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研究生:陶櫻園
研究生(外文):Dao Thi Ngoc Nuong
論文名稱:Oryzasin 1 在水稻種子耐熱性之功能分析
論文名稱(外文):Functional Analysis of Oryzasin 1 in Thermotolerance of Rice
指導教授:葉靖輝
指導教授(外文):Ching-Hui Yeh
學位類別:碩士
校院名稱:國立中央大學
系所名稱:生命科學系
學門:生命科學學門
學類:生物學類
論文出版年:2020
畢業學年度:108
語文別:英文
論文頁數:66
中文關鍵詞:Oryzasin 1
外文關鍵詞:Functional Analysis of Oryzasin 1 in Thermotolerance of Rice
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Aspartic proteases(APs)是一種蛋白水解酶,其廣泛存在於所有生物中。數種AP已被證明對於應對生物和非生物逆境至關重要。熱逆境是影響植物生長發育的主要非生物逆境。透過蛋白質體學,我們發現水稻AP的Oryzasin 1與水稻第一族群小分子量熱休克蛋白質Oshsp16.9A在高溫下有相互作用。為了探討Oryzasin 1在水稻耐熱性中的作用,我們將OsAP基因轉入水稻基因組中,以建立過量表現Oryzasin 1的水稻轉植株並以PCR確認是否成功,以供進一步研究。獲得Oryzasin 1過量表現轉植株(OsAP-OEs)後,我們比較了轉植株與野生型(WT)在高溫下的種子發芽率及幼苗存活率。研究成果表明,在熱處理條件下,OsAP-OE轉殖株的種子發芽率和幼苗存活率更高,與野生型相比,在耐熱性方面有顯著提升。此外,我們測量OsAP-OE轉殖株與WT種子在熱處理後的TTC還原活性(TTC reduction activity)和電解質滲漏率(electrolyte leakage)。TTC還原活性實驗中,WT經熱處理後喪失還原能力,而OsAP-OE轉植株仍然能將TTC還原。在電解質滲漏實驗中,熱處理對OsAP-OE轉植株的影響比WT小,代表OsAP-OE的細胞膜受損較少。最後,我們比較了OsAP-OE轉植株與WT的花粉在高溫處理後的存活率,而OsAP-OE轉植株亦取得較好的表現。綜合上述研究,我們證實OsAP能夠正向調控水稻的耐熱性,使OsAP-OE轉植株擁有較好的耐熱表現
Aspartic proteases (APs) are a group of proteolytic enzymes that are broadly distributed in all organisms. Several APs have been demonstrated to be essential for responses to biotic and abiotic stresses. Heat stress is the major abiotic stress seriously influencing plant growth and development. Using proteomic approaches, we found the interplay between oryzasin 1, a rice AP, and Oshsp16.9A, a rice class I small heat shock protein, in rice seeds during high temperature. Here, we are trying to characterize the role of oryzasin 1 in thermotolerance of rice seeds. We inserted oryzasin 1 gene into the rice genome to establish oryzasin 1-overexpressing rice plants, named as OsAP-OEs for further study. The PCR results showed that we first successfully insert oryzasin 1 into the rice genome. We compared the germination rate of seeds and survival rates of seedling between the transgenic plants and the wild-type (WT) plants exposed to heat treatment. The results showed that OsAP-OE transgenic lines have better performance in the germination and the survival rates under heat stress conditions. The germination rate of seeds and survival rate of seedlings of OsAP-OE transgenic lines were higher in comparison with the WT. In addition, we compared TTC reduction activity and electrolyte leakage of the WT and OsAP-OE seeds after heat treatment. Seedlings were viable among each transgenic line, whereas WT seedlings were sensitive to heat stress condition in the result of the TTC reduction. Besides that, the conductivity of the ion leakage also showed that oryzasin 1-overexpression line less effect in the membrane leakage than the WT line. The percentages of pollen viability of transgenic lines were higher in comparison with the WT under high temperature. These results confirm that the OsAP-OE seeds have higher thermotolerance than the WT. Our data revealed that oryzasin 1 positively regulates heat stress tolerance in rice.
CHINESE ABSTRACT i
ENGLISH ABSTRACT ii
ACKNOWLEDGMENT iii
LIST of CONTENTS iv
LIST of FIGURES vi
LIST of TABLES vii
LIST of ACRONYMS viii
CHAPTER 1. INTRODUCTION 9
1.1. Rice and its importance to human life 9
1.2. Heat stress in Crops 10
1.3. Physiological responses to heat stress 12
1.4. Small heat shock protein 13
1.5. Aspartic proteases 15
1.6. Aspartic proteases in plant 16
1.7. Aspartic proteases in rice 17
CHAPTER 2. MATERIALS AND METHODS 9
2.1. Plant materials and growth conditions 9
2.2. Plasmid construction 9
2.2.1. Primers 9
2.2.2. Plasmid construction 14
2.3. RT-PCR analysis 20
2.3.2. RNA extraction 22
2.3.3. RT-PCR analysis 23
2.4. Phenotyping 24
2.5. Protein extraction 27
CHAPTER 3. RESULTS 29
3.1. The expression levels of oryzasin 1 in rice plant 29
3.2. Transgenic rice plants showed normal phenotype under normal growth conditions 30
3.3. Overexpression of oryzasin 1 displayed high germination rate and survival rate in rice seeds and seedlings under heat stress conditions 31
3.4. Thermotolerance of oryzasin 1 overexpression line rice seedling under heat stress conditions 32
3.5. Overexpression lines can be rescued membrane leakage caused by the high temperatures 33
3.6. Observation of pollen shape and pollen viability 33
3.7. Oryzasin 1 may function in the recovery stage 35
CHAPTER 4. DISCUSSION 50
4.1. Oryzasin 1 is involved in seed development and seed germination 50
4.2. Oryzasin 1 may play a positive role in thermotolerance in rice seeds and rice seedlings 51
WORKING MODEL 54
CONCLUSIONS 55
REFERENCES 56
1. Crawford, G.W. and C. Shen, The origins of rice agriculture: recent progress in East Asia. Antiquity, 1998. 72(278): p. 858-866.
2. Khush, G.S., What it will take to Feed 5.0 Billion Rice consumers in 2030. Plant Molecular Biology, 2005. 59(1): p. 1-6.
3. Gale, M.D. and K.M. Devos, Comparative genetics in the grasses. Proceedings of the National Academy of Sciences of the United States of America, 1998. 95(5): p. 1971-1974.
4. Eckardt, N.A., Sequencing the Rice Genome. The Plant Cell, 2000. 12(11): p. 2011.
5. Mittler, R., Abiotic stress, the field environment and stress combination. Trends in Plant Science, 2006. 11(1): p. 15-19.
6. Mikhailenko, I. and V.J.С.б. Dragavtsev, Mathematical modelling in plant breeding. I. Theoretical basis of genotypes identification on their phenotypes during selection in segregating generations. 2013(1 (eng)).
7. Urazaliev, K., Bioinformation technologies in plant breeding. 2019.
8. Allard, R.W., Principles of plant breeding. 1999: John Wiley & Sons.
9. Hallauer, A.R., M.J. Carena, and J.d. Miranda Filho, Quantitative genetics in maize breeding. Vol. 6. 2010: Springer Science & Business Media.
10. Field, C.B., et al., Managing the risks of extreme events and disasters to advance climate change adaptation: special report of the intergovernmental panel on climate change. 2012: Cambridge University Press.
11. Livingston, B.E. and F.W. Haasis, Relations of Time and Maintained Temperature to Germination Percentage for a Lot of Rice Seed. American Journal of Botany, 1933. 20(9): p. 596-615.
12. Yoshida, S., Effects of temperature on growth of the rice plant (Oryza sativa L.) in a controlled environment. Soil Science and Plant Nutrition, 1973. 19(4): p. 299-310.
13. Yoshida, S., Fundamentals of rice crop science. 1981: Int. Rice Res. Inst.
14. Nishiyama, I., Decrease in Germination Activity of Rice Seeds due to Excessive Desiccation in Storage. Japanese journal of crop science, 1977. 46(1): p. 111-118.
15. Han, F., et al., A comparative proteomic analysis of rice seedlings under various high-temperature stresses. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2009. 1794(11): p. 1625-1634.
16. Wahid, A., et al., Heat tolerance in plants: An overview. Environmental and Experimental Botany, 2007. 61(3): p. 199-223.
17. Frank, G., et al., Transcriptional profiling of maturing tomato (Solanum lycopersicum L.) microspores reveals the involvement of heat shock proteins, ROS scavengers, hormones, and sugars in the heat stress response. Journal of Experimental Botany, 2009. 60(13): p. 3891-3908.
18. Li, W., et al., Proteomics analysis of alfalfa response to heat stress. 2013. 8(12).
19. Kaplan, F., et al., Exploring the temperature-stress metabolome of Arabidopsis. 2004. 136(4): p. 4159-4168.
20. Bokszczanin, K.L., et al., Perspectives on deciphering mechanisms underlying plant heat stress response and thermotolerance. 2013. 4: p. 315.
21. Liu, X. and B.J.J.o.t.A.S.f.H.S. Huang, Carbohydrate accumulation in relation to heat stress tolerance in two creeping bentgrass cultivars. 2000. 125(4): p. 442-447.
22. Huber, A.E. and T.L. Bauerle, Long-distance plant signaling pathways in response to multiple stressors: the gap in knowledge. Journal of Experimental Botany, 2016. 67(7): p. 2063-2079.
23. Rizhsky, L., et al., When defense pathways collide. The response of Arabidopsis to a combination of drought and heat stress. 2004. 134(4): p. 1683-1696.
24. Sicher, R.C. and J.Y. Barnaby, Impact of carbon dioxide enrichment on the responses of maize leaf transcripts and metabolites to water stress. Physiologia Plantarum, 2012. 144(3): p. 238-253.
25. Sicher, R.C., D. Timlin, and B. Bailey, Responses of growth and primary metabolism of water-stressed barley roots to rehydration. Journal of Plant Physiology, 2012. 169(7): p. 686-695.
26. Goufo, P., et al., Cowpea (Vigna unguiculata L. Walp.) Metabolomics: Osmoprotection as a Physiological Strategy for Drought Stress Resistance and Improved Yield. 2017. 8(586).
27. Farooq, M., et al., Heat Stress in Wheat during Reproductive and Grain-Filling Phases. Critical Reviews in Plant Sciences, 2011. 30(6): p. 491-507.
28. Dwivedi, R., et al., Evaluation of wheat genotypes (Triticum aestivum L.) at grain filling stage for heat tolerance. 2017. 5(2): p. 971-975.
29. Shanmugam, S., et al., The Alleviating Effect of Elevated CO2 on Heat Stress Susceptibility of Two Wheat (Triticum aestivum L.) Cultivars. Journal of Agronomy and Crop Science, 2013. 199(5): p. 340-350.
30. Kalra, N., et al., Effect of increasing temperature on yield of some winter crops in northwest India. 2008: p. 82-88.
31. Devasirvatham, V., et al., Effect of high temperature on the reproductive development of chickpea genotypes under controlled environments. 2012. 39(12): p. 1009-1018.
32. Cairns, J.E., et al., Maize production in a changing climate: impacts, adaptation, and mitigation strategies, in Advances in agronomy. 2012, Elsevier. p. 1-58.
33. Djanaguiraman, M., et al., Physiological differences among sorghum (Sorghum bicolor L. Moench) genotypes under high temperature stress. Environmental and Experimental Botany, 2014. 100: p. 43-54.
34. Singh, V., et al., Genotypic Differences in Effects of Short Episodes of High-Temperature Stress during Reproductive Development in Sorghum. Crop Science, 2016. 56.
35. Giorno, F., et al., Ensuring Reproduction at High Temperatures: The Heat Stress Response during Anther and Pollen Development. Plants (Basel, Switzerland), 2013. 2(3): p. 489-506.
36. Hedhly, A., Sensitivity of flowering plant gametophytes to temperature fluctuations. Environmental and Experimental Botany, 2011. 74: p. 9-16.
37. Hasanuzzaman, M., et al., Physiological, biochemical, and molecular mechanisms of heat stress tolerance in plants. 2013. 14(5): p. 9643-9684.
38. Paupière, M.J., A.W. van Heusden, and A.G. Bovy, The metabolic basis of pollen thermo-tolerance: perspectives for breeding. Metabolites, 2014. 4(4): p. 889-920.
39. Morimoto, R.I., Cells in stress: transcriptional activation of heat shock genes. Science, 1993. 259(5100): p. 1409.
40. Feder, M. and G. Hofmann, Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and Ecological Physiology. Annual review of physiology, 1999. 61: p. 243-82.
41. Ritossa, F., A new puffing pattern induced by temperature shock and DNP in drosophila. Experientia, 1962. 18(12): p. 571-573.
42. Boston, R.S., P.V. Viitanen, and E. Vierling, Molecular chaperones and protein folding in plants. Plant Molecular Biology, 1996. 32(1): p. 191-222.
43. Lindquist, S. and E.A. Craig, THE HEAT-SHOCK PROTEINS. Annual Review of Genetics, 1988. 22(1): p. 631-677.
44. Vierling, E., The Roles of Heat Shock Proteins in Plants. Annual Review of Plant Physiology and Plant Molecular Biology, 1991. 42(1): p. 579-620.
45. Lindquist, S., THE HEAT-SHOCK RESPONSE. Annual Review of Biochemistry, 1986. 55(1): p. 1151-1191.
46. Wang, W., et al., Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends in Plant Science, 2004. 9(5): p. 244-252.
47. Hüttner, S. and R. Strasser, Endoplasmic reticulum-associated degradation of glycoproteins in plants. Frontiers in plant science, 2012. 3: p. 67-67.
48. Sitia, R. and I. Braakman, Quality control in the endoplasmic reticulum protein factory. Nature, 2003. 426(6968): p. 891-894.
49. Whitley, D., S.P. Goldberg, and W.D. Jordan, Heat shock proteins: A review of the molecular chaperones. Journal of Vascular Surgery, 1999. 29(4): p. 748-751.
50. Gupta, S.C., et al., Heat shock proteins in toxicology: How close and how far? Life Sciences, 2010. 86(11): p. 377-384.
51. Kappé, G., J.A.M. Leunissen, and W.W. de Jong, Evolution and Diversity of Prokaryotic Small Heat Shock Proteins, in Small Stress Proteins, A.-P. Arrigo and W.E.G. Müller, Editors. 2002, Springer Berlin Heidelberg: Berlin, Heidelberg. p. 1-17.
52. Haslbeck, M., et al., Some like it hot: the structure and function of small heat-shock proteins. Nature Structural & Molecular Biology, 2005. 12(10): p. 842-846.
53. Waters, E.R., The evolution, function, structure, and expression of the plant sHSPs. Journal of Experimental Botany, 2012. 64(2): p. 391-403.
54. Seo, J.S., et al., The intertidal copepod Tigriopus japonicus small heat shock protein 20 gene (Hsp20) enhances thermotolerance of transformed Escherichia coli. Biochemical and Biophysical Research Communications, 2006. 340(3): p. 901-908.
55. Sun, W., M. Van Montagu, and N. Verbruggen, Small heat shock proteins and stress tolerance in plants. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2002. 1577(1): p. 1-9.
56. Haslbeck, M. and E. Vierling, A first line of stress defense: small heat shock proteins and their function in protein homeostasis. Journal of molecular biology, 2015. 427(7): p. 1537-1548.
57. Miernyk, J.A., Protein folding in the plant cell. Plant physiology, 1999. 121(3): p. 695-703.
58. Ferguson, D.L., J.A. Guikema, and G.M. Paulsen, Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress. Plant physiology, 1990. 92(3): p. 740-746.
59. Santhanagopalan, I., et al., Model chaperones: small heat shock proteins from plants, in The big book on small heat shock proteins. 2015, Springer. p. 119-153.
60. Davies, D.R., The Structure and Function of the Aspartic Proteinases. Annual Review of Biophysics and Biophysical Chemistry, 1990. 19(1): p. 189-215.
61. Barrett, A.J., Cellular Proteolysis An Overview. Annals of the New York Academy of Sciences, 1992. 674(1): p. 1-15.
62. Rawlings, N.D. and A.J. Barrett, MEROPS: the peptidase database. Nucleic acids research, 1999. 27(1): p. 325-331.
63. Cooper, J.J.C.d.t., Aspartic proteinases in disease: a structural perspective. 2002. 3(2): p. 155-173.
64. Dunn, B.M., Structure and Mechanism of the Pepsin-Like Family of Aspartic Peptidases. Chemical Reviews, 2002. 102(12): p. 4431-4458.
65. Barrett, A.J., J.F. Woessner, and N.D. Rawlings, Handbook of proteolytic enzymes. Vol. 1. 2012: Elsevier.
66. Simões, I. and C. Faro, Structure and function of plant aspartic proteinases. European Journal of Biochemistry, 2004. 271(11): p. 2067-2075.
67. Rawlings, N.D. and A. Bateman, Pepsin homologues in bacteria. BMC genomics, 2009. 10: p. 437-437.
68. Krysan, D.J., et al., Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae. Eukaryotic cell, 2005. 4(8): p. 1364-1374.
69. Cao, S., et al., Genome-wide characterization of aspartic protease (AP) gene family in Populus trichocarpa and identification of the potential PtAPs involved in wood formation. BMC Plant Biology, 2019. 19(1): p. 276.
70. Takahashi, K., et al., Widespread tissue expression of nepenthesin-like aspartic protease genes in Arabidopsis thaliana. Plant Physiology and Biochemistry, 2008. 46(7): p. 724-729.
71. Chen, J., et al., Aspartic proteases gene family in rice: Gene structure and expression, predicted protein features and phylogenetic relation. Gene, 2009. 442(1): p. 108-118.
72. Guo, R., et al., Genome-wide identification, evolutionary and expression analysis of the aspartic protease gene superfamily in grape. BMC genomics, 2013. 14: p. 554-554.
73. Stael, S., et al., Plant proteases and programmed cell death. 2019, Oxford University Press UK.
74. Faro, C., S.J.C.P. Gal, and P. Science, Aspartic proteinase content of the Arabidopsis genome. 2005. 6(6): p. 493-500.
75. Mutlu, A. and S. Gal, Plant aspartic proteinases: enzymes on the way to a function. Physiologia Plantarum, 1999. 105(3): p. 569-576.
76. Gao, H., et al., Two Membrane-Anchored Aspartic Proteases Contribute to Pollen and Ovule Development. Plant Physiology, 2017. 173(1): p. 219.
77. Paparelli, E., et al., Misexpression of a chloroplast aspartyl protease leads to severe growth defects and alters carbohydrate metabolism in Arabidopsis. Plant physiology, 2012. 160(3): p. 1237-1250.
78. Phan, H.A., et al., The MYB80 Transcription Factor Is Required for Pollen Development and the Regulation of Tapetal Programmed Cell Death in Arabidopsis thaliana. The Plant Cell, 2011. 23(6): p. 2209.
79. Chen, F. and M.R. Foolad, Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration. Plant Molecular Biology, 1997. 35(6): p. 821-831.
80. Alam, M.M., et al., Response of an aspartic protease gene OsAP77 to fungal, bacterial and viral infections in rice. Rice (New York, N.Y.), 2014. 7(1): p. 9-9.
81. Breitenbach, H.H., et al., Contrasting Roles of the Apoplastic Aspartyl Protease APOPLASTIC, ENHANCED DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in Arabidopsis Systemic Acquired Resistance. Plant physiology, 2014. 165(2): p. 791-809.
82. Li, Y., et al., Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants. The Plant Cell, 2016. 28(1): p. 233.
83. Prasad, B.D., et al., Overexpression of Rice (Oryza sativa L.) OsCDR1 Leads to Constitutive Activation of Defense Responses in Rice and Arabidopsis. Molecular Plant-Microbe Interactions®, 2009. 22(12): p. 1635-1644.
84. Xia, Y., et al., An extracellular aspartic protease functions in Arabidopsis disease resistance signaling. The EMBO journal, 2004. 23(4): p. 980-988.
85. Yao, X., et al., Overexpression of the aspartic protease ASPG1 gene confers drought avoidance in Arabidopsis. Journal of Experimental Botany, 2012. 63(7): p. 2579-2593.
86. Nakano, T., et al., A novel protein with DNA binding activity from tobacco chloroplast nucleoids. The Plant cell, 1997. 9(9): p. 1673-1682.
87. Nakano, T., et al., CND41, a chloroplast nucleoid protein that regulates plastid development, causes reduced gibberellin content and dwarfism in tobacco. Physiologia Plantarum, 2003. 117(1): p. 130-136.
88. Chen, J., et al., A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica–japonica hybrids in rice. Proceedings of the National Academy of Sciences, 2008. 105(32): p. 11436.
89. Ji, Q., et al., Molecular basis underlying the S5-dependent reproductive isolation and compatibility of indica/japonica rice hybrids. Plant physiology, 2012. 158(3): p. 1319-1328.
90. Ge, X., et al., An Arabidopsis aspartic protease functions as an anti-cell-death component in reproduction and embryogenesis. EMBO reports, 2005. 6: p. 282-8.
91. Huang, J., et al., OsAP65, a rice aspartic protease, is essential for male fertility and plays a role in pollen germination and pollen tube growth. Journal of experimental botany, 2013. 64(11): p. 3351-3360.
92. Niu, N., et al., EAT1 promotes tapetal cell death by regulating aspartic proteases during male reproductive development in rice. Nature Communications, 2013. 4(1): p. 1445.
93. Asakura, T., et al., Rice Aspartic Proteinase, Oryzasin, Expressed During Seed Ripening and Germination, has a Gene Organization Distinct from Those of Animal and Microbial Aspartic Proteinases. European Journal of Biochemistry, 1995. 232(1): p. 77-83.
94. Asakura, T., et al., Oryzasin as an Aspartic Proteinase Occurring in Rice Seeds:  Purification, Characterization, and Application to Milk Clotting. Journal of Agricultural and Food Chemistry, 1997. 45(4): p. 1070-1075.
95. Asakura, T., et al., The plant aspartic proteinase-specific polypeptide insert is not directly related to the activity of oryzasin 1. European Journal of Biochemistry, 2000. 267(16): p. 5115-5122.
96. Fukamizu, A., et al., Structure of the rat renin gene. 1988. 201(2): p. 443-450.
97. Faust, P.L., S. Kornfeld, and J.M.J.P.o.t.N.A.o.S. Chirgwin, Cloning and sequence analysis of cDNA for human cathepsin D. 1985. 82(15): p. 4910-4914.
98. Horiuchi, H., et al., Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus. 1988. 170(1): p. 272-278.
99. RUNEBERG‐ROOS, P., K. TÖRMÄKANGAS, and A.J.E.j.o.b. ÖSTMAN, Primary structure of a barley‐grain aspartic proteinase: A plant aspartic proteinase resembling mammalian cathepsin D. 1991. 202(3): p. 1021-1027.
100. Cordeiro, M.C., et al., Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin. 1994. 24(5): p. 733-741.
101. Alexander, M.P., Differential Staining of Aborted and Nonaborted Pollen. Stain Technology, 1969. 44(3): p. 117-122.
102. Crick, F., Central Dogma of Molecular Biology. Nature, 1970. 227(5258): p. 561-563.
103. Srinivasan, A., H. Takeda, and T.J.E. Senboku, Heat tolerance in food legumes as evaluated by cell membrane thermostability and chlorophyll fluorescence techniques. 1996. 88(1): p. 35-45.
104. Georgieva, K., et al., Response of chlorina barley mutants to heat stress under low and high light %J Functional Plant Biology. 2003. 30(5): p. 515-524.
105. Blum, A. and A. Ebercon, Cell Membrane Stability as a Measure of Drought and Heat Tolerance in Wheat1. Crop Science, 1981. 21: p. 43-47.
106. Ilík, P., et al., Estimating heat tolerance of plants by ion leakage: a new method based on gradual heating. New Phytologist, 2018. 218(3): p. 1278-1287.
107. Xu, H., et al., Comparison of investigation methods of heat injury in grapevine (Vitis) and assessment to heat tolerance in different cultivars and species. BMC plant biology, 2014. 14: p. 156-156.
108. Boothe, J., et al., Seed-based expression systems for plant molecular farming. Plant Biotechnology Journal, 2010. 8(5): p. 588-606.
109. Schwechheimer, C. and K. Schwager, Regulated proteolysis and plant development. Plant cell reports, 2004. 23: p. 353-64.
110. van der Hoorn, R.A.L., Plant Proteases: From Phenotypes to Molecular Mechanisms. Annual Review of Plant Biology, 2008. 59(1): p. 191-223.
111. Tan-Wilson, A.L. and K.A. Wilson, Mobilization of seed protein reserves. Physiologia Plantarum, 2012. 145(1): p. 140-153.
112. Shu, K., et al., Two Faces of One Seed: Hormonal Regulation of Dormancy and Germination. Molecular Plant, 2016. 9(1): p. 34-45.
113. Shutov, A.D. and I.A. Vaintraub, Degradation of storage proteins in germinating seeds. Phytochemistry, 1987. 26(6): p. 1557-1566.
114. Müntz, K., et al., Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth. 2001. 52(362): p. 1741-1752.
115. D'Hondt, K., et al., An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro. 1993. 268(28): p. 20884-91.
116. Runeberg-Roos, P., et al., The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro. Plant physiology, 1994. 105(1): p. 321-329.
117. Gruis, D.F., et al., Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases. The Plant cell, 2002. 14(11): p. 2863-2882.
118. Otegui, M.S., et al., The Proteolytic Processing of Seed Storage Proteins in Arabidopsis Embryo Cells Starts in the Multivesicular Bodies. The Plant Cell, 2006. 18(10): p. 2567.
119. Belozersky, M.A., S.T. Sarbakanova, and Y.E. Dunaevsky, Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin. Planta, 1989. 177(3): p. 321-326.
120. Capocchi, A., et al., Degradation of Gluten by Proteases from Dry and Germinating Wheat (Triticum durum) Seeds:  An in Vitro Approach to Storage Protein Mobilization. Journal of Agricultural and Food Chemistry, 2000. 48(12): p. 6271-6279.
121. Tamura, T., et al., Differential expression of wheat aspartic proteinases, WAP1 and WAP2, in germinating and maturing seeds. Journal of Plant Physiology, 2007. 164(4): p. 470-477.
122. Brijs, K., W. Bleukx, and J.A. Delcour, Proteolytic Activities in Dormant Rye (Secale cereale L.) Grain. Journal of Agricultural and Food Chemistry, 1999. 47(9): p. 3572-3578.
123. Shen, W., et al., Arabidopsis Aspartic Protease ASPG1 Affects Seed Dormancy, Seed Longevity and Seed Germination. Plant and Cell Physiology, 2018. 59(7): p. 1415-1431.
124. He, F., et al., Protein storage vacuole acidification as a control of storage protein mobilization in soybeans. Journal of Experimental Botany, 2007. 58(5): p. 1059-1070.
125. Gao, C., et al., Dual roles of an Arabidopsis ESCRT component FREE1 in regulating vacuolar protein transport and autophagic degradation. Proceedings of the National Academy of Sciences of the United States of America, 2015. 112(6): p. 1886-1891.
126. Elpidina, E., Y. Dunaevsky, and M.J.J.o.e.b. Belozersky, Protein bodies from buckwheat seed cotyledons: isolation and characteristics. 1990. 41(8): p. 969-977.
127. Marttila, S., B.L. Jones, and A.J.P.P. Mikkonen, Differential localization of two acid proteinases in germinating barley (Hordeum vulgare) seed. 1995. 93(2): p. 317-327.
128. Parsell, D.A. and S. Lindquist, THE FUNCTION OF HEAT-SHOCK PROTEINS IN STRESS TOLERANCE: DEGRADATION AND REACTIVATION OF DAMAGED PROTEINS. Annual Review of Genetics, 1993. 27(1): p. 437-496.
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