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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張世宗 | |
| dc.contributor.author | Nien-Ming Chen | en |
| dc.contributor.author | 陳年明 | zh_TW |
| dc.date.accessioned | 2021-06-15T05:03:56Z | - |
| dc.date.available | 2014-09-18 | |
| dc.date.copyright | 2011-09-18 | |
| dc.date.issued | 2011 | |
| dc.date.submitted | 2011-08-23 | |
| dc.identifier.citation | 蔡佳芸 (2009) 胞外 SUMO 化系統之建立與多 SUMO 化機制之探討，碩士論文，國立臺灣大學微生物與生化學研究所
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/46330 | - |
| dc.description.abstract | 透過SUMO化修飾目標蛋白質或以 SUMO 專一性蛋白酶 (SUMO/Sentrin-specific proteases, SENPs) 進行其可逆性移除乃是細胞內重要的蛋白質修飾作用。與泛素化修飾相同，SUMO 化修飾亦調控了細胞中許多重要功能，包括影響蛋白質間之交互作用與穩定性等。已知泛素可透過不同位置形成聚合長鏈，且其具有不同的生理意義，而 SUMO 化修飾雖被證實亦可形成多 SUMO 長鏈，然其生理角色與形成機制仍不十分清楚。
本論文透過將 SUMO 化修飾所需之各酵素轉形至大腸桿菌中，建立一不受 SENPs 所調節的 SUMO 化修飾反應系統，進行多 SUMO 化修飾的觀察與探討。結果顯示，在所建立的系統中，被認為無法形成聚合長鏈的 SUMO1 可透過非保守性 SUMO 化修飾作用於特定離胺酸形成聚合長鏈，且其生成的位置偏好發生於結構鬆散的 N 端，顯示空間上的障礙乃是影響多 SUMO 長鏈生成的重要因素。為探討各 SENP 對於多 SUMO 長鏈降解之影響，本論文以細胞外 SENP 活性分析發現，除 SENP5 外，各 SENP 其 C 端蛋白酶活性區皆可水解多 SUMO1 及多 SUMO2 長鏈，而其中 SENP1、SENP2 水解兩種 SUMO 長鏈之活性並無顯著差異。由於先前研究多認為 SENP1 及 SENP2 不具有降解多 SUMO 長鏈的能力，本論文所得結果顯示降解多 SUMO 長鏈的活性廣泛存在於大多數 SENP 保守性的活性區中。此外，本研究亦發現 SENP6、SENP7 蛋白酶活性區水解多 SUMO2 長鏈的活性較多 SUMO1 為佳，顯示其活性區與受質專一性有關。 | zh_TW |
| dc.description.abstract | The conjugation of SUMO moiety by SUMO conjugation system and the removal of the moiety by SENPs are important aspects of protein modification in cells. Analogous to ubiquitination, sumoylation regulates many physiological functions of proteins. It has been demonstrated that ubiquitin can form various polymeric chains via specific lysines to execute distinct functions. Although certain types of polymeric SUMO chains have been described, their roles in biological processes and the mechanism of formation remain unclear.
In this study, I transformed the enzymes required for sumoylation into Escherichia coli BL21 (DE3) to establish a sumoylation system, which lacks SENP-mediated desumoylation for analyzing the formation of polymeric SUMO chains. The results suggest that SUMO1, which has been considered unable to form polymers, is able to form polymeric chains mainly through self-conjugation at specific lysine residues nearby the flexible N terminus, indicating that the steric hindrance is a key factor modulating polySUMO chains formation. To investigate the character of polySUMO degradation catalyzed by SENPs, I examined the degradation of polySUMO chains by conducting the in vitro SENP activity analysis. The data showed that the catalytic domains of all SENPs, except SENP5, are able to deconjugate both polySUMO1 chains and polySUMO2 chains. Moreover, the catalytic core of SENP1 and SENP2 present similar preference toward polySUMO1 and polySUMO2 chains. I also found that the catalytic cores of SENP6 and SENP7 exhibit an exquisite substrate selectivity that polySUMO2 chains are deconjugated more efficiently than polySUMO1 chains. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T05:03:56Z (GMT). No. of bitstreams: 1 ntu-100-R98b47204-1.pdf: 17050382 bytes, checksum: 7e77cc769daa62a00c1155d6030fbf41 (MD5) Previous issue date: 2011 | en |
| dc.description.tableofcontents | 摘要 i
Abstract ii 縮寫表…… iii 第一章 緒論 1 1.1 類泛素蛋白質 1 1.2 SUMO 化作用 1 1.2.1 SUMO 及其修飾機制 1 1.2.2 多 SUMO 聚合長鏈 3 1.2.3 SUMO 化修飾之生理作用 4 1.3 SUMO專一性蛋白酶 (SENPs) 6 1.3.1 SENPs 分類 6 1.3.2 SENPs 催化活性與作用機制 7 1.3.3 SENPs 之生理作用 7 1.4 研究動機與方向 8 第二章 材料與方法 10 2.1 質體建構 10 2.1.1 野生型 SUMO1 及其單一離胺酸突變株之重組質體建構 10 2.1.2 野生型 SUMO1 及 SUMO2 聚合長鏈表現質體 10 2.1.3 螢光蛋白標誌之多 SUMO1 長鏈表現質體 11 2.1.4 SUMO 專一性蛋白酶表現質體 11 2.2 大腸桿菌 SUMO 化修飾系統 12 2.3 重組蛋白質表現與純化 12 2.3.1 野生型 SUMO1 及其突變株聚合長鏈的表現與純化 12 2.3.2 螢光蛋白標誌之SUMO1表現與純化 13 2.3.3 螢光蛋白標誌之多 SUMO1 長鏈的表現與純化 13 2.3.4 各 SENP 之表現與純化 13 2.4 SENP之活性分析 14 2.5 以螢光共振能量轉移分析 SENP 水解多 SUMO1 長鏈之活性 14 第三章 結果 16 3.1各離胺酸對於多 SUMO1 長鏈生成之影響 16 3.1.1 以 pQE30-His-SUMO1 為表現質體 16 3.1.2 以 pET30a-His-SUMO1 為表現質體 16 3.1.3 以 pET30a-HA-SUMO1 為表現質體 17 3.2各 SENP 對於多 SUMO 長鏈之水解活性分析 18 3.2.1 SENP3 重組質體之建構 18 3.2.2 多 SUMO1 及多SUMO2 長鏈及各 SENP 之表現與純化 19 3.2.3 SENPs 對於多 SUMO長鏈之水解活性分析 19 3.3 SENP1 對螢光蛋白標誌之多 SUMO1 長鏈水解活性 19 3.3.1 螢光蛋白標誌之多 SUMO1 長鏈的純化 19 3.3.2 以免疫染色法檢視 SENP1 水解受質之活性 20 3.3.3 以螢光共振能量轉移作為指標分析 SENP1 水解受質之活性 20 第四章 討論 22 4.1多 SUMO1 長鏈的生成屬於非保守性 SUMO 化修飾 22 4.2多 SUMO1 長鏈的生成與特定胺基酸有關 23 4.3 SUMO 化修飾系統亦為 SUMO 化修飾調控之標的 24 4.4除 SENP5, 各SENP 活性區皆可降解多 SUMO 長鏈 24 4.5 SENP1 及 SENP2 之 N 端會影響其受質辨識及 chain editing 的能力 25 4.6 SENP 6與 SENP7 蛋白酶活性區會影響其受質專一性 25 4.7無法順利透過螢光共振能量轉移分析 SENPs 之活性 26 第五章 未來展望 28 參考文獻 29 表與圖……………………………………………………………………………………………………………………….35 附錄….……………………………………………………………………………………………………………………....56 | |
| dc.language.iso | zh-TW | |
| dc.subject | SUMO專一性蛋白酶 | zh_TW |
| dc.subject | 聚合長鏈 | zh_TW |
| dc.subject | SUMO化修飾 | zh_TW |
| dc.subject | Polymeric chains | en |
| dc.subject | SUMO | en |
| dc.subject | SENPs | en |
| dc.title | SUMO1自我長鏈聚合之研究與SENPs降解多SUMO長鏈
之性質分析 | zh_TW |
| dc.title | Study of the Self-polymerization of SUMO1 and Characterization of the PolySUMO Chain Degradation Catalyzed by SENPs | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 99-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 莊榮輝,陳威戎,張麗冠,鄭貽生 | |
| dc.subject.keyword | SUMO化修飾,SUMO專一性蛋白酶,聚合長鏈, | zh_TW |
| dc.subject.keyword | SUMO,SENPs,Polymeric chains, | en |
| dc.relation.page | 61 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2011-08-23 | |
| 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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