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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 鄭貽生(Yi-Sheng Cheng) | |
dc.contributor.author | Ting-Chun Liu | en |
dc.contributor.author | 劉庭君 | zh_TW |
dc.date.accessioned | 2021-06-17T08:07:56Z | - |
dc.date.available | 2021-08-20 | |
dc.date.copyright | 2019-08-20 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-08-18 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/73679 | - |
dc.description.abstract | 阿拉伯芥組蛋白去乙醯基酶15 (Histone deacetylase 15, HDA15)為RDP3/HDAC1-like家族中的第二群組蛋白去乙醯基酶,HDA15去乙醯基功能區 (histone deacetylase domain, HD)之四聚體結構已由本實驗室解析完成,研究指出去乙醯基功能區的HDA15重組蛋白 (HD)以四聚體及單元體形式存在,而具有鋅手指區 (zinc finger domain)的去乙醯基功能區的HDA15重組蛋白 (ZFHD)會以二聚體形式存在,ZFHD二聚體酵素活性(kcat)較HD四聚體形式高40倍;另外HDA15之Ser448及Ser452為磷酸化位點,在in vitro或in vivo之實驗中,HDA15被磷酸化後,會改以單元體形式存在並造成酵素活性消失;由於HDA15磷酸化造成多聚體與活性改變的關連性尚未被探討,因此本研究以點突變分析位於二聚體及四聚體介面之胺基酸,結合酵素動力學及蛋白質結構分析,探討HDA15多聚體之形成與酵素活性的關連性。本研究針對三區進行點突變,1) loop1中央之單點突變E163A、E165A僅影響HD四聚體的形成而不影響ZFHD二聚體構型,同樣於loop1中央之單點突變Q169A皆不影響HD及ZFHD之多聚體形成;2)位於β2之Y228與Y230雙突變造成ZFHD以單元體形式存在而無法形成二聚體;3)單點突變近α2之loop1上E173A及α2上的R177A,兩者皆位在二聚體介面及活性位點,同時造成ZFHD無法形成二聚體以及活性下降。分析S448及S452磷酸化位點、去乙醯基酶活性區與二聚體在結構上的氫鍵網絡,可以發現磷酸化位點與去乙醯基酶活性區之胺基酸,以直接或間接方式連結至loop1或β2,本研究綜合胺基酸位點突變數據及氫鍵網絡分析證明HDA15之酵素活性與多聚體之形成可受到磷酸化調節之能力。 | zh_TW |
dc.description.abstract | Arabidopsis histone deacetylase 15 (HDA15) belongs to the class II of histone deacetylase in the RDP3/HDAC1-like family. The tetrameric structure of HDA15 HD has been resolved by our colleagues. Previous study revealed that different oligomerization states of histone deacetylase domain (HD) and zinc finger with histone deacetylase domain (ZFHD) could be observed. HDA15 HD contains tetramer and monomer while ZFHD is dimer. The enzyme activity (kcat) of ZFHD dimer is higher 40-foldthan that of HD tetramer. Moreover, two phosphorylation sites S448 and S452 with phosphomimetic would form monomer and result in loss of HDAC activity in vitro and in vivo. It is unknown about how to regulate oligomerization and enzyme activity of HDA15 by phosphorylation. Therefore, the study used site-directed mutagenesis of the key residues at the dimer and tetramer interface to explore the relationship between oligomerization and enzyme activity of HDA15. Three regions for point mutation are difined: 1) the single mutants E163A and E165A at loop1 would disrupt the formation of HD tetramer, but didn’t affect the dimer of ZFHD. The single mutant Q169A at loop 1 didn’t show any alterations. 2) The double mutant of Y228A/Y230A at β2 caused ZFHD from dimer to monomer. 3) The single mutants E173A at loop1 adjacent α2 and R177A at α2 located between the dimer interface and the active site would simultaneously disrupt oligomerization and enzyme activity. Analysis of phosphorylation sites (S448 and S452), active site, and dimer interface revealed that the loop1 and β2 are connected by several hydrogen bonds directly and indirectly. Therefore, the study provided the evidences to show how the enzyme activity and oligomerization of HDA15 could be regulated by phosphorylation via the hydrogen bond network. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T08:07:56Z (GMT). No. of bitstreams: 1 ntu-108-R05b21015-1.pdf: 10329433 bytes, checksum: 6b9f397a561f87c1d54fab06cadf13e2 (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | 口試委員審定書 I
誌謝 II 中文摘要 III Abstract IV 縮寫對照表 V HDA15點突變位點對照表 VI 目錄 VII 圖目錄 X 表目錄 XII 第一章 前言 1 1-1 表觀遺傳學 (Epigenetics) 1 1-2 組蛋白轉譯後修飾與作用機制 1 1-3 蛋白質多聚體之形成 (Oligomerization) 2 1-4 組蛋白乙醯基化 (Histone acetylation)與去乙醯基化 (Histone deacetylation) 2 1-5 組蛋白去乙醯基酶 (Histone deacetylase, HDAC) 3 1-6 阿拉伯芥中組蛋白去乙醯基酶 3 1-7 阿拉伯芥組蛋白去乙醯基酶15 (Arabidopsis thaliana Histone deacetylase 15, AtHDA15) 6 1-8 阿拉伯芥組蛋白去乙醯基酶15之去乙醯基酶功能區多聚體形式、結構與活性分析 7 1-9 去乙醯基酶的鋅手指 8 1-10 HDA15 Ser448、Ser452磷酸化研究 9 1-11 研究方向及目標 9 第二章 材料與方法 11 2-1 實驗材料 11 2-1-1 菌種 11 2-1-2 質體 11 2-1-3 藥品 11 2-2 實驗方法 11 2-2-1 大腸桿菌勝任細胞製備 (competent cell preparation) 11 2-2-2 大腸桿菌之轉型作用 (transformation) 12 2-2-3 DNA質體萃取 12 2-2-4 阿拉伯芥Class II HDA功能區(HD)及鋅手指HDA功能區(ZFHD)突變質體之製備與構築 12 2-2-5 重組蛋白質之大量表現 (over-expression) 13 2-2-6 重組蛋白質之純化 13 2-2-7 SDS-聚丙烯醯胺膠體電泳 (Sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDS-PAGE) 15 2-2-8 膠體管柱層析Superdex-200標準品線性公式 15 2-2-9 蛋白質定量分析 15 2-2-10 去乙醯基酶之酵素動力學分析 16 2-2-10-1去乙醯基受質(Boc-Lys-AMC)標準曲線 16 2-2-10-2酵素活性檢測 16 2-2-11 鋅手指功能區之模擬結構 18 第三章 結果 19 3-1 HDA15 HD蛋白質結構分析各單元體介面之胺基酸 19 3-2 HDA15 HD蛋白質純化、聚合形式分析及去乙醯基酵素動力學檢測 20 3-3 HD-E163A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 21 3-4 HD-E165A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 21 3-5 HD-Q169A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 22 3-6 HD-E173A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 23 3-7 HDA15 ZFHD蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 24 3-8 ZFHD-E163A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 25 3-9 ZFHD-E165A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 25 3-10 ZFHD-Q169A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 26 3-11 ZFHD-Y228A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 27 3-12 ZFHD-Y230A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 28 3-13 雙突變ZFHD-Y228A/Y230A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 29 3-14 ZFHD-E173A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 29 3-15 ZFHD-R177A蛋白質純化、多聚體分析及去乙醯基酵素動力學檢測 30 3-16 鋅手指功能區之模擬結構 31 第四章 討論 32 4-1 E163及E165 影響HD四聚體形成,但不影響ZFHD二聚體形成 32 4-2 Y228及Y230可協助ZFHD形成二聚體 33 4-3 鋅手指功能區之模擬結構說明ZFHD的二聚體形成方式 34 4-4 E173A對ZFHD形成二聚體之影響 34 4-5 R177A 影響ZFHD二聚體形成並降低去乙醯基酶活性 35 4-6 HD磷酸化位點、活性區與多聚體交界區之氫鍵網絡 35 第五章 結論 38 參考文獻 39 圖表 45 附錄 97 | |
dc.language.iso | zh-TW | |
dc.title | 阿拉伯芥組蛋白去乙醯基酶HDA15多聚體與酵素活性之關鍵胺基酸研究 | zh_TW |
dc.title | Study on the key residues of oligomerization and enzyme activity of Arabidopsis Histone Deacetylase 15 | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 吳克強(Keqiang Wu),王雅筠(Ya-Yun Wang),張世宗(Shih-Chung Chang),蔡麗珠(Li-Chu Tsai) | |
dc.subject.keyword | 阿拉伯芥,組蛋白去乙醯基?,HDA15,多聚體形成, | zh_TW |
dc.subject.keyword | Arabidopsis,Histone Deacetylase,HDA15,oligomerization, | en |
dc.relation.page | 107 | |
dc.identifier.doi | 10.6342/NTU201903581 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2019-08-18 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生命科學系 | zh_TW |
顯示於系所單位: | 生命科學系 |
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