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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張世宗 | |
| dc.contributor.author | Yun-Hsuan Liu | en |
| dc.contributor.author | 劉昀瑄 | zh_TW |
| dc.date.accessioned | 2021-06-13T01:17:26Z | - |
| dc.date.available | 2011-08-11 | |
| dc.date.copyright | 2011-08-11 | |
| dc.date.issued | 2011 | |
| dc.date.submitted | 2011-08-03 | |
| dc.identifier.citation | 劉邦宇 (2009) 哺乳類動物細胞中SUMO結合受質之蛋白質體學研究。碩士論文，國立台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/123456789/29752 | - |
| dc.description.abstract | Rpt5 (Regulatory particle triple-A ATPase 5) is one of the 19S proteasomal ATPase subunits, which forms the 19S base together with Rpt1, Rpt2, Rpt3, Rpt4 and Rpt6. Rpts modulate the functions of recognizing polyubiquitin chain, substrate unfolding, gate opening of the 20S core particle, and translocation of target proteins.
Our previous findings have shown that Rpt3 and Rpt5 were SUMOylated by SUMO1 (small ubiquitin-like modifier 1) and SUMO2 (small ubiquitin-like modifier 2). In this study, by expressing truncated Rpt5 fragments in the Escherichia coli SUMOylation system, the results reveal that there are two lysine residues located in the Rpt51-242 and Rpt5243-355 regions are the potential SUMOylation sites. Notably, K56 located in the SUMOylation consensus motif of Rpt5 is not the SUMOylated site. By using site-directed mutagenesis at nine lysine residues within Rpt5243-355, the data showed that K294 might be the lysine residue for SUMO conjugation. Rpt5 contains six putative SUMO interacting motifs (SIM), herein named SIM1-6. The SUMOylation level of Rpt5 is markedly reduced as substituting the hydrophobic residues of SIMs to alanine. Among six SIMs, SIM5 seems to play the most significant role in mediating Rpt5 SUMOylation. In addition to Rpt3 and Rpt5, this study also showed that Rpt2 was SUMOylated by SUMO1 in the E. coli SUMOylation system. However, it remains unclear that whether Rpt1, Rpt4 and Rpt6 are SUMOylated or not, since they cannot be expressed properly in the E. coli SUMOylation system. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T01:17:26Z (GMT). No. of bitstreams: 1 ntu-100-R98b47205-1.pdf: 1692976 bytes, checksum: 385521d21f4b455cb4ea4d0c60343bfa (MD5) Previous issue date: 2011 | en |
| dc.description.tableofcontents | 中文摘要 i
Abstract ii 縮寫表 iii 第一章 緒論 1 1.1 蛋白酶體的組成 1 1.2 蛋白酶體之轉譯後修飾作用 2 1.3 SUMO (small ubiquitin-like modifier) 3 1.4 SUMO 與 SUMO化作用 3 1.5 哺乳動物之SUMO蛋白質 4 1.6 去SUMO化作用 4 1.7 Consensus motifs of SUMOylation 5 1.8 SUMO-interacting motif (SIM) 6 1.9 研究動機 7 第二章 材料與方法 8 2.1 基因選殖與質體DNA建構 8 2.1.1 基因選殖 8 2.1.2 質體DNA建構 8 2.2 大腸桿菌SUMO修飾系統 8 2.3 His-Tag binding agarose pull-down assay 9 2.4 利用Discovery Studio TM模擬Rpt5之結構 9 第三章 結果 10 3.1 鑑定Rpt5受SUMO修飾的位置 10 3.1.1 在大腸桿菌SUMO修飾系統中表現Rpt5 10 3.1.2 表現Rpt5-K56R 於大腸桿菌SUMO修飾系統 10 3.1.3 表現不同長度的Rpt5以探討Rpt5受SUMO修飾的位置 11 3.1.4 以定位點突變法鑑定Rpt5受SUMO修飾的位置 11 3.2 鑑定 Rpt5之SIM片段 12 3.2.1 利用點突變法鑑定Rpt5之SIM 12 3.3 19S Rpt ATPase受SUMO修飾之情形 12 3.3.1 Rpt1、Rpt2、Rpt4與Rpt6之基因選殖 12 3.3.2 表現並觀察Rpt1、Rpt2、Rpt4與Rpt6受SUMO修飾之情形 13 第四章 討論 14 4.1 Rpt5中至少有兩個Lys會受到SUMO的修飾 14 4.2 Rpt5的SUMO化並非發生於保守性基序中的Lys 14 4.3 Rpt5受SUMO修飾後可能會發生結構上的改變 15 4.4 大腸桿菌SUMO修飾系統的非專一性修飾現象 15 4.5 Rpt5受到SUMO修飾的機制可能與SIM有關 16 4.6 於大腸桿菌系統中無法順利表現Rpt1、Rpt4和Rpt6 16 第五章 未來展望 17 參考文獻 18 圖與表 27 附錄 39 論士論文口試問答摘要 47 | |
| dc.language.iso | zh-TW | |
| dc.subject | Rpt | zh_TW |
| dc.subject | SIM | zh_TW |
| dc.subject | SUMO化修飾 | zh_TW |
| dc.subject | AAA ATPase | zh_TW |
| dc.subject | SUMOylation | en |
| dc.subject | SIM | en |
| dc.subject | AAA ATPase | en |
| dc.subject | Rpt | en |
| dc.title | 蛋白酶體19S Rpt5 ATPase受SUMO化修飾之研究 | zh_TW |
| dc.title | Study of the SUMOylation of 19S Proteasomal Rpt5 ATPase | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 99-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 莊榮輝,張麗冠,陳威戎,鄭貽生 | |
| dc.subject.keyword | Rpt,SUMO化修飾,AAA ATPase,SIM, | zh_TW |
| dc.subject.keyword | Rpt,SUMOylation,AAA ATPase,SIM, | en |
| dc.relation.page | 48 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2011-08-03 | |
| 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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