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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 鄭梅君 | zh_TW |
| dc.contributor.advisor | Mei-Chun Cheng | en |
| dc.contributor.author | 林雯琪 | zh_TW |
| dc.contributor.author | Wen-Chi Lin | en |
| dc.date.accessioned | 2023-03-19T23:38:33Z | - |
| dc.date.available | 2023-08-10 | - |
| dc.date.copyright | 2022-10-08 | - |
| dc.date.issued | 2022 | - |
| dc.date.submitted | 2002-01-01 | - |
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/86136 | - |
| dc.description.abstract | ETHYLENE RESPONSE FACTOR 1 (ERF1)是阿拉伯芥當中參與在生物性與非生物性逆境中，一個極為重要的轉錄因子，並且主要調控乙烯訊息傳遞路徑。先前已有研究指出ERF1蛋白在黑暗中會受到UBIQUITIN-CONJUGATING ENZYME 18 (UBC18)的泛素化調控，經過酵素的合作，會負責標記目標蛋白使其透過proteasome的途徑降解而趨於不穩定。在本研究中，我們發現SUMO-CONJUGATING ENZYME 1 (SCE1)與ERF1有交互作用。同時另一個在阿拉伯芥當中扮演E3 ubiquitin ligase的蛋白CONSTITUTIVE PHOTOMORPHOGENESIS 1 (COP1)，在黑暗下會藉由調控ERF1的ubiquitination而使其降解，反之在光照下SCE1會透過SUMOylation使ERF1蛋白趨於穩定。我們更進一步發現，當ERF1蛋白的SUMOylation位點被突變 (ERF14KR) 後，ubiquitination和SUMOylation的修飾都有減少的現象，並且在植物當中我們也觀察到在進入黑暗後ERF14KR沒有被降解，間接證實了對於ERF1，ubiquitination和SUMOylation存在著光照條件之間的競爭關係。不僅如此，我們也看到sce1突變株不管在鹽處理或是乾旱下，側根數量以及植株存活率都較WT來的低。同時我們也發現sce1突變株在黑暗處理下，ERF1的下游基因P5CS1以及OSM34的表現量都較WT更低，表示SCE1可以藉由調控ERF1的穩定性正向地參與在植物逆境反應中。綜上所述，我們的研究證實了一項新的調控ERF1蛋白穩定性的分子機制，以及SCE1在逆境訊息傳遞當中扮演的重要角色。 | zh_TW |
| dc.description.abstract | ETHYLENE RESPONSE FACTOR 1 (ERF1) is an important transcription factor which involves in biotic and abiotic stress, and plays a major role in ethylene signaling. Previous studies have shown that ERF1 is unstable in the dark and its degradation is mediated by UBIQUITIN-CONJUGATING ENZYME 18. Here, we demonstrated that SUMO-CONJUGATING ENZYME 1 (SCE1) can physically interact with ERF1 in plants. CONSTITUTIVE PHOTOMORPHOGENESIS 1 (COP1) is an E3 ubiquitin ligase that target substrate protein for proteosome degradation pathway. In vitro and in vivo ubiquitination and SUMOylation assays suggest that COP1 mediates ERF1 ubiquitination in the dark while SCE1 mediates ERF1 SUMOylation in the light. Moreover, in vitro ubiquitination assay showed that the SUMOylation sites-mutated ERF1 (ERF1-4KR) led to less ubiquitination compared to wild-type ERF1, suggesting that ubiquitination of ERF1 might compete with its SUMOylation on the same residues. Our drought- and salt-stress analyses also suggest that SCE1 plays a positive role in stress response. sce1 mutants showed less tolerant phenotype under both drought and high salinity. The induction of ERF1’s downstream genes such as P5CS1 and OSM34 are negatively regulated by SCE1 under light/dark cycle. Collectively, this study reveals the molecular mechanism regulating ERF1’s stability and light-stress signaling crosstalk. | en |
| dc.description.provenance | Made available in DSpace on 2023-03-19T23:38:33Z (GMT). No. of bitstreams: 1 U0001-0609202213595200.pdf: 2259990 bytes, checksum: 44c34892c00a8bd84ab28e3d5da890f0 (MD5) Previous issue date: 2022 | en |
| dc.description.tableofcontents | CONTENTS
致謝 i CONTENTS iii LIST OF FIGURES AND TABLES vi 中文摘要 vii ABSTRACT viii Chapter 1 Introduction 1 1.1 The abiotic stress signaling pathways in plants 1 1.2 AP2/ERF family transcription factors in Arabidopsis 3 1.3 The background of ERF1 5 1.4 Post-translational modification-ubiquitination 7 1.5 Post-translational modification-SUMOylation 9 1.6 Experimental strategy and goals 12 Chapter 2 Materials and Methods 13 2.1 Plant materials 13 2.1.1 Arabidopsis wild type (WT) 13 2.1.2 sce1 mutants 13 2.1.3 ERF1 overexpression transgenic lines 14 2.2 Plant growth conditions 14 2.3 Methods 15 2.3.1 In Vitro Co-immunoprecipitation Assays 15 2.3.2 Genomic DNA extraction from Arabidopsis 16 2.3.3 Relative gene expression 16 2.3.3.1 RNA isolation from Arabidopsis 16 2.3.3.2 cDNA synthesis 17 2.3.3.3 Real-time PCR 17 2.3.4 Protein extraction and western blot analysis 18 2.3.5 Bimolecular fluorescence complementation (BiFC) 19 2.3.5.1 Construction and preparation of plasmids 19 2.3.5.2 Protoplast isolation and plasmid transformation 19 2.3.6 In vitro SUMOylation and Ubiquitination 20 2.3.6.1 Protein purification 20 2.3.6.2 In vitro SUMOylation assay 21 2.3.6.3 In vitro ubiquitination assay 22 2.3.7 Salt stress tolerance test 22 Chapter 3 Results 23 3.1 ERF1 interacts with SCE1 in vitro 23 3.2 Screening of the T-DNA insertion mutants of SCE1 23 3.3 SCE1 facilitates ERF1 protein stabilization 24 3.4 SCE1 facilitates the SUMOylation of ERF1 in the light 24 3.5 ERF1 shows stronger interaction activity with SCE1 in the light 25 3.6 COP1 promotes ERF1 protein degradation 26 3.7 COP1 promotes the ubiquitination of ERF1 under darkness 26 3.8 SUMOylation site analysis and purification of SUMO-site mutated ERF1 27 3.9 K77, K177, K180 and K190 might be the SUMOylation sites of ERF1 27 3.10 Ubiquitination competes with SUMOylation on the same lysine residues of ERF1 28 3.11 ERF14KR is more stable than ERF1WT in the dark 29 3.12 sce1-4 and sce1-7 mutants are more sensitive to salt stress compared to WT 30 3.13 SCE1 mediates the ERF1 downstream gene expression 30 3.14 Protein level of SCE1 is regulated under light/dark cycle and ACC treatment 31 Chapter 4 Discussion 32 4.1 SCE1 interacts with ERF1 in the light but not in the dark 32 4.2 SCE1 and COP1 mediate ERF1 stability under light/dark cycle 33 4.3 SCE1 is involved in stress response through ERF1 35 4.4 SUMOylation and Ubiquitination might compete the same lysine site 35 4.5 Conclusion 36 REFERENCES 38 FIGRURES AND TABLES 51 APPENDIX 69 論文口試問答集與討論建議 75 LIST OF FIGURES AND TABLES Figure 1. In vitro Co-IP assay of ERF1 and SCE1. 51 Figure 2. Co-IP assay of ERF1 and SCE1. 52 Figure 3. Identification of sce1-4 and sce1-7 T-DNA insertion mutants. 53 Figure 4. ERF1 protein level is regulated by SCE1 under light and dark condition. 54 Figure 5. SUMOylation of ERF1 is mediated by SCE1. 55 Figure 6. BiFC assay of SCE1 and ERF1 under light-to-dark condition. 56 Figure 7. ERF1 protein level is regulated by COP1 in the dark. 57 Figure 8. Ubiquitination of ERF1 is mediated by COP1. 58 Figure 9. Prediction of SUMOylation sites in ERF1. 59 Figure 10. SCE1 promotes SUMOylation of ERF1 in vitro. 60 Figure 11. COP1 promotes ubiquitination of ERF1 in vitro. 61 Figure 12. ERF14KR maintains the ERF1 protein level. 62 Figure 13. Phenotypic analysis of sce1-4 and sce1-7 mutants in response to salt stress. 63 Figure 14. Gene expression of P5CS1 and OSM34 in the dark. 64 Figure 15. SCE1 is mediated by light and ACC treatment. 65 Figure 16. A proposed model showing SCE1- and COP1-mediated regulation of ERF1 in light and stress response. 66 Table 1. List of primers for qPCR 67 Table 2. List of primers for other usages 68 | - |
| dc.language.iso | zh_TW | - |
| dc.title | 阿拉伯芥中的SCE1和COP1會透過泛素化與類小泛素化調節轉錄因子ERF1在光照與黑暗下的蛋白質穩定性 | zh_TW |
| dc.title | SCE1 and COP1 regulate the stability of ERF1 through SUMOylation and ubiquitination under light-dark cycle in Arabidopsis | en |
| dc.type | Thesis | - |
| dc.date.schoolyear | 110-2 | - |
| dc.description.degree | 碩士 | - |
| dc.contributor.oralexamcommittee | 楊健志;洪傳揚;許富鈞;常怡雍 | zh_TW |
| dc.contributor.oralexamcommittee | Chien-Chih Yang;Chwan-Yang Hong;Fu-Chiun Hsu;Yee-yung Charng | en |
| dc.subject.keyword | 阿拉伯芥,ERF1,SCE1,COP1,泛素化,類小泛素化,蛋白質穩定性,鹽逆境, | zh_TW |
| dc.subject.keyword | Arabidopsis,ERF1,SCE1,COP1,ubiquitination,SUMOylation,protein stability,salt stress, | en |
| dc.relation.page | 79 | - |
| dc.identifier.doi | 10.6342/NTU202203192 | - |
| dc.rights.note | 同意授權(全球公開) | - |
| dc.date.accepted | 2022-09-07 | - |
| dc.contributor.author-college | 生命科學院 | - |
| dc.contributor.author-dept | 生化科技學系 | - |
| dc.date.embargo-lift | 2023-08-10 | - |
| 顯示於系所單位： | 生化科技學系 | |
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