.
[34] P. J. Seo and P. Mas, “Stressing the role of the plant circadian clock,” Trends in Plant Science, vol. 20, pp. 230–237, Apr. 2015.
[35] Y. Song, Y. Jiang, B. Kuai, and L. Li, “Circadian clock-associated 1 inhibits leaf senescence in Arabidopsis,” Frontiers in Plant Science, vol. 9, pp. 280, Mar. 2018.
[36] M. Bienz, “The PHD finger, a nuclear proteininteraction domain,” Trends in Biochemical Sciences, vol. 31, pp. 35–40, Jan. 2006.
[37] Q. Wang, J. Liu, Y. Wang, Y. Zhao, H. Jiang, and B. Cheng, “Systematic analysis of the maize PHD-finger gene family reveals a subfamily involved in abiotic stress response,” International Journal of Molecular Sciences, vol. 16, no. 10, pp. 23517–23544, Oct. 2015.
[38] M. Kuhn, C. Mering, M. Campillos, L. J. Jensen, and P. Bork, “STITCH: Interaction networks of chemicals and proteins,” Nucleic Acids Research, vol. 36, pp. D684–D688, Dec. 2008.
[39] M. W. Hameed, “Hypoxia up-regulates mitochondrial genome-encoded transcripts in Arabidopsis roots,” Genes and Genetic Systems, vol. 90, pp. 325–334, Apr. 2015.
[40] T. Fukao and J. Bailey-Serres, “Plant responses to hypoxia; is survival a balancing act,” Trends in Plant Science, vol. 9, no. 9, pp. 449–456, Sep. 2004.
[41] J. Fang, A. Lin, W. Qiu, H. Cai, M. Umar, R. Chen, and R. Ming, “Transcriptome profiling revealed stress-induced and disease resistance genes up-regulated in PRSV resistant transgenic papaya,” Frontiers in Plant Science, vol. 7, p. 855, Jun. 2016.