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DC 欄位 | 值 | 語言 |
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dc.contributor.advisor | 李芳仁(Fang-Jen S. Lee) | |
dc.contributor.author | Hsin-Chia Hsu | en |
dc.contributor.author | 許俽嘉 | zh_TW |
dc.date.accessioned | 2021-06-08T04:15:02Z | - |
dc.date.copyright | 2010-09-09 | |
dc.date.issued | 2010 | |
dc.date.submitted | 2010-08-09 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/22293 | - |
dc.description.abstract | 腺嘌呤核苷二磷酸核醣化因子(ADP-ribosylation factors, ARFs)在真核細胞中的蛋白質運輸與細胞骨架的組織中扮演著很重要的角色,而腺嘌呤核苷二磷酸核糖化相似因子(ARL)就隸屬於ARF這個家族。小鳥糞嘌呤核苷三磷酸結合蛋白(small GTP-binding protein)需要鳥糞嘌呤核苷酸交換因子來協助他從鳥糞嘌呤核苷二磷酸結合的形式轉換為鳥糞嘌呤核苷三磷酸結合的形式,進一步被活化而具有活性。之前的報告指出Syt1p此蛋白質為酵母菌的第二腺嘌呤核苷二磷酸核醣化因子(Arf2p)之鳥糞嘌呤核苷酸交換因子,並且參與在囊泡的運輸過程中。而我們實驗室的研究報告也指出他不只身為Arf2p的鳥糞嘌呤核苷酸交換因子,更是第一腺嘌呤核苷二磷酸核糖化相似因子(Arl1p)的鳥糞嘌呤核苷酸交換因子。在此份報告中,我們進一步去研究Syt1p的特性。首先,Syt1p對Brefeldin A這個藥物並不具敏感性。第二,Syt1p能夠利用許多不同的片段來和Arl1p結合。他的胺基端片段,以及具有催化作用的Sec7區域,和羧基端片段都能夠跟截短胺基端17個胺基酸之Arl1p結合。更重要的是,Syt1p的這三個區域對Arl1p的結合力全都大於全長Syt1p和Arl1p的結合力,暗示著Syt1p可能和其它的鳥糞嘌呤核苷酸交換因子相同,或許都具有分子內部自我抑制的能力。而我們進一步也發現,Syt1p能夠利用其羧基端片段來和Sec7區域做分子內部的結合,而且羧基端片段也可以和另一個羧基端片段進行分子間的結合。在細胞內Syt1p確實能夠相互結合形成二聚體(dimer)或寡聚體(oligomer),而且Syt1p的胺基端片段對二聚體或寡聚體的形成也扮演著重要的角色。接著我們也利用酵母菌雙雜合(yeast two-hybrid)來大規模搜尋可能身為Syt1p調控者的蛋白質,然而這些可和Syt1p相互結合的蛋白質是否真正參與Syt1p的調控,則需進一步的確認。此外,Syt1p形成二聚體或寡聚體是否在生物上具有生物功能性,還有Syt1p在細胞中是否真的有自我抑制的能力皆需要更深入的探討。 | zh_TW |
dc.description.abstract | ARF-like (ARL) proteins belong to ADP-ribosylation factor (ARF) GTPase family, which are involved in protein trafficking and cytoskeleton organization. Those small G proteins require guanine-nucleotide exchange factors (GEFs) to switch from GDP-bound to GTP-bound form and become active. Previous reports suggested that Syt1p is the GEF of Arf2p and is involved in vesicle trafficking. Recently, our studies showed that Syt1p also acted as a GEF for Arl1p. In this study, Syt1p was further characterized. Firstly, it has been shown that Syt1p belongs to BFA-resistant GEFs. Secondly, Syt1p can use multiple regions to interact with Arl1p. The N-terminus, Sec7 domain, and C-terminus of Syt1p can all interact with Arl1d17N form, whose N-terminal first 17 amino acids are deleted. The interactions between all of the three regions and Arl1d17N are stronger than the interaction between full-length Syt1p and Arl1pd17N. Therefore, it might hint that Syt1p is autoregulated as other GEFs of Small GTPases. Surprisingly, we next found that Syt1p has an intramolecular interaction between the C-terminal region and Sec7 domain and an intermolecular interaction between C-terminal regions, indicating that Syt1p could form dimers or oligomers and might be autoregulated. Syt1p dimerization or oligomerization is also supported by in vivo pull down results, which proved that Syt1p can interact with itself. Moreover, the N-terminus is important for the formation of dimers or oligomers. Yeast two-hybrid screen was also performed to search for putative regulators of Syt1p. However, those candidates remain to be elucidated. Besides, whether dimerization or oligomerization plays an important role in Syt1p activation or membrane tethering and whether autoinhibition truly exists in Syt1p in vivo require further investigation. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T04:15:02Z (GMT). No. of bitstreams: 1 ntu-99-R97448005-1.pdf: 2223570 bytes, checksum: 849bc6cf1fe02feca69ab935dd3d882f (MD5) Previous issue date: 2010 | en |
dc.description.tableofcontents | 中文摘要 .................................................................................................................... IV
Abstract ....................................................................................................................... V Abbreviations............................................................................................................. VII Introduction .................................................................................................................. 1 Small GTP-binding proteins .................................................................................. 1 ADP-ribosylation factors (ARFs) .......................................................................... 3 Regulators of ARFs ............................................................................................... 5 Guanine nucleotide exchange factors ..................................................................... 6 GTPase-activating proteins .................................................................................... 8 ARF function in vesicle formation ....................................................................... 10 ARF-like proteins (ARLs) ................................................................................... 11 Syt1p functions in Arl3p-Arl1p signaling pathway .............................................. 12 Materials and Methods ................................................................................................ 15 Stains and Media ................................................................................................. 15 Plasmid and Strain Construction .......................................................................... 15 Construction of different forms of SYT1 for yeast two-hybrid assay ..................... 16 Construction of N-terminal and C-terminal HA-tagged SYT1............................... 18 Construction of the N-terminus and C-terminus of SYT1 for in vitro pull down assays .................................................................................................................. 18 N-terminal GST-tagging and overexpression of dN form of chromosomal SYT1 gene .................................................................................................................... 19 Polymerase chain reaction ................................................................................... 19 Yeast two-hybrid assay ........................................................................................ 20 Yeast two-hybrid screen ...................................................................................... 20 Yeast cell extracts preparation and Western blotting............................................. 21 GFP localization by fluorescence microscopy ...................................................... 23 Expression and purification of recombinant proteins ........................................... 24 In vitro GST pull-down assay .............................................................................. 25 In vivo pull-down assay ....................................................................................... 26 Results ........................................................................................................................ 28 I. Syt1p is resistant to BFA .................................................................................. 28 II. Interactions between Arl1d17N and Syt1p ...................................................... 29 Syt1p interacts with Arl1p in yeast two-hybrid analysis ............................... 29 Both of the N-terminus and Sec7 domain of Syt1p have stronger interaction with Arl1QLd17N than Arl1TNd17N in in vitro pull down assay ................. 29 III. Syt1p self-interaction ..................................................................................... 31 The intramolecular and intermolecular interactions of Syt1p determined by yeast two-hybrid .......................................................................................... 31 The interaction between the C-terminus and C-terminus of Syt1p can not be verified by yeast two-hybrid assays ............................................................. 32 The Sec7 domain and C-terminus of Syt1p can truly interact with the C-terminus of Syt1p proved by in vitro pull down assays ............................. 33 The interaction between Syt1p and Arl1dNQL might not be affected by the intramolecular interaction in Syt1p .............................................................. 33 Syt1p can interact with itself in vivo ............................................................ 34 HA-tagged and GST-tagged Syt1p will still have their function ................... 35 N-terminal deleted form of Syt1p will have stronger dimer formation than full-length Syt1p .......................................................................................... 36 Syt1p can still form dimer in arl3 deletion strain ......................................... 37 Yeast two-hybrid screen was performed for finding the putative regulator and interacting protein of Syt1p.......................................................................... 37 Searching for the putative upstream kinases of Syt1p ................................... 38 Discussion .................................................................................................................. 40 Tables ......................................................................................................................... 46 Table 1. Yeast strains used in this study ............................................................... 46 Table 2. Primers used in this study ....................................................................... 49 Table 3. Antibodies used in this study .................................................................. 52 Figures ........................................................................................................................ 53 Figure 1. The structural GDP/GTP cycle of ARF6. .............................................. 53 Figure 2. Regulation of ARF activity by GEFs that accelerate GTP binding and GAPs that activate GTP hydrolysis. ..................................................................... 54 Figure 3. Model for general mechanism of transport vesicle budding................... 55 Figure 4. Model for the Arl3p-Syt1p-Arl1p-Imh1p pathway. ............................... 56 Figure 5. Syt1p is resistant to BFA treatment. ...................................................... 57 Figure 6. Syt1p interacts with Arl1p in yeast two-hybrid assays. .......................... 58 Figure 7. The N-terminus of Syt1p has stronger interaction with Arl1QLd17N than Arl1TNd17N in in vitro pull down assays. ........................................................... 59 Figure 8. The intramolecular and intermolecular interactions of Syt1p................. 60 Figure 9. The interaction between the C-terminus and C-terminus of Syt1p can not be verified by yeast two-hybrid assays. ................................................................ 61 Figure 10. The C-terminus of Syt1p can interact with both the Sec7 domain and C-terminus in in vitro pull down assays. .............................................................. 63 Figure 11. The interaction between Syt1p and Arl1dNQL might not be affected by the intramolecular interaction in Syt1p. ............................................................... 64 Figure 12. Syt1p can interact with itself. .............................................................. 65 Figure 13. HA-Syt1p and GST-Syt1p still have the ability to restore the localization of Imh1p when SYT1 was deleted. .................................................... 66 Figure 14. The N-terminal deleted form of Syt1p will have stronger dimer formation than full-length Syt1p. ......................................................................... 67 Figure 15. Syt1p can still form dimer in arl3 deletion strain. ............................... 68 Appendixes ................................................................................................................. 69 Appendix 1. Yeast two-hybrid screen was performed to find the putative regulators and kinases of Syt1p. ........................................................................................... 70 Appendix 2. The localization of GFP-Imh1p is not affected by SHC1, CHK1, or KHA1 deletion. .................................................................................................... 71 Appendix 3. The localization of GFP-Imh1p in different kinase deletion strains. . 72 Appendix 4. arl3, arl1, imh1, syt1-null strains are not sensitive to DTT. .............. 73 Appendix 5. The interaction between the Sec7 domain of Syt1p and Arl1dNQL is stronger than Arl1dNTN. ..................................................................................... 74 References .................................................................................................................. 75 | |
dc.language.iso | en | |
dc.title | 探討第一腺嘌呤核苷二磷酸核糖化因子相似蛋白之鳥糞嘌呤核苷酸交換因子的特性 | zh_TW |
dc.title | Characterization of an Arl1p Guanine-Nucleotide Exchange Factor, Syt1p | en |
dc.type | Thesis | |
dc.date.schoolyear | 98-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 陳瑞華,鄧述諄,周祖述 | |
dc.subject.keyword | 第一腺嘌呤核苷,二磷酸核糖化因子相似蛋白,鳥糞嘌呤核苷,酸交換因子, | zh_TW |
dc.subject.keyword | Arl1p,Syt1p, | en |
dc.relation.page | 79 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2010-08-10 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 分子醫學研究所 | zh_TW |
顯示於系所單位: | 分子醫學研究所 |
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