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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 鄭貽生 | zh_TW |
| dc.contributor.advisor | Yi-Sheng Cheng | en |
| dc.contributor.author | 于庭懿 | zh_TW |
| dc.contributor.author | Ting-Yi Yu | en |
| dc.date.accessioned | 2023-03-19T22:48:09Z | - |
| dc.date.available | 2023-11-10 | - |
| dc.date.copyright | 2022-08-12 | - |
| dc.date.issued | 2022 | - |
| dc.date.submitted | 2002-01-01 | - |
| dc.identifier.citation | Arner, E.S., and Holmgren, A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267, 6102-6109.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/85173 | - |
| dc.description.abstract | 植物荷爾蒙水楊酸(salicylic acid)所調節的免疫反應，在對抗非生物與生物逆境中扮演重要角色。在阿拉伯芥水楊酸免疫反應路徑中，NPR1調控約90%下游防禦基因的表現。在正常的狀況下，NPR1 是以多聚體的形式存在於細胞質中，當病菌侵染時，NPR1 會被硫氧化還原蛋白 TRX-h3或h5 還原成單體，單體的 NPR1 可入細胞核調控下游的防禦基因表現。先前的研究中顯示，NPR1表現與逆境相關蛋白AtSAP5有關；另外，初步研究發現，AtSAP5與TRX-h3有交互作用，但其交互作用後啟動的功能則未知。本研究發現AtSAP5具有結合並還原TRX-h3的能力且AtSAP5序列刪減分析之結果顯示 AtSAP5 的 A20 domain 與 TRX-h3 具有最佳結合能力。在還原力的測試顯示，A20 domain 具還原TRX-h3的能力，且在cysteine突變分析發現A20 domain中四個在不同植物物種中保守的cysteine在與TRX-h3之交互作用與保有還原酶活性皆十分重要。本研究對AtSAP5 如何參與 SA調控的免疫途徑提出新的見解。 | zh_TW |
| dc.description.abstract | Phytohormone salicylic acid (SA) plays a vital role in the plant defense responses against abiotic and biotic stresses. In SA-mediated immune pathway, NONEXPRESSOR OF PATHOGENESIS RELATED GENES1 (NPR1) involved in regulation of 90% of downstream SA-dependent immune related genes in Arabidopsis thaliana. Under normal conditions, NPR1 mainly exists as oligomeric form and is located in the cytosol. Upon pathogen infection, NPR1 is reduced from oligomer to monomer through thioredoxin (TRX)-h3 or –h5. Previous result indicates that the expression of NPR1 was regulated by stress-associated protein 5 (AtSAP5). Preliminary data also suggests that AtSAP5 could interact with TRX-h3. However, the function of interaction between AtSAP5 and TRX-h3 is unclear. In this study, the interaction between AtSAP5 and TRX3 is further confirmed and AtSAP5 function as a reductase to reduce TRX-h3 is demonstrated. To identify the region of AtSAP5 that interacts with TRX-h3, I generated several deletion clones of AtSAP5. The results show that the A20 domain exhibits the highest interacting ability with TRX-h3 and also confers the reductase activity. Four conserved cysteines were identified from SAP family in different plant species. Mutational analysis demonstrates each conserved cysteine is important for A20 domain to binds to TRX-h3, and also important for conferring reductase activity. This finding brings a new insight regarding how AtSAP5 regulates the SA-mediated immune pathway. | en |
| dc.description.provenance | Made available in DSpace on 2023-03-19T22:48:09Z (GMT). No. of bitstreams: 1 U0001-0308202209285400.pdf: 2832333 bytes, checksum: ab78488fc0ab05f0e33bff0e38c946c4 (MD5) Previous issue date: 2022 | en |
| dc.description.tableofcontents | 摘要………………………………………………………………..……………i
Abstract ii Contents iii List of figures vi Chapter 1. Introduction 1 1.1 Plant innate immunity 1 1.2 Salicylic acid (SA)-mediated immunity 2 1.3 Thioredoxin (TRX) 4 1.4 Stress-associated protein (SAP) 6 1.5 Dissertation projects……………………………………………………....................10 Chapter 2. Materials and Methods 11 2.1 Plant materials and growth conditions 11 2.1.1 Agro-infiltration 11 2.1.2 Split luciferase assay 11 2.2 Protein expression and purification 13 2.2.1 Competent cell preparation: 13 2.2.2 Transformation 13 2.2.3 Protein large-scale expression and purification 13 2.2.4 NADPH consumption assay 15 2.2.5 Insulin precipitation assay 15 2.2.6 Quartz crystal microbalance (QCM) 16 2.2.7 4-acetamido-4′-maleimidylstilbene-2,2′-disulfonate (AMS) modification 16 2.2.8 Sequence alignment 17 Chapter 3. Results 18 3.1 AtSAP5 interacts with TRX-h3 in split luciferase assay 18 3.2 His-TRX-h3 shows disulfide reductase activity 18 3.3 AtSAP5 interacts with TRX-h3 in vitro 19 3.4 AtSAP5 acts as a TRX-h3 reductase 20 3.5 A20 domain of AtSAP5 is more important for interaction with TRX-h3 21 3.7 A20 domain of AtSAP5 reduces TRX-h3 instead of AN1 domain. 22 3.8 The conserved residues of AtSAPs are identified via sequence alignment analysis 22 3.9 The four cysteines are important to the protein-protein interaction of AtSAP5 and TRX-h3 23 3.10 The four cysteines of N5 region support the reductase function to reduce TRX-h3 24 Chapter 4. Discussions 25 4.1 AtSAP5 was easily to interact with other proteins 25 4.2 AtSAP5 is a moonlight protein confers both E3 ligase and reductase activity 26 4.3 AtSAP5 can serves as a reductase to reduce TRX-h3 27 4.4 AtSAP5 involved in SA-regulated redox signaling and plant immunity 27 References 30 Figures 40 Figure 1. AtSAP5 interacts with TRX-h3 in split luciferase assay 40 Figure 2. SDS-PAGE analysis of His-TRX-h3, His-GST-AtSAP5, and GST protein purification. 41 Figure 3. His-MBP-NTRA protein purification and enzyme activity assay of TRX-h3. 42 Figure 4. The molecular interaction between AtSAP5 and TRX-h3 was detected by QCM 44 Figure 5. AtSAP5 facilitates reduction of TRX-h3 with free thiols 45 Figure 6. The diagram of truncated-domains of AtSAP5 46 Figure 7. A20 domain is the main region to interact with TRX-h3 by split luciferase assay 47 Figure 8. SDS-PAGE analysis of His-GST-N5, His-GST-N6, His-GST-A20-AN1, His-GST-A20 and His-GST-AN1 49 Figure 9. A20 domain is the main region to interact with TRX-h3 through QCM 50 Figure 10 A20 domain of AtSAP5 play more important role in reducing TRX-h3 52 Figure 11. Sequence alignment of SAP proteins form different plant species 53 Figure 12. Diagram of the single, double and Quadruple cysteine mutations of GST-N5 protein 54 Figure 13. The four cysteine mutants of N5 protein decrease the interaction ability to TRX-h3 through the split luciferase assay 55 Figure 14. SDS-PAGE analysis of His-GST-N5 C26A, His-GST-N5 C30A, His-GST-N5 C42A, His-GST-N5 C45A, His-GST-N5 C26/30A, His-GST-N5 C42/45A, and His-GST-N5 C26/30/42/45A 57 Figure 15. The four cysteine mutant of N5 protein decrease the interaction ability to TRX-h3 through QCM 58 Figure 16. Four cystines of A20 domain supports the reducatase function of AtSAP5 60 Appendix 61 Appendix Table 1. The buffer conditions 61 Appendix Table 2. The SDS-PAGE preparing protocol 62 Appendix Table 3. Primer list 63 Appendix Figure 1. AtSAP5 secondary structure prediction 68 Appendix Figure 2. AtSAP5-TRX-h3 putative working model 69 | - |
| dc.language.iso | zh_TW | - |
| dc.subject | 逆境相關蛋白 | zh_TW |
| dc.subject | 氧化還原震盪 | zh_TW |
| dc.subject | 水楊酸 | zh_TW |
| dc.subject | 硫氧化還原蛋白 | zh_TW |
| dc.subject | Salicylic acid (SA) | en |
| dc.subject | SA-induced redox oscillation | en |
| dc.subject | Stress-associated protein (SAP) | en |
| dc.subject | Thioredoxin (TRX) | en |
| dc.title | 阿拉伯芥逆境相關蛋白AtSAP5為硫氧化還原蛋白TRX-h3之還原酶 | zh_TW |
| dc.title | Arabidopsis thaliana stress-associated protein 5 (AtSAP5) functions as thioredoxin-h3 (TRX-h3) reductase | en |
| dc.type | Thesis | - |
| dc.date.schoolyear | 110-2 | - |
| dc.description.degree | 碩士 | - |
| dc.contributor.coadvisor | 葉信宏 | zh_TW |
| dc.contributor.coadvisor | Hsin-Hung Yeh | en |
| dc.contributor.oralexamcommittee | 鄭秋萍;楊淑怡;李金美 | zh_TW |
| dc.contributor.oralexamcommittee | Chiu-Ping Cheng;Shu-Yi Yang;Chin-Mei Lee | en |
| dc.subject.keyword | 水楊酸,氧化還原震盪,逆境相關蛋白,硫氧化還原蛋白, | zh_TW |
| dc.subject.keyword | Salicylic acid (SA),SA-induced redox oscillation,Stress-associated protein (SAP),Thioredoxin (TRX), | en |
| dc.relation.page | 69 | - |
| dc.identifier.doi | 10.6342/NTU202201997 | - |
| dc.rights.note | 同意授權(限校園內公開) | - |
| dc.date.accepted | 2022-08-08 | - |
| dc.contributor.author-college | 生命科學院 | - |
| dc.contributor.author-dept | 植物科學研究所 | - |
| dc.date.embargo-lift | 2022-08-12 | - |
| 顯示於系所單位： | 植物科學研究所 | |
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