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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 莊榮輝 | |
| dc.contributor.author | Yi-Chen Lin | en |
| dc.contributor.author | 林怡岑 | zh_TW |
| dc.date.accessioned | 2021-06-17T00:23:43Z | - |
| dc.date.available | 2022-05-17 | |
| dc.date.copyright | 2012-06-27 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-05-22 | |
| dc.identifier.citation | 莊榮輝 (1985) 水稻蔗糖合成酶之研究
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/66153 | - |
| dc.description.abstract | 蛋白質的轉譯後修飾調控了許多重要的生理機制。早期研究顯示質體型澱粉磷解酶 (L-SP) 可能受到蛋白質降解性後修飾作用所調控。本實驗室在純化L-SP的過程中，發現一高分子量、且具有L-SP活性之色帶 (簡稱HX)。本論文進一步利用免疫共沉澱與免疫螢光組織定位等方法，證明HX由L-SP與20S proteasome所組成。並且在45°C熱處理下，HX會立即消失，可觀察到L-SP隨著熱處理的時間增加，發生階段性降解的現象，這個降解作用可隨著20 proteasome的活性受到proteasome專一性抑制劑 (MG132) 的抑制，而減緩L-SP之降解，顯示20S proteasome可能參與此降解作用。以酵素動力學分析降解前後L-SP之生化性質差異，發現降解後的L-SP對於Glc-1-P的親和力下降，進而降低澱粉合成方向的活性。因此我們推測20S proteasome可能會受到熱逆境的刺激，進而以降解機制修飾L-SP，來調控L-SP催化方向之活性。
另一方面，以L-SP單株抗體進行免疫共沉澱時，意外地發現一個分子量約65 kDa的蛋白質可能也與L-SP互相結合；經LC-MS/MS定序，此蛋白質為DPE1 (D-enzyme, disproportionating enzyme, 4-alpha-glucanotransferase; EC 2.4.1.25)。DPE1催化可逆性的 alpha-1,4鏈結葡聚醣之裂解與轉移反應，改變寡糖之鏈長分布。過去的研究顯示，在E coli中，malQ (DPE1同源基因) 和malP (L-SP同源基因) 位於相同的malA操作組，故推測兩者有類似的功能，可能共同作用。進一步，本論文以二維電泳 (native PAGE/SDS-PAGE)、GST pull-down assay、以及FRET-confocal microscopy為工具，證明L-SP與DPE1互相結合，形成蛋白質複合體 (SP-DPE complexes)。此外，膠體過濾法與二維電泳之結果顯示，SP-DPE complexes可能是由四個L-SP單元體與四個DPE1單元體，結合為一個分子量約為700 kDa之蛋白質複合體。以酵素動力學比較SP-DPE complexes與DPE1之間的差異，顯示SP-DPE complexes對於麥芽三糖 (maltotriose) 具有較高的親和力，而對於麥芽四糖 (maltotetraose) 則有較高的催化效率；而在SP-DPE complexes的酵素催化作用中，則觀察到基質快速轉移的現象。另外SP-DPE complexes在直徑15-20 mm大小之甘藷塊根中含量最多，顯示其與澱粉快速累積有重要的關聯性。這部份的結果顯示，在甘藷塊根的造粉體中，L-SP與DPE1可能形成蛋白質複合體，以幫助澱粉的快速累積，其生理作用可能扮演有效地回收再利用短鏈麥芽寡糖，或直接作用在短鏈分支之澱粉結構中，正確決定澱粉的結構。 | zh_TW |
| dc.description.abstract | Post-translational regulation plays an important role in cellular metabolism. Earlier studies showed that the activity of plastidal starch phosphorylase (L-SP) may be regulated by proteolytic modification. During the purification of L-SP from sweet potato roots, an unknown high molecular weight complex (HX) showing L-SP activity was constantly observed. Its mobility was significantly slower than the typical L-SP on native PAGE. We utilized mass spectrometry, coimmunoprecipitation, Ouchterlony double immunodiffusion, two-dimensional gel electrophoresis, and confocal microscopy as tools to demonstrate that HX was composed of L-SP and the 20S proteasome. Furthermore, we found that the amount of HX decreased immediately after 45°C heat treatment, which caused stepwise degradation of L-SP in a time-dependent mode. This degradation process was strongly inhibited by MG132, suggesting that the 20S proteasome might be involved in L-SP degradation. In addition, kinetic studies indicated that the proteolytic modification of L-SP caused it to decrease the binding affinity toward Glc-1-P and subsequently reduced its starch-synthesizing activity. This work demonstrates the role of the 20S proteasome as a regulator of L-SP activity, which may be controlled by stressful condition.
On the other hand, immunoprecipitation experiments with L-SP mAbs showed that another protein might associate with L-SP. This protein was identified as DPE1 (D-enzyme, disproportionating enzyme, 4-alpha-glucanotransferase; EC 2.4.1.25) by LC/MS/MS. DPE1 catalyses the cleavage and transfer reactions involving alpha-1,4 linked glucans and alters the chain length distribution of oligosaccharides. Previous studies suggested that DPE1 might work in conjunction with L-SP. Furthermore, we utilized 2-DE (native PAGE/SDS-PAGE), GST pull-down assay, and confocal microscopy as tools to demonstrate that L-SP might interact with DPE1, suggesting that these enzymes may form protein complexes (SP-DPE complexes). The results from gel-filtration chromatography and 2-DE (native PAGE/SDS-PAGE) indicated that SP-DPE complexes might be composed of four L-SP subunits and four DPE1 subunits with molecular weight around 700 kDa. In addition, protein complex forms of DPE1 showed a higher affinity toward maltotriose and a higher catalytic activity toward maltotetraose than DPE1 monomers. The efficient passage of the product of one enzyme to the next enzyme in SP-DPE complexes was also be observed. Moreover, the protein levels of SP-DPE complexes were shown to become higher in the middle stage of sweet potato root development where starch accumulated fast. These results suggest that SP-DPE complexes may either efficiently recycle short chain malto-oligosaccharides to produce Glc-1-P for starch synthesis, or may specifically edit short-chain amylopectin, thus resulting in the formation of correct starch structure. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-17T00:23:43Z (GMT). No. of bitstreams: 1 ntu-101-D94b47203-1.pdf: 5292175 bytes, checksum: a629e0b0058d651d10acd58c23710029 (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 誌謝 iii
中文摘要 v 英文摘要 vii 第一章 緒論 1 1.1 澱粉磷解酶 4 1.1.1 澱粉磷解酶之生理功能 7 1.1.2 L型澱粉磷解酶可受到磷酸化修飾 9 1.1.3 磷酸化可能導致澱粉磷解酶經由proteasome路徑降解 11 1.1.4 澱粉磷解酶可能與其他蛋白質形成蛋白質複合體 13 1.2 Ubiquitin/26S Proteasome路徑 15 1.2.1 26S proteasome之基本構造 16 1.2.2 20S proteasome之組成與結構 17 1.2.3 20S proteasome之生化性質 18 1.2.4 19S調節蛋白質之組成與功能 18 1.2.5 Ubiquitin-conjugating system 19 1.2.6 E3 ubiquitin ligases 20 1.3 DPE1 21 1.3.1 DPE1之生理角色 21 1.3.2 DPE1與L-SP 22 1.4 研究動機 24 第二章 材料與方法 27 2.1 實驗材料與藥品試劑 27 2.2 蛋白質定量與酵素活性分析 27 2.3 電泳分析、CBR染色、電泳轉印與免疫染色 27 2.4 2-DE膠體電泳 28 2.5 L-SP與DPE1電泳活性染色法 28 2.6 膠片乾燥法及護貝 29 2.7 甘藷塊根L-SP、20S proteasome以及L-SP高分子量複合體之純化 29 2.8 多源傳統性抗體與單株抗體之製備 30 2.9 免疫沉澱法 31 2.10 膠體內蛋白酶水解與LC/MS/MS分析 31 2.11 甘藷塊根DPE1之選殖 32 2.12 GST Pull-Down Assay 32 2.13 免疫螢光染色 32 2.14 甘藷塊根切片之45°C熱處理 33 2.15 蛋白解體降解試驗 34 2.16 螢光共振能量轉移 (FRET) 34 2.17 以HPLC測定短鏈麥芽寡糖 35 第三章 結果與討論 37 3.1 L-SP受到20S蛋白解體之降解性調控 38 3.1.1 製備20S proteasome傳統性血清 38 3.1.2 以膠體過濾法分析甘藷塊根粗抽萃取蛋白質 40 3.1.3 免疫共沉澱 (Coimmunoprecipitation) 41 3.1.4 L-SP與20S proteasome共存於甘藷塊根之造粉體中 43 3.1.5 45°C熱處理會加速L-SP之降解反應 45 3.1.6 L-SP的降解受到蛋白解體抑制劑的抑制 49 3.1.7 降解修飾後的L-SP對於Glc-1-P的親和力較低 51 3.1.8 L-SP降解性修飾之可能生理角色 52 3.2 澱粉磷解酶與DPE1在澱粉代謝中之交互作用 53 3.2.1 免疫共沉澱實驗 53 3.2.2 製備DPE1單株抗體 56 3.2.3 L-SP高分子量活性色帶以2-DE觀察及LC-MS/MS鑑定 60 3.2.4 L-SP高分子量活性色帶中含有DPE1活性 63 3.2.5 以DPE1單株抗體進行免疫共沉澱 68 3.2.6 GST pull-down assay 72 3.2.7 FRET 76 3.2.8 觀察不同生長時期甘藷塊根中SP-DPE complex的表現與分佈 78 3.2.9 探討SP-DPE complex與L-SP + DPE1對於酵素催化機制之差異 83 3.2.10 探討SP-DPE complex之可能結構 90 3.2.11 SP-DPE complex之可能生理角色 91 3.3 何種原因導致L-SP形成高分子量複合體？ 93 3.3.1 L-SP高分子量活性色帶經CIAP處理後之活性變化 93 3.3.2 利用2DE觀察L-SP是否有轉譯後修飾現象 95 第四章 總結 97 參考文獻 101 問答錄 109 附錄 113 | |
| dc.language.iso | zh-TW | |
| dc.title | 甘藷塊根質體型澱粉磷解酶所形成之蛋白質複合體之鑑定與功能研究 | zh_TW |
| dc.title | Identification and Functional Study of Plastidial Starch Phosphorylase Interacting Protein Complexes in Sweet Potato Roots | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 陳翰民,楊健志,吳裕仁,張世宗 | |
| dc.subject.keyword | 澱粉磷解酶,蛋白質複合體,甘藷塊根, | zh_TW |
| dc.subject.keyword | Starch Phosphorylase,Protein Complexes,Sweet Potato Roots, | en |
| dc.relation.page | 116 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-05-23 | |
| 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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