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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張世宗(Shih-Chung Chang) | |
dc.contributor.author | Yung-Cheng Shin | en |
dc.contributor.author | 辛永誠 | zh_TW |
dc.date.accessioned | 2021-06-17T01:50:07Z | - |
dc.date.available | 2019-07-27 | |
dc.date.copyright | 2017-07-27 | |
dc.date.issued | 2017 | |
dc.date.submitted | 2017-07-25 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/67791 | - |
dc.description.abstract | 已知有超過十種以上的類泛素蛋白質,其胺基酸序列與立體結構皆與泛素有很高的相似性,但是在細胞內確具有不同的的生理功能。類泛素蛋白質中以NEDD8 (Neural Precursor Cell Expressed, Developmentally Down-Regulated 8) 與ubiquitin (Ub) 的序列相似度最高 (有高達80%的胺基酸序列相同),然而各自的專屬蛋白酶SENP8與USP2卻仍可專一性地針對NEDD8或Ub進行反應。研究指出當蛋白質產生錯誤的NEDD8或Ub修飾時,可能會導致疾病的發生,故探討不同類泛素蛋白質的專一性辨識機制是相當重要的研究課題。本研究以單胞綠藻之bi-ubiquitin CrRUB1 (Chlamydomonas reinhardtii related to ubiquitin 1;其原態為Ub與NEDD8之融合蛋白質) 為基質,利用定位點突變技術將NEDD8與Ub相對應的51及72號胺基酸互換並進行活性分析,發現51號及72號胺基酸分別為SENP8辨識其基質的主要及次要位置,但是這兩個胺基酸的突變並未影響USP2的活性,顯示USP2與SENP8具有不同的基質辨識機制。分析人類USP2與Ub共結晶之結構發現,Ub第4、12與14號胺基酸可與USP2產生交互作用,而且這三個位置的序列也與NEDD8完全不同,故將人類Ub之4、12及14號的胺基酸突變為人類NEDD8之相對應的序列,發現USP2無法有效地水解這些突變株;而將NEDD8之4、12及14號的胺基酸分別突變為Ub之相對應序列後則可被USP2水解,顯示此三個位點是USP2辨識基質的重要胺基酸序列。此外,活性區的重要胺基酸序列及結構與USP2高度相似之USP21也具有相同之基質辨識機制。然而,Ub之 E1-activating enzyme Ube1仍可作用於NEDD8及本實驗所使用之Ub突變株,顯示並非所有參與泛素化修飾之酵素,都具有分辨Ub與NEDD8的能力。 | zh_TW |
dc.description.abstract | There are more than ten kinds of ubiquitin-like proteins (Ubls) have been found. Ubls have high similarity of amino acid sequences and three-dimensional structures with ubiquitin, but perform different physiological functions in cells. NEDD8 (Neural Precursor Cell Expressed, Developmentally Down-Regulated 8) and ubiquitin (Ub) have the highest similarity (up to 80%) among different Ubls, whereas the respective proteases SENP8 and USP2 still can react to NEDD8 or Ub correctly. Studies have shown that when proteins with wrong NEDD8 or Ub modification will possibly lead to disease, so it’s important to explore the specific identification mechanism between NEDD8 and Ub modification systems. In the present study, the fusion protein of Ub and NEDD8, CrRUB1 (Chlamydomonas reinhardtii related to ubiquitin 1), was utilized as the substrate for investigating the catalytic specificity of SENP8. By using the site-directed mutagenesis method for replacing the amino acid residues 51 and 72 of CrNEDD8 with their CrUb equivalents, and vice versa, the experimental results showed that CrNEDD8 with N51E/A72R mutations was not cleaved by SENP8, but CrUb with E51N/R72A mutations was efficiently cleaved by SENP8, implying that residues 51 and 72 are the major determinants for specific recognition by SENP8. However, the mutation of residues 51 and 72 of CrNEDD8 and CrUb didn’t largely influence the activity of USP2, suggesting that USP2 and SENP8 have different substrate identification mechanism. The three-dimensional structure of human USP2 and Ub reveals that residues 4, 12 and 14 of Ub could interact with USP2, and these three residues were not conserved in NEDD8. The experimental results showed that Ub4K/12E/14E/72A mutant was not cleaved by USP2, but N84F/12T/14T/72A mutant was efficiently cleaved by USP2, indicating that these four residues were the important determinants for distinguishing between ubiquitin and NEDD8 by USP2. In addition, USP21 also displays the same substrate recognition mechanism. In contrast, Ub E1-activating enzyme Ube1 can still react to NEDD8 and the Ub4K/12E/14E/72A mutant, suggesting that not all the enzymes involved in ubiquitination pathway have the ability to distinguish Ub and NEDD8. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T01:50:07Z (GMT). No. of bitstreams: 1 ntu-106-D01b22009-1.pdf: 3960625 bytes, checksum: 7f0684c3ae34e32b88a18473ee57737e (MD5) Previous issue date: 2017 | en |
dc.description.tableofcontents | 中文摘要 I
Abstract II 縮寫表 III 第一章 緒論 1 1.1 泛素與類泛素蛋白質 1 1.1.1 泛素修飾系統 2 1.1.2 NEDD8修飾系統 3 1.2 類泛素蛋白質胜肽酶 4 1.2.1去泛素化酵素 5 1.2.2 NEDD8蛋白酶 12 1.2.3 DUBs與疾病治療 13 1.3 泛素與NEDD8在細胞內之交互作用 17 1.3.1 Neddylation調控Cullin RING E3 ligases活性 17 1.3.2泛素化及Neddylation調控MDM2及下游蛋白質生理功能 19 1.3.3 Neddylation可以經由泛素化修飾過程發生 20 1.4 研究動機 21 第二章 材料與方法 24 2.1單胞微藻 (Chlamydomonas reinhardtii) 與培養條件 24 2.2 表現載體之建構 24 2.2.1 Total mRNA分離及反轉錄聚合酶連鎖反應 24 2.2.2聚合酶鏈鎖反應 25 2.2.3 限制酶切反應 25 2.2.4 接合反應 25 2.2.5勝任細胞之製備 26 2.2.6 質體之轉形 26 2.2.7質體DNA製備 27 2.2.8 洋菜糖膠體電泳 27 2.2.9 DNA 片段之分離純化法 28 2.2.10 DNA定量 28 2.3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 Hisx6親和層析法 29 2.4.2 GST親和層析法 29 2.4.3 蛋白質脫鹽與濃縮 30 2.5蛋白質相關基本操作方法 30 2.5.1蛋白質定量 30 2.5.2 蛋白質電泳檢定 30 2.5.3 Coomassie Brilliant Blue R-250蛋白質染色法 31 2.5.4 蛋白質電泳轉印 31 2.5.5 酵素免疫染色法 32 2.6去泛素化酵素對泛素和NEDD8之基質專一性分析 33 2.6.1 SENP8之基質專一性分析 33 2.6.2 USP2之基質專一性分析 33 2.7泛素化酵素E1對泛素之基質專一性分析 33 第三章 結果 34 3.1 CRRUB1基因選殖與表現質體之建構 34 3.2 SENP8對泛素與NEDD8之辨識機制 34 3.3 USP2對泛素與NEDD8之辨識機制 36 3.4 USP21對泛素與NEDD8之辨識機制 38 3.5 泛素活化酶專一性泛素化酵素UBE1對泛素與NEDD8之辨識機制 39 第四章 討論 40 參考文獻 49 圖與表 66 附錄 87 | |
dc.language.iso | zh-TW | |
dc.title | 類泛素蛋白酶之基質專一性辨識分子機制研究 | zh_TW |
dc.title | Study on the molecular mechanism for substrate specific recognition by ubiquitin-like protein peptidases | en |
dc.type | Thesis | |
dc.date.schoolyear | 105-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 楊健志,徐駿森,張麗冠,林翰佳,廖憶純 | |
dc.subject.keyword | 泛素, | zh_TW |
dc.subject.keyword | Ubiquitin,NEDD8,USP2,SENP8, | en |
dc.relation.page | 99 | |
dc.identifier.doi | 10.6342/NTU201701402 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2017-07-25 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生化科技學系 | zh_TW |
顯示於系所單位: | 生化科技學系 |
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