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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18622完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳美如(Mei-Ru Chen) | |
| dc.contributor.author | Chou-Wei Chang | en |
| dc.contributor.author | 張洲維 | zh_TW |
| dc.date.accessioned | 2021-06-08T01:15:29Z | - |
| dc.date.copyright | 2014-10-09 | |
| dc.date.issued | 2014 | |
| dc.date.submitted | 2014-08-13 | |
| dc.identifier.citation | Adam, S.A., R.S. Marr, and L. Gerace. 1990. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J Cell Biol. 111:807-816.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18622 | - |
| dc.description.abstract | BGLF4是EB病毒（Epstein-Barr virus）中唯一的Ser/Thr蛋白質激酶，它會磷酸化許多病毒本身或宿主細胞的受質使得周圍環境適合病毒複製和病毒核殼體（nucleocapsid）的出核。在病毒複製的早期及晚期，BGLF4蛋白質表現主要分佈在細胞核中，但是有少部份的BGLF4會在複製晚期進入細胞質並被包裹於病毒顆粒裡。因此，本研究分成兩個主題來探討。第一是找出與BGLF4蛋白質進核（nuclear import）有關的功能性區域和機制。首先藉由系統性分析蛋白質功能性區域，發現BGLF4的N端和C端都扮演重要的調控角色。進一步透過共免疫沈澱法和蛋白質體外結合實驗（in vitro GST pull down）發現BGLF4會和核孔蛋白（nucleoporins, Nup）Nup62和Nup153有交互作用。尤其是利用HeLa細胞透化作用（permeabilize）進行進核實驗更證明了BGLF4進核過程是不須要細胞質中的調控分子協助。由於大多數的物質進入細胞核皆須透過核定位訊號（nuclear localization signal）協同細胞質調控分子與核孔蛋白交互作用，因此本研究證明BGLF4是透過一個新的進核機制達到細胞核中。在第二部份則進一步去探討BGLF4蛋白質對核孔複合體（nuclear pore complex, NPC）的結構影響及進核功能的調控。透過共軛焦顯微鏡分析，發現BGLF4蛋白質激酶會利用其激酶活性去影響Nup62和Nup153在細胞中的分佈。進一步實驗中發現，BGLF4會去抑制進核蛋白beta（importin beta）的進核，使得需要透過典型核定位訊號進核的蛋白質無法進入細胞核。值得注意的是BGLF4可以幫助不具有核定位訊號的病毒蛋白進核，包括病毒的複製蛋白BSLF1、BBLF2/3、BBLF4和主要的殼體蛋白VCA。綜合以上實驗結果，本研究發現BGLF4蛋白質激酶會透過干擾Nup62和Nup153的正常功能而幫助病毒蛋白的進核，進而促進病毒的DNA複製和殼體的組裝（assembly）。 | zh_TW |
| dc.description.abstract | BGLF4 of Epstein-Barr virus (EBV) encodes a serine/threonine protein kinase that phosphorylates multiple viral and cellular substrates to optimize the cellular environment for viral DNA replication and nuclear egress of viral nucleocapsids. BGLF4 is expressed predominantly in the nucleus at early and late stages of virus replication, while a small portion of BGLF4 is distributed in cytoplasm at late stage of virus replication and packaged into the virion. In this study, two specific aims are addressed. The first part is to identify the functional domains and the mechanism involved in the nuclear localization of BGLF4. We analyzed the functional domains crucial for nuclear localization of BGLF4 and found both N- and C-termini play important modulating roles. Both co-immunoprecipitation and in vitro pull-down assays further demonstrated that BGLF4 binds to Nup62 and Nup153. Remarkably, nuclear import assay with permeabilized HeLa cells demonstrated that BGLF4 translocated into nucleus independent of cytosolic factors. Data here suggest BGLF4 employs a novel mechanism through direct interactions with nucleoporins for its nuclear targeting. The second part is to investigate the regulatory effects of BGLF4 on the structure and biological functions of nuclear pore complex (NPC). We found that BGLF4 modified the distribution pattern of Nup62 and Nup153 in a kinase activity-dependent manner in confocal microscopy analysis. Further, the nuclear targeting of importin-beta was attenuated in the presence of BGLF4, leading to the inhibition of canonical nuclear localization signal (NLS)-mediated nuclear import. Notably, we found BGLF4 promoted the nuclear import of several non-NLS containing EBV proteins including viral DNA replicating enzymes BSLF1, BBLF2/3 and BBLF4 and the major capsid protein (VCA). Taken together, BGLF4 interferes with the normal functions of Nup62 and Nup153, and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-08T01:15:29Z (GMT). No. of bitstreams: 1 ntu-103-D96445010-1.pdf: 7179104 bytes, checksum: eac4308730491c4c4bb5b07ea48684c3 (MD5) Previous issue date: 2014 | en |
| dc.description.tableofcontents | 誌謝 i
中文摘要 I Abstract II Contents 4 Chapter 1: introduction 1 1.1 Epstein-Barr virus (EBV) 1 1.1.1 EBV associated diseases 1 1.1.2 EBV structure and genome 2 1.1.3 The life cycle of EBV 2 1.2 BGLF4 protein kinase 5 1.2.1 Characteristics of BGLF4 5 1.2.2 Substrates and functions of BGLF4 6 1.3 Nuclear envelope 7 1.3.1 Nuclear envelope associated proteins 7 1.3.2 Nucleoporins and nuclear pore complex (NPC) 8 1.3.3 Cytoplasmic and nuclear function of FG-nucleoporins 9 1.3.4 Viruses and NPC 10 1.4 Nuclear and cytoplasmic transport 10 1.5 Aims of this study 12 Chapter 2: EBV protein kinase BGLF4 targets the nucleus through interaction with nucleoporins 14 2.1 Introduction 14 2.2 Results 14 2.2.1 Mapping the regulatory domains for the nuclear localization of BGLF4. 14 2.2.2 The C-terminal amino acids 386-393 of BGLF4 are essential for its nuclear distribution but do not contain a classical NLS. 16 2.2.3 The putative helical regions at the C-terminus of BGLF4 are important for its nuclear localization. 16 2.2.4 The helix regions of a.a. 290-300 and 303-313 are important for BGLF4 nuclear targeting. 17 2.2.5 The C-terminal helical regions of BGLF4 associate with the nuclear envelope apparatus but the C-terminus alone is not sufficient for correct nuclear localization. 18 2.2.6 BGLF4 interacts directly with FG repeat-containing nucleoporins. 20 2.2.7 BGLF4 translocates into the nuclei of permeabilized cells in the absence of cytosolic factors. 21 2.3 Conclusion 22 Chapter 3: BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins 24 3.1 Introduction 24 3.2 Results 24 3.2.1 Nuclear envelope associated proteins are irregularly distributed in NA cells during EBV reactivation. 24 3.2.2 BGLF4 kinase modified the nuclear envelope structure and induced redistribution of nuclear envelope associated proteins. 25 3.2.3 BGLF4 induces the phosphorylation of nucleoporins. 27 3.2.4 Nuclear pores were enlarged in HeLa cells expressing BGLF4.28 3.2.5 BGLF4 inhibits the nuclear import of importin beta and canonical NLS-mediated nuclear transport pathways. 28 3.2.6 The permeability barrier of the nuclear envelope was partially impaired by BGLF4. 29 3.2.7 BGLF4 promotes the nuclear transport of EBV lytic proteins. 30 3.2.8 Only the conserved UL protein kinases of gamma-, and not alpha- and beta-, herpesviruses induce nuclear import of VCA. 32 3.3 Conclusion 33 Chapter 4: Discussion 36 4.1 Nuclear targeting of EBV BGLF4 kinase 36 4.1.1 Ran independent nuclear import pathway 36 4.1.2 Multiple regions within BGLF4 mediate the interactions to FG-Nups 36 4.1.3 Nuclear import of BGLF4 may through sequential direct interactions with FG-nucleoporins 37 4.1.4 BGLF4 SIMs also contribute to its nuclear import 38 4.1.5 BGLF4 may modulate NPC function 39 4.2 BGLF4 interferes with nuclear transport 40 4.2.1 BGLF4-induced modification of nuclear pore transport may facilitate viral lytic replication 40 4.2.2 The mechanism of BGLF4 to induce nuclear import of viral proteins 42 4.2.3 The outcome of BGLF4-induced nucleoplasm distributed FG-Nups 43 4.2.4 The role of SUMOylation in BGLF4 regulated nuclear transport 44 Chapter 5: Materials and Methods 45 5.1 Cell culture and transfection 45 5.2 Plasmids 45 5.3 Antibodies and immunoblotting 47 5.4 Immunofluorescence assay 48 5.5 Subcellular fractionation 49 5.6 Nuclear envelope fractionation 50 5.7 Expression and purification of GST-fusion protein 51 5.8 Co- immunoprecipitation assay 52 5.9 In vitro transcription coupled translation and GST pull-down assays 53 5.10 Cell permeabilization and in vitro nuclear import assay 53 5.11 Immunoprecipitation kinase assay 54 5.12 Transmission electron microscopy (TEM) 55 Figures and Table 56 Figure 1. Nuclear envelope (NE) and LINC complex. 57 Figure 2. A schematic summary of the conserved kinase motifs of BGLF4 and subcellular distribution of BGLF4 mutants used in this study. 58 Figure 3. BGLF4 expression patterns in EBV reactivated NA cells. 59 Figure 4. Both N- and C-terminal regions of BGLF4 contribute to its nuclear localization. 60 Figure 5. Amino acids 386-393 of BGLF4 are important for its nuclear localization, but do not compose a canonical NLS. 61 Figure 6. The C-terminal helical regions of BGLF4 contribute to its nuclear localization. 62 Figure 7. The helix regions of a.a. 290-300 and 303-313 are important for BGLF4 nuclear targeting. 63 Figure 8. The nuclear localization of BGLF4 is not regulated by its kinase activity. 64 Figure 9. The C-terminus alone is not sufficient for correct nuclear localization. 65 Figure 10. Nuclear envelope fractionation of BGLF4 C-terminus. 66 Figure 11. The C-terminus of BGLF4 associates with the nuclear envelope. 67 Figure 12. BGLF4 interacts with FG-nucleoporins. 68 Figure 13. The helix regions of a.a. 290-300 interacts with FG-nucleoporins. 69 Figure 14. BGLF4 interacts with Nup62 and Nup153. 70 Figure 15. BGLF4 translocates into the nuclei of permeabilized cells in the absence of cytosolic factors. 71 Figure 16. The predicted 3D structure of BGLF4. 72 Figure 17. EBV reactivation induces redistribution of nuclear envelope associated proteins. 73 Figure 18. BGLF4 did not change the nuclear envelope associated proteins expression. 74 Figure 19. BGLF4 induces redistribution of nuclear envelope associated proteins. 75 Figure 20. Redistribution of FG-Nups in EBV reactivated NA cells. 76 Figure 21. Redistribution of FG-Nups in EBV reactivated NA cells. 77 Figure 22. Redistribution of FG-Nups in EBV reactivated Akata+ cells. 78 Figure 23. BGLF4 but not K102I induces FG-Nup redistribution. 79 Figure 24. FG-Nups were phosphorylated by BGLF4 in vivo and in vitro. 80 Figure 25. TEM analysis of BGLF4 induced redistribution of NPC. 81 Figure 26. Nuclear transport of importin beta was inhibited in BGLF4 expressing cells. 82 Figure 27. Nuclear transport of classical NLS containing protein was blocked in BGLF4 expressing cells. 83 Figure 28. BGLF4 induces RanGAP1 redistribution. 84 Figure 29. The gating of NPC was impaired in BGLF4 expressing cells. 85 Figure 30. BGLF4 does not induce the leak of intranuclear proteins into cytoplasm. 86 Figure 31. BGLF4 promotes nuclear import of EBV replication components. 87 Figure 32. BGLF4 induces nuclear import of HA-VCA. 88 Figure 33. HA-VCA co-stains with alpha-actin and beta-tubulin. 89 Figure 34. Microtubule reorganization is involved in nuclear import of HA-VCA. 90 Figure 35. Microtubule reorganization is not required for nuclear import of EBV replication components. 91 Figure 36. Gamma-herpesviral UL kinases promotes nuclear import of VCA. 92 Figure 37.ORF36 cannot promote nuclear import of EBV replication proteins. 93 Figure 38. A hypothetical model of the EBV BGLF4 induced structural and functional changes of nuclear pore complex. 94 Table. 1 Oligonucleotide primers and plasmid DNA templates used to geneate BGLF4 mutants 95 References 96 | |
| dc.language.iso | en | |
| dc.title | EB病毒BGLF4蛋白質激酶進核機制及對物質進核調控之探討 | zh_TW |
| dc.title | The nuclear targeting of EBV BGLF4 kinase and its regulatory effects on nuclear import | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 102-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 張麗冠(Li-Kwan Chang),張明富(Ming-Fu Chang),譚婉玉(Woan-Yuh Tarn),李重霈(Chung-Pei Lee) | |
| dc.subject.keyword | EB病毒,BGLF4,核孔複合體,核孔蛋白,進核, | zh_TW |
| dc.subject.keyword | EBV,BGLF4,nuclear pore complex,nucleoporins,nuclear import, | en |
| dc.relation.page | 109 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2014-08-13 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| 顯示於系所單位： | 微生物學科所 | |
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