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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張世宗(Shih-Chung Chang) | |
| dc.contributor.author | Pang-Yu Liu | en |
| dc.contributor.author | 劉邦宇 | zh_TW |
| dc.date.accessioned | 2021-06-08T04:47:25Z | - |
| dc.date.copyright | 2009-08-03 | |
| dc.date.issued | 2009 | |
| dc.date.submitted | 2009-07-30 | |
| dc.identifier.citation | 參考文獻
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/23206 | - |
| dc.description.abstract | SUMO (samll ubiquitin-like modifier) 由於與泛素具有相似結構與類似的酵素作用系統而得名。SUMO化 (SUMOylation) 是由E1活化酶、E2銜接酶和E3黏合酶三種酵素依序進行活化、銜接與黏合的步驟，以有效調控生物體內之蛋白質的SUMO化修飾作用。相較於絕大多數經泛素修飾的蛋白質所導向的蛋白酶體降解，SUMO化在細胞中已被發現有更多樣且範圍廣泛的生理功能，如訊息傳遞、蛋白質穩定性、酵素活性調控，以及細胞內分子運送等，因而使其相關的研究受到高度的重視。
本論文利用蛋白質體學技術分析細胞內尚未被發現之SUMO化受質，同時並結合金屬逆境之研究，探討逆境下是否會誘導細胞內SUMO化修飾作用的改變。實驗結果顯示，砷逆境會誘導COS-7細胞內SUMO之耦合蛋白質明顯的上升；而鋅與鎘處理細胞後則沒有觀察到SUMO化有提升的現象。此外，經質譜儀鑑定結果發現19S蛋白解體次單元Rpt3與Rpt5可能為SUMO之受質。利用真核細胞HeLa或大腸桿菌的SUMO化系統，進一步證實了Rpt3會受SUMO-1修飾，而Rpt5則會受SUMO-1與SUMO-2共同修飾。本研究發現蛋白解體可能直接受SUMO化修飾而調控，顯示SUMO與泛素-蛋白解體兩個系統間有更為複雜的交互作用機制，這將是未來值得深入研究的方向之一。 | zh_TW |
| dc.description.abstract | SUMO (small ubiquitin-like modifier) has similar molecular structure and undergoes similar conjugation mechanism with ubiquitn. SUMOylation is a sequential catalytic enzyme cascase, which includes E1 activation, E2 conjugation and E3 ligation, for effectively regulating SUMOylated proteins in vivo. In contrast to the fact that most ubiquitinated proteins undergo proteasomal degradation, it has been shown that SUMOylated proteins are involved in a wide range of physiological functions, including signal transduction, protein stability, enzyme activity and localization. Due to this interesing difference, more and more research has been done on sumoylation.
In this study, the proteomics technique has been applied to analyze the unidentified SUMOlyated substrates in mammalian cells. To understand that whether the heavy metal stress can change the level of SUMOylated protein, cells were treated with As, Zn and Cd under various conditions. The results demonstrate that arsenic stress induces SUMO-2 sumoylation in COS-7 cells, however, this phenomemon is missing in Zn and Cd treatment . The data of mass spectrometry analysis showed that Rpt3 and Rpt5, whitch are both of proteasomal 19S subunits, are possibly SUMO SUMOylated. Furthermore, I found that Rpt3 undergoes SUMO-1 SUMOylation and Rpt5 undergoes SUMO-1 and SUMO-2 co-SUMOylation by using gene transfection in HeLa cells and E. coli sumoylation system. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T04:47:25Z (GMT). No. of bitstreams: 1 ntu-98-R96b47217-1.pdf: 25134136 bytes, checksum: 4481559a12af5fa7db10afb5fe4519c7 (MD5) Previous issue date: 2009 | en |
| dc.description.tableofcontents | 目錄
中文摘要 i 英文摘要 ii 縮寫表 iii 第一章 緒論 1 1.1 SUMO蛋白質修飾系統 1 1.1.1 SUMO (small ubiquitin-like modifier) 1 1.1.2 SUMO化之反應機制 3 1.1.3去SUMO化之反應 4 1.1.4 SUMO目標蛋白質之蛋白質體學研究 6 1.1.5 SUMO化修飾之生理作用 8 1.1.6逆境壓力下誘導SUMO化修飾 9 1.1.7 SUMO化與泛素化修飾系統間訊息交換 10 1.2泛素-蛋白解體系統 12 1.2.1泛素化系統與蛋白解體系統之反應機制 12 1.2.2 26S蛋白解體之組成 13 1.2.3轉譯後修飾作用調控蛋白質體系統 15 1.3金屬逆境 15 1.3.1微量金屬元素 15 1.3.2細胞對金屬逆境之調節 17 1.4 研究動機與方向 18 第二章 材料與方法 20 2.1實驗材料 20 2.1.1 大腸桿菌菌株 20 2.1.2 真核細胞株 20 2.2 目標基因表現載體之建構 21 2.2.1 真核表現系統載體 21 2.2.2 原核表現系統載體 22 2.2.3 核酸引子設計 22 2.2.4 聚合酶鏈鎖反應 23 2.2.5 限制酶切反應 24 2.2.6 接合反應 25 2.3 原核宿主細胞表現系統 26 2.3.1 化學法勝任細胞製備 26 2.3.2 大腸桿菌細胞轉形 27 2.3.3 重組蛋白質誘導表現 28 2.4 重組蛋白質之純化方法 29 2.4.1 His6-tag重組蛋白質親和性層析法 30 2.4.2 GST-tag 重組蛋白質親和性層析法 31 2.4.3蛋白質脫鹽與濃縮 31 2.5真核宿主細胞表現系統 32 2.5.1 動物細胞培養 32 2.5.2 真核細胞轉染 34 2.5.3 細胞冷凍保存 35 2.6 核酸基本操作方法 36 2.6.1 信息RNA (mRNA) 純化與製備 36 2.6.2 反轉錄聚合酶鏈鎖反應 (RT-PCR) 38 2.6.3 小量質體 DNA 製備 39 2.6.4 洋菜膠體電泳 40 2.6.5 核酸定量 41 2.6.6 核酸純化套組 42 2.7 蛋白質相關基本操作方法 43 2.7.1 蛋白質定量 43 2.7.2 蛋白質電泳檢定 44 2.7.3 二維蛋白質電泳 45 2.7.4 蛋白質電泳膠片染色法 50 2.7.5 蛋白質轉印法 51 2.7.6 免疫染色法 52 2.7.7免疫染色退染法 53 2.7.8 免疫沉澱 53 2.8 SUMO蛋白質水解酶活性測試 55 2.9大腸桿菌SUMO化系統 56 第三章 結果 57 3.1 in vitro去SUMO化系統建立 57 3.1.1 SUMO2-GC26表現質體建構 57 3.1.2 SUMO2-GC26重組蛋白質表現與純化 57 3.1.3 ULP1-C275 重組蛋白質表現與活性分析 58 3.1.4 ESD4-C268 表現載體之建構 59 3.1.5 ESD4-C268 重組蛋白質表現與活性分析 60 3.1.6 SUMO專一性蛋白酶溶離效率測試 61 3.2 金屬逆境壓力對細胞蛋白質SUMO化影響之探討 61 3.2.1砷逆境壓力對細胞內蛋白質SUMO化電泳分析 62 3.2.2鋅逆境壓力對細胞內蛋白質SUMO化電泳分析 63 3.2.3鎘逆境壓力對細胞內蛋白質SUMO化電泳分析 64 3.3 SUMO化蛋白質之二維電泳分析 64 3.3.1 二維電泳分析條件之測試 64 3.3.2砷逆境壓力對細胞蛋白質SUMO化二維電泳分析 65 3.4真核細胞胞內SUMO-2耦合蛋白質之分析 65 3.4.1細胞胞內SUMO化蛋白質之二維電泳分析 65 3.4.2質譜儀分析之結果 65 3.4 19S蛋白解體次單元體Rpt3與Rpt5之SUMO化研究 66 3.5.1 細胞胞內Rpt5之SUMO化之電泳分析 66 3.5.2 pcDNA6-Rpt5與pcDNA6-Rpt3之表載體之建構 66 3.5.3 Rpt5 in vivo SUMO化測試 67 3.5.4 pET28-Rpt3與pET28-Rpt5之表現載體建構 68 3.5.5利用大腸桿菌SUMO化系統證明Rpt3與Rpt5受SUMO化修飾 69 3.6 蛋白解體次單元體之SUMO化研究 70 3.6.1 蛋白解體次單元之SUMO保留性序列分析 70 3.6.2 20S蛋白解體a次單元in vivo SUMO化測試 70 第四章 討論 72 4.1阿拉伯芥之SUMO蛋白酶表現與純化 72 4.2無法利用SENP1作為SUMO受質純化系統中之去SUMO酵素 72 4.3砷逆境造成蛋白質SUMO化修飾程度上升 73 4.4 SUMO之耦合蛋白質之二維電泳分析與身份鑑定 74 4.5 Rpt5之SUMO化修飾可能扮演之生理角色 75 4.6無法以共轉染方式於細胞內表現Rpt3 76 4.7其他蛋白解體次單元受SUMO化修飾之可能性 76 未來展望 77 參考文獻 78 圖與表 85 碩士論文口試問答摘要 120 | |
| dc.language.iso | zh-TW | |
| dc.subject | 蛋白解體 | zh_TW |
| dc.subject | SUMO化修飾作用 | zh_TW |
| dc.subject | 蛋白質體學 | zh_TW |
| dc.subject | 金屬逆境 | zh_TW |
| dc.subject | SUMO | en |
| dc.subject | Proteasome | en |
| dc.subject | Rpt | en |
| dc.subject | Heavy metal stress | en |
| dc.subject | Proteomics | en |
| dc.title | 哺乳類動物細胞中SUMO結合受質之蛋白質體學研究 | zh_TW |
| dc.title | The Proteomics Study of the SUMO-conjugated Substrates in Mammalian Cells | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 97-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 莊榮輝(Rong-Huay Juang),陳威戎(Wei-Jung Chen),張麗冠(Li-Kwan Chang) | |
| dc.subject.keyword | SUMO化修飾作用,蛋白質體學,金屬逆境,蛋白解體, | zh_TW |
| dc.subject.keyword | SUMO,Proteomics,Heavy metal stress,Proteasome,Rpt, | en |
| dc.relation.page | 122 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2009-07-30 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 微生物與生化學研究所 | zh_TW |
| 顯示於系所單位： | 微生物學科所 | |
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