請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/25829
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 鄭石通(Shih-Tong Jeng) | |
dc.contributor.author | Hsin-Yin Lin | en |
dc.contributor.author | 林欣穎 | zh_TW |
dc.date.accessioned | 2021-06-08T06:32:17Z | - |
dc.date.copyright | 2011-09-08 | |
dc.date.issued | 2011 | |
dc.date.submitted | 2011-08-02 | |
dc.identifier.citation | 紀姵如 (2003.) Hydrogen Peroxide與Nitric Oxide對於甘藷防禦機制之功能探討。國立台灣大學植物科學研究所碩士論文。
周以祥 (2005.) 甘藷中SUMO基因表現及其訊息傳遞路徑。國立台灣大學植物科學研究所碩士論文。 Bernier-Villamor, V., Sampson, D.A., Matunis, M.J., and Lima, C.D. (2002). Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108, 345-356. Bishop, P.D., Makus, D.J., Pearce, G., and Ryan, C.A. (1981). Proteinase inhibitor-inducing factor activity in tomato leaves resides in oligosaccharides enzymically released from cell walls. Proc. Natl. Acad. Sci. U. S. A. 78, 3536-3540. Bolwell, G.P. (1999). Role of active oxygen species and NO in plant defence responses. Curr. Opin. Plant Biol. 2, 287-294. Budhiraja, R., Hermkes, R., Muller, S., Schmidt, J., Colby, T., Panigrahi, K., Coupland, G., and Bachmair, A. (2009). Substrates related to chromatin and to RNA-dependent processes are modified by Arabidopsis SUMO isoforms that differ in a conserved residue with influence on desumoylation. Plant Physiol. 149, 1529-1540. Cadenas, E. (1989). Biochemistry of oxygen toxicity. Annu. Rev. Biochem. 58, 79-110. Catala, R., Ouyang, J., Abreu, I.A., Hu, Y., Seo, H., Zhang, X., and Chua, N.H. (2007). The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses. Plant Cell 19, 2952-2966. Chen, D., Colditz, I.G., Glenn, G.M., and Tsonis, C.G. (2000). Induction of systemic immune responses in sheep by topical application of cholera toxin to skin. Vet. Immunol. Immunopathol. 77, 191-199. Conti, L., Price, G., O'Donnell, E., Schwessinger, B., Dominy, P., and Sadanandom, A. (2008). Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis. Plant Cell 20, 2894-2908. Dat, J., Vandenabeele, S., Vranova, E., Van Montagu, M., Inze, D., and Van Breusegem, F. (2000). Dual action of the active oxygen species during plant stress responses. Cell. Mol. Life Sci. 57, 779-795. Dicke, M. (2000). Chemical ecology of host-plant selection by herbivorous arthropods: a multitrophic perspective. Biochem Syst Ecol 28, 601-617. Farmer, E.E., and Ryan, C.A. (1990). Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proc. Natl. Acad. Sci. U. S. A. 87, 7713-7716. Garcia-Mata, C., and Lamattina, L. (2001). Nitric oxide induces stomatal closure and enhances the adaptive plant responses against drought stress. Plant Physiol. 126, 1196-1204. Hanania, U., Furman-Matarasso, N., Ron, M., and Avni, A. (1999). Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death. Plant J. 19, 533-541. Hotson, A., Chosed, R., Shu, H., Orth, K., and Mudgett, M.B. (2003). Xanthomonas type III effector XopD targets SUMO-conjugated proteins in planta. Mol. Microbiol. 50, 377-389. Jin, J.B., Jin, Y.H., Lee, J., Miura, K., Yoo, C.Y., Kim, W.Y., Van Oosten, M., Hyun, Y., Somers, D.E., Lee, I., Yun, D.J., Bressan, R.A., and Hasegawa, P.M. (2008). The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affects on FLC chromatin structure. Plant J. 53, 530-540. Kurepa, J., Walker, J.M., Smalle, J., Gosink, M.M., Davis, S.J., Durham, T.L., Sung, D.Y., and Vierstra, R.D. (2003). The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J. Biol. Chem. 278, 6862-6872. Lamb, C., and Dixon, R.A. (1997). The Oxidative Burst in Plant Disease Resistance. Plant Biol. 48, 251-275. Lee, G.W., Melchior, F., Matunis, M.J., Mahajan, R., Tian, Q., and Anderson, P. (1998). Modification of Ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue. J. Biol. Chem. 273, 6503-6507. Lee, J., Nam, J., Park, H.C., Na, G., Miura, K., Jin, J.B., Yoo, C.Y., Baek, D., Kim, D.H., Jeong, J.C., Kim, D., Lee, S.Y., Salt, D.E., Mengiste, T., Gong, Q., Ma, S., Bohnert, H.J., Kwak, S.S., Bressan, R.A., Hasegawa, P.M., and Yun, D.J. (2007). Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase. Plant J. 49, 79-90. Lois, L.M., Lima, C.D., and Chua, N.H. (2003). Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell 15, 1347-1359. Mahajan, R., Gerace, L., and Melchior, F. (1998). Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140, 259-270. Matunis, M.J., Coutavas, E., and Blobel, G. (1996). A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol. 135, 1457-1470. Miller, M.J., Barrett-Wilt, G.A., Hua, Z., and Vierstra, R.D. (2010). Proteomic analyses identify a diverse array of nuclear processes affected by small ubiquitin-like modifier conjugation in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 107, 16512-16517. Miura, K., Jin, J.B., Lee, J., Yoo, C.Y., Stirm, V., Miura, T., Ashworth, E.N., Bressan, R.A., Yun, D.J., and Hasegawa, P.M. (2007). SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and freezing tolerance in Arabidopsis. Plant Cell 19, 1403-1414. Miura, K., Rus, A., Sharkhuu, A., Yokoi, S., Karthikeyan, A.S., Raghothama, K.G., Baek, D., Koo, Y.D., Jin, J.B., Bressan, R.A., Yun, D.J., and Hasegawa, P.M. (2005). The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses. Proc. Natl. Acad. Sci. U. S. A. 102, 7760-7765. Murtas, G., Reeves, P.H., Fu, Y.F., Bancroft, I., Dean, C., and Coupland, G. (2003). A nuclear protease required for flowering-time regulation in Arabidopsis reduces the abundance of SMALL UBIQUITIN-RELATED MODIFIER conjugates. Plant Cell 15, 2308-2319. Novatchkova, M., Budhiraja, R., Coupland, G., Eisenhaber, F., and Bachmair, A. (2004). SUMO conjugation in plants. Planta 220, 1-8. O'Donnell, P.J., Calvert, C., Atzorn, R., Wasternack, C., Leyser, H.M.O., and Bowles, D.J. (1996). Ethylene as a Signal Mediating the Wound Response of Tomato Plants. Science 274, 1914-1917. Park, J.J., Yi, J., Yoon, J., Cho, L.H., Ping, J., Jeong, H.J., Cho, S.K., Kim, W.T., and An, G. (2011). OsPUB15, an E3 ubiquitin ligase, functions to reduce cellular oxidative stress during seedling establishment. Plant J. 65, 194-205. Pena-Cortes, H., Sanchez-Serrano, J.J., Mertens, R., Willmitzer, L., and Prat, S. (1989). Abscisic acid is involved in the wound-induced expression of the proteinase inhibitor II gene in potato and tomato. Proc. Natl. Acad. Sci. U. S. A. 86, 9851-9855. Pieterse, C.M., and van Loon, L.C. (1999). Salicylic acid-independent plant defence pathways. Trends Plant Sci 4, 52-58. Reinbothe, S., Mollenhauer, B., and Reinbothe, C. (1994). JIPs and RIPs: the regulation of plant gene expression by jasmonates in response to environmental cues and pathogens. Plant Cell 6, 1197-1209. Roden, J., Eardley, L., Hotson, A., Cao, Y., and Mudgett, M.B. (2004). Characterization of the Xanthomonas AvrXv4 effector, a SUMO protease translocated into plant cells. Mol Plant Microbe Interact. 17, 633-643. Ryan, C.A. (2000). The systemin signaling pathway: differential activation of plant defensive genes. Biochim. Biophys. Acta 1477, 112-121. Saitoh, H., and Hinchey, J. (2000). Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem. 275, 6252-6258. Saracco, S.A., Miller, M.J., Kurepa, J., and Vierstra, R.D. (2007). Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol. 145, 119-134. Su, H.L., and Li, S.S. (2002). Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. Gene 296, 65-73. Vierstra, R.D., and Callis, J. (1999). Polypeptide tags, ubiquitous modifiers for plant protein regulation. Plant Mol. Biol. 41, 435-442. Walling, L.L. (2000). The Myriad Plant Responses to Herbivores. J Plant Growth Regul. 19, 195-216. Xue, Y., Zhou, F., Fu, C., Xu, Y., and Yao, X. (2006). SUMOsp: a web server for sumoylation site prediction. Nucleic Acids Res. 34, W254-257. Yoo, C.Y., Miura, K., Jin, J.B., Lee, J., Park, H.C., Salt, D.E., Yun, D.J., Bressan, R.A., and Hasegawa, P.M. (2006). SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid. Plant Physiol. 142, 1548-1558. Zhang, H., Saitoh, H., and Matunis, M.J. (2002). Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell. Biol. 22, 6498-6508. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/25829 | - |
dc.description.abstract | 蛋白質的轉譯後修飾作用在調節蛋白質作用上扮演一個重要的角色。Small ubiquitin-related modifier (SUMO)是近年來被發現與ubiquitin蛋白結構相似,且作用機制也與ubiquitination相似。SUMO以共價類胜肽鍵(isopeptide bond)的方式與其目標蛋白(target protein)上的Lys產生鍵結,進而修飾目標蛋白質的活性、穩定性或細胞內座落的位置等,而這個過程稱為sumoylation。Sumoylation影響許多植物生長發育與逆境的調控,包含開花時間、非生物性逆境反應等。然而,sumoylation影響這些訊息傳遞分子的詳細機制目前仍然不清楚。在實驗室先前調取一氧化氮(nitric oxide, NO)誘導蛋白的研究中,以蛋白質二維電泳系統(two-dimensional electrophoresis system)分離甘藷葉片(Ipomoea batatas cv. Tainung 57)在處理NO後的差異性蛋白, 再以LC/MS/MS分析,發現IbSUMO2為NO所誘導的蛋白質之一。此外,也在阿拉伯芥中建構大量表現GFP-IbSUMO2-GFP融合蛋白系統,進而來觀測IbSUMO2的細胞位置,結果顯示IbSUMO2主要坐落在細胞核;然而有趣的是,植株在處理過氧化氫(Hydrogen peroxide, H2O2)下,位於細胞核的IbSUMO2會轉移到細胞質。因此,為了瞭解IbSUMO2在細胞間移動的機制,我們利用甘藷及阿拉伯芥系統來調取IbSUMO2結合的目標蛋白。在甘藷系統中,主要以蛋白質二維電泳分離系統來找出H2O2誘導下可被IbSUMO2修飾之蛋白,而在阿拉伯芥系統,則以免疫沉澱(immunoprecipitation, IP)進行分離IbSUMO2修飾之蛋白,最後再以LC/MS/MS鑑定分析蛋白身分。根據液相層析質譜儀分析結果,我們獲得三個可能會被IbSUMO2結合的蛋白,分別為BiP1 (Luminal-binding protein 1)、putative F-Box protein以及HSC70-1 (Heat shock cognate 70 kDa protein ),且在H2O2處理下這三個基因的表現量也會被誘導上升,推測這三個蛋白質極可能受到IbSUMO2調控來參與氧化逆境的反應。 | zh_TW |
dc.description.abstract | Post-translational modifications of proteins play critical roles in regulation of protein activities. Small ubiquitin-related modifiers (SUMOs) were discovered to resemble ubiquitin in their three-dimensional structures and the way they link to other proteins. SUMO becomes covalently linked by an isopeptide bond between its C-terminal glycine and the lysines within the target proteins. Sumoylation controls a broad spectrum of cellular activities, including roles in changing protein activities, stabilizing proteins, and nuclear trafficking. Protein sumoylation plays an important role in plant development, flowering-time regulation, and abiotic stress response. However, the molecular roles of sumoylation in these pathways are largely unknown. In the previous studies in our laboratory, the leaves of sweet potato (Ipomoea batatas cv. Tainung 57) were treated with nitric oxide (NO), and the abundance of several proteins was increased based on the analyses of 2D electrophoresis. After the identification of LC/MS/MS, IbSUMO2 is one of the NO-induced proteins. Furthermore, fusion protein GFP-IbSUMO2-GFP was constructed to study the localization of IbSUMO2 within Arabidopsis cells by confocal microscopes. Results indicated that most GFP- IbSUMO2-GFP was in nucleus, and, however, after H2O2 treatment GFP-IbSUMO2-GFP translocated to cytoplasm in Arabidopsis cells. In order to understand the mechanism of IbSUMO2 translocation, a method to isolate IbSUMO2-conjugated proteins from sweet potato and Arabidopsis was developed. The effect of H2O2 on the accumulation of IbSUMO2 conjugates in sweet potato was studied by 2D electrophoresis. In addition, immunoprecipitation was used to isolate the putative proteins modified by IbSUMO2 in Arabidopsis after H2O2 treatment, and sumoylated proteins were identified by LC/MS/MS. According to the LC/MS/MS data, I found three putative proteins could be sumoylated after H2O2 treatment, they were BiP1 (Luminal-binding protein 1), putative F-Box protein, and HSC70-1 (Heat shock congnate 70 KDa protein). RT-PCR indicated that these three transcripts were also induced by H2O2, indicating that sumoylation of these three proteins played important roles during oxidative stress. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T06:32:17Z (GMT). No. of bitstreams: 1 ntu-100-R98B42002-1.pdf: 2707187 bytes, checksum: 1ec6708fcdab478e9b4a30e0501bf664 (MD5) Previous issue date: 2011 | en |
dc.description.tableofcontents | 口試委員議定書 i
誌謝 ii 中文摘要 iii Abstract iv 第一章 前言 3 植物的防禦機制 3 SUMO的作用機制 5 SUMO調控蛋白之研究 6 研究目的與方向 7 第二章 材料與方法 8 一、 植物材料與處理 8 二、 實驗方法 9 第三章 結果 8 H2O2誘導甘藷Sumoylation的表現 21 H2O2影響IbSUMO2在甘藷細胞中的表現位置 21 蛋白質二維電泳系統分離IbSUMO2結合蛋白 22 H2O2亦誘導大量表現IbSUSO2的阿拉伯芥轉殖株產生sumoylation現象 23 H2O2影響IbSUMO2在阿拉伯芥細胞中的表現位置 24 建立IbSUMO2/Atsumo1/Atsumo2轉殖株 25 免疫沉澱分離阿拉伯芥中IbSUMO2結合蛋白 26 液相層析串連質譜儀(LC/MS/MS)分析與IbSUMO2結合之阿拉伯芥蛋白 26 H2O2誘導IbSUNO2可能結合蛋白之基因表現 27 第四章 討論 29 H2O2誘導IbSUMO2形成結合態 29 IbSUMO2藉由調控結合蛋白質來幫助甘藷度過氧化逆境 30 H2O2誘導IbSUMO2和阿拉伯芥蛋白質結合 32 IbSUMO2可能之結合蛋白質(putative F-Box protein)在阿拉伯芥中扮演之功能探討 34 比較IbSUMO2在甘藷系統及阿拉伯芥系統之差異 35 結論 35 第五章 參考文獻 36 圖表 42 附錄 58 | |
dc.language.iso | zh-TW | |
dc.title | 甘藷IbSUMO結合蛋白之釣取與研究 | zh_TW |
dc.title | Isolation and study of Ipomoea batatas small ubiquitin related-modifier (SUMO)-regulated protein | en |
dc.type | Thesis | |
dc.date.schoolyear | 99-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 鄭貽生(Yi-Sheng Cheng),張世宗(Shih-Chung Chang),葉靖輝(Jin-Huh Yeh),吳少傑(Shaw-Jye Wu) | |
dc.subject.keyword | IbSUMO2,sumoylation,過氧化氫, | zh_TW |
dc.subject.keyword | IbSUMO2,sumoylation,H 2 O 2, | en |
dc.relation.page | 64 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2011-08-02 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 植物科學研究所 | zh_TW |
顯示於系所單位: | 植物科學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-100-1.pdf 目前未授權公開取用 | 2.64 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。