請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/72275
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張麗冠(Li-Kwan Chang) | |
dc.contributor.author | Tsun-Chieh Liang | en |
dc.contributor.author | 梁尊傑 | zh_TW |
dc.date.accessioned | 2021-06-17T06:32:43Z | - |
dc.date.available | 2018-08-18 | |
dc.date.copyright | 2018-08-18 | |
dc.date.issued | 2018 | |
dc.date.submitted | 2018-08-16 | |
dc.identifier.citation | Adamson, A.L., Darr, D., Holley-Guthrie, E., Johnson, R.A., Mauser, A., Swenson, J., Kenney, S., 2000. Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases. J Virol 74, 1224-1233.
Allday, M.J., Crawford, D.H., Griffin, B.E., 1989. Epstein-Barr virus latent gene expression during the initiation of B cell immortalization. J Gen Virol 70 ( Pt 7), 1755-1764. Amon, W., Binne, U.K., Bryant, H., Jenkins, P.J., Karstegl, C.E., Farrell, P.J., 2004. Lytic cycle gene regulation of Epstein-Barr virus. J Virol 78, 13460-13469. Bürkle, A., 2001. Posttranslational Modification. Encyclopedia of Genetics. Bachmair, A., Varshavsky, A., 1989. The degradation signal in a short-lived protein. Cell 56, 1019-1032. Bancroft, J.B., Hiebert, E., 1967. Formation of an infectious nucleoprotein from protein and nucleic acid isolated from a small spherical virus. Virology 32, 354-356. Baumann, M., Feederle, R., Kremmer, E., Hammerschmidt, W., 1999. Cellular transcription factors recruit viral replication proteins to activate the Epstein-Barr virus origin of lytic DNA replication, oriLyt. EMBO J 18, 6095-6105. Bertani, G., 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol 62, 293-300. Bonifacino, J.S., Traub, L.M., 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72, 395-447. Burkitt, D., 1958. A sarcoma involving the jaws in African children. Br J Surg 46, 218-223. Burkitt, D., 1962. A children's cancer dependent on climatic factors. Nature 194, 232-234. Campbell, E.M., Dodding, M.P., Yap, M.W., Wu, X., Gallois-Montbrun, S., Malim, M.H., Stoye, J.P., Hope, T.J., 2007. TRIM5 alpha cytoplasmic bodies are highly dynamic structures. Mol Biol Cell 18, 2102-2111. Chang, L.K., Chuang, J.Y., Nakao, M., Liu, S.T., 2010. MCAF1 and synergistic activation of the transcription of Epstein-Barr virus lytic genes by Rta and Zta. Nucleic Acids Res 38, 4687-4700. Chang, L.K., Chung, J.Y., Hong, Y.R., Ichimura, T., Nakao, M., Liu, S.T., 2005. Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via an interaction with MCAF1. Nucleic Acids Res 33, 6528-6539. Chang, L.K., Lee, Y.H., Cheng, T.S., Hong, Y.R., Lu, P.J., Wang, J.J., Wang, W.H., Kuo, C.W., Li, S.S., Liu, S.T., 2004. Post-translational modification of Rta of Epstein-Barr virus by SUMO-1. J Biol Chem 279, 38803-38812. Chang, L.K., Liu, S.T., Kuo, C.W., Wang, W.H., Chuang, J.Y., Bianchi, E., Hong, Y.R., 2008. Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM. J Mol Biol 379, 231-242. Chaugule, V.K., Walden, H., 2016. Specificity and disease in the ubiquitin system. Biochem Soc Trans 44, 212-227. Chen, L.W., Chang, P.J., Delecluse, H.J., Miller, G., 2005. Marked variation in response of consensus binding elements for the Rta protein of Epstein-Barr virus. J Virol 79, 9635-9650. Chevallier-Greco, A., Manet, E., Chavrier, P., Mosnier, C., Daillie, J., Sergeant, A., 1986. Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter. EMBO J 5, 3243-3249. Chou, C.K., Chang, Y.T., Korinek, M., Chen, Y.T., Yang, Y.T., Leu, S., Lin, I.L., Tang, C.J., Chiu, C.C., 2017. The regulations of deubiquitinase USP15 and its pathophysiological mechanisms in diseases. Int J Mol Sci 18. Ciechanover, A., 2005. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 6, 79-87. Ciechanover, A., Finley, D., Varshavsky, A., 1984. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37, 57-66. Cox, M.A., Leahy, J., Hardwick, J.M., 1990. An enhancer within the divergent promoter of Epstein-Barr virus responds synergistically to the R and Z transactivators. J Virol 64, 313-321. Cozzone, A.J., 1998. Post-translational modification of proteins by reversible phosphorylation in prokaryotes. Biochimie 80, 43-48. Dambaugh, T., Beisel, C., Hummel, M., King, W., Fennewald, S., Cheung, A., Heller, M., Raab-Traub, N., Kieff, E., 1980. Epstein-Barr virus (B95-8) DNA VII: molecular cloning and detailed mapping. Proc Natl Acad Sci U S A 77, 2999-3003. Dawson, C.W., Tramountanis, G., Eliopoulos, A.G., Young, L.S., 2003. Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling. J Biol Chem 278, 3694-3704. Deribe, Y.L., Pawson, T., Dikic, I., 2010. Post-translational modifications in signal integration. Nat Struct Mol Biol 17, 666-672. Dolyniuk, M., Pritchett, R., Kieff, E., 1976a. Proteins of Epstein-Barr virus. I. Analysis of the polypeptides of purified enveloped Epstein-Barr virus. J Virol 17, 935-949. Dolyniuk, M., Wolff, E., Kieff, E., 1976b. Proteins of Epstein-Barr Virus. II. Electrophoretic analysis of the polypeptides of the nucleocapsid and the glucosamine- and polysaccharide-containing components of enveloped virus. J Virol 18, 289-297. Dyson, O.F., Pagano, J.S., Whitehurst, C.B., 2017. The Translesion Polymerase Pol eta Is Required for Efficient Epstein-Barr Virus Infectivity and Is Regulated by the Viral Deubiquitinating Enzyme BPLF1. J Virol 91. El-Guindy, A., Ghiassi-Nejad, M., Golden, S., Delecluse, H.J., Miller, G., 2013. Essential role of Rta in lytic DNA replication of Epstein-Barr virus. J Virol 87, 208-223. Epstein, M.A., Achong, B.G., Barr, Y.M., 1964. Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma. Lancet 1, 702-703. Epstein, M.A., Barr, Y.M., 1964. Cultivation in vitro of human lymphoblasts from Burkitt's malignant lymphoma. Lancet 1, 252-253. Ferreira, J.V., Soares, A.R., Ramalho, J.S., Pereira, P., Girao, H., 2015. K63 linked ubiquitin chain formation is a signal for HIF1A degradation by Chaperone-Mediated Autophagy. Sci Rep 5, 10210. Fixman, E.D., Hayward, G.S., Hayward, S.D., 1992. trans-acting requirements for replication of Epstein-Barr virus ori-Lyt. J Virol 66, 5030-5039. Fixman, E.D., Hayward, G.S., Hayward, S.D., 1995. Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays. J Virol 69, 2998-3006. Flemington, E., Speck, S.H., 1990. Autoregulation of Epstein-Barr virus putative lytic switch gene BZLF1. J Virol 64, 1227-1232. Fujii, K., Yokoyama, N., Kiyono, T., Kuzushima, K., Homma, M., Nishiyama, Y., Fujita, M., Tsurumi, T., 2000. The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1-BBLF2/3 complex. J Virol 74, 2550-2557. Full, F., Hahn, A.S., Grosskopf, A.K., Ensser, A., 2017. Gammaherpesviral Tegument Proteins, PML-Nuclear Bodies and the Ubiquitin-Proteasome System. Viruses 9. Gao, Z., Krithivas, A., Finan, J.E., Semmes, O.J., Zhou, S., Wang, Y., Hayward, S.D., 1998. The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins. J Virol 72, 8559-8567. Geng, F., Wenzel, S., Tansey, W.P., 2012. Ubiquitin and proteasomes in transcription. Annu Rev Biochem 81, 177-201. Geser, A., de The, G., Lenoir, G., Day, N.E., Williams, E.H., 1982. Final case reporting from the Ugandan prospective study of the relationship between EBV and Burkitt's lymphoma. Int J Cancer 29, 397-400. Goldstein, G., Scheid, M., Hammerling, U., Schlesinger, D.H., Niall, H.D., Boyse, E.A., 1975. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc Natl Acad Sci U S A 72, 11-15. Gonzalez, C.M., Wang, L., Damania, B., 2009. Kaposi's sarcoma-associated herpesvirus encodes a viral deubiquitinase. J Virol 83, 10224-10233. Gould, S.J., Subramani, S., 1988. Firefly luciferase as a tool in molecular and cell biology. Anal Biochem 175, 5-13. Graham, F.L., Smiley, J., Russell, W.C., Nairn, R., 1977. Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J Gen Virol 36, 59-74. Gruffat, H., Duran, N., Buisson, M., Wild, F., Buckland, R., Sergeant, A., 1992. Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter. J Virol 66, 46-52. Gruffat, H., Sergeant, A., 1994. Characterization of the DNA-binding site repertoire for the Epstein-Barr virus transcription factor R. Nucleic Acids Res 22, 1172-1178. Grutter, C., Briand, C., Capitani, G., Mittl, P.R., Papin, S., Tschopp, J., Grutter, M.G., 2006. Structure of the PRYSPRY-domain: implications for autoinflammatory diseases. FEBS Lett 580, 99-106. Haas, A.L., Bright, P.M., 1987. The dynamics of ubiquitin pools within cultured human lung fibroblasts. J Biol Chem 262, 345-351. Hammerschmidt, W., Sugden, B., 1988. Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55, 427-433. Hampar, B., Tanaka, A., Nonoyama, M., Derge, J.G., 1974. Replication of the resident repressed Epstein-Barr virus genome during the early S phase (S-1 period) of nonproducer Raji cells. Proc Natl Acad Sci U S A 71, 631-633. Hardwick, J.M., Lieberman, P.M., Hayward, S.D., 1988. A new Epstein-Barr virus transactivator, R, induces expression of a cytoplasmic early antigen. J Virol 62, 2274-2284. Harlow, E., and David Lane. , 1999. Immunoprecipitation. Cold Spring Harbor Laboratory Press. 7. Harper, S., Gratton, H.E., Cornaciu, I., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I., 2014. Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains. Biochemistry 53, 2966-2978. Harris, R.J., 1964. Aetiology of Central African Lymphomata. Br Med Bull 20, 149-153. He, M., Zhou, Z., Shah, A.A., Zou, H., Tao, J., Chen, Q., Wan, Y., 2016. The emerging role of deubiquitinating enzymes in genomic integrity, diseases, and therapeutics. Cell Biosci 6, 62. Henderson, E.E., Long, W.K., 1981. Host cell reactivation of uv- and X-ray-damaged herpes simplex virus by Epstein-Barr virus (EBV)-transformed lymphoblastoid cell lines. Virology 115, 237-248. Hendriks, I.A., Schimmel, J., Eifler, K., Olsen, J.V., Vertegaal, A.C., 2015. Ubiquitin-specific protease 11 (USP11) deubiquitinates hybrid small ubiquitin-like modifier (SUMO)-ubiquitin chains to counteract RING finger protein 4 (RNF4). J Biol Chem 290, 15526-15537. Henle, G., Henle, W., 1966. Studies on cell lines derived from Burkitt's lymphoma. Trans N Y Acad Sci 29, 71-79. Henle, G., Henle, W., Diehl, V., 1968. Relation of Burkitt's tumor-associated herpes-type virus to infectious mononucleosis. Proc Natl Acad Sci U S A 59, 94-101. Henson, B.W., Perkins, E.M., Cothran, J.E., Desai, P., 2009. Self-assembly of Epstein-Barr virus capsids. J Virol 83, 3877-3890. Hershko, A., Ciechanover, A., 1992. The ubiquitin system for protein degradation. Annu Rev Biochem 61, 761-807. Hershko, A., Ciechanover, A., 1998. The ubiquitin system. Annu Rev Biochem 67, 425-479. Hershko, A., Ciechanover, A., Heller, H., Haas, A.L., Rose, I.A., 1980. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci U S A 77, 1783-1786. Hicke, L., Dunn, R., 2003. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19, 141-172. Hochstrasser, M., Varshavsky, A., 1990. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell 61, 697-708. Holley-Guthrie, E.A., Quinlivan, E.B., Mar, E.C., Kenney, S., 1990. The Epstein-Barr virus (EBV) BMRF1 promoter for early antigen (EA-D) is regulated by the EBV transactivators, BRLF1 and BZLF1, in a cell-specific manner. J Virol 64, 3753-3759. Holowaty, M.N., Zeghouf, M., Wu, H., Tellam, J., Athanasopoulos, V., Greenblatt, J., Frappier, L., 2003. Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7. J Biol Chem 278, 29987-29994. Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H.D., Jentsch, S., 2000. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586. Huang, H.H., Chen, C.S., Wang, W.H., Hsu, S.W., Tsai, H.H., Liu, S.T., Chang, L.K., 2016. TRIM5alpha promotes ubiquitination of Rta from Epstein-Barr virus to attenuate lytic progression. Front Microbiol 7, 2129. Hung, C.H., Chen, L.W., Wang, W.H., Chang, P.J., Chiu, Y.F., Hung, C.C., Lin, Y.J., Liou, J.Y., Tsai, W.J., Hung, C.L., Liu, S.T., 2014. Regulation of autophagic activation by Rta of Epstein-Barr virus via the extracellular signal-regulated kinase pathway. J Virol 88, 12133-12145. Hung, C.H., Liu, S.T., 1999. Characterization of the Epstein-Barr virus BALF2 promoter. J Gen Virol 80 ( Pt 10), 2747-2750. Iconomou, M., Saunders, D.N., 2016. Systematic approaches to identify E3 ligase substrates. Biochem J 473, 4083-4101. Ikeda, M., Ikeda, A., Longnecker, R., 2002. Lysine-independent ubiquitination of Epstein-Barr virus LMP2A. Virology 300, 153-159. Jentsch, S., McGrath, J.P., Varshavsky, A., 1987. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-134. Johannsen, E., Luftig, M., Chase, M.R., Weicksel, S., Cahir-McFarland, E., Illanes, D., Sarracino, D., Kieff, E., 2004. Proteins of purified Epstein-Barr virus. Proc Natl Acad Sci U S A 101, 16286-16291. Johnson, E.S., Gonda, D.K., Varshavsky, A., 1990. cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature 346, 287-291. Jura, J., Skalniak, L., Koj, A., 2012. Monocyte chemotactic protein-1-induced protein-1 (MCPIP1) is a novel multifunctional modulator of inflammatory reactions. Biochim Biophys Acta 1823, 1905-1913. Kane, L.A., Lazarou, M., Fogel, A.I., Li, Y., Yamano, K., Sarraf, S.A., Banerjee, S., Youle, R.J., 2014. PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol 205, 143-153. Kaye, K.M., Izumi, K.M., Kieff, E., 1993. Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation. Proc Natl Acad Sci U S A 90, 9150-9154. Kenney, S., Kamine, J., Holley-Guthrie, E., Lin, J.C., Mar, E.C., Pagano, J., 1989. The Epstein-Barr virus (EBV) BZLF1 immediate-early gene product differentially affects latent versus productive EBV promoters. J Virol 63, 1729-1736. Kenney, S.C., 2007. Reactivation and lytic replication of EBV, in: Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., Yamanishi, K. (Eds.), Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis, Cambridge. Kieff, E.R., A.B.. 2001. Epstein-Barr virus and its replication. Fields Virology. 2., 2603-2654. . Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., Iwai, K., 2006. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J 25, 4877-4887. Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H.D., Mayer, T.U., Jentsch, S., 1999. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644. Kuppers, R., 2003. B cells under influence: transformation of B cells by Epstein-Barr virus. Nat Rev Immunol 3, 801-812. Lamoliatte, F., Caron, D., Durette, C., Mahrouche, L., Maroui, M.A., Caron-Lizotte, O., Bonneil, E., Chelbi-Alix, M.K., Thibault, P., 2014. Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling. Nat Commun 5, 5409. Lauwers, E., Jacob, C., Andre, B., 2009. K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J Cell Biol 185, 493-502. Lee, J.Y., Nagano, Y., Taylor, J.P., Lim, K.L., Yao, T.P., 2010. Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J Cell Biol 189, 671-679. Lee, Y.H., Chiu, Y.F., Wang, W.H., Chang, L.K., Liu, S.T., 2008. Activation of the ERK signal transduction pathway by Epstein-Barr virus immediate-early protein Rta. J Gen Virol 89, 2437-2446. Levy, J.A., Henle, G., 1966. Indirect immunofluorescence tests with sera from African children and cultured Burkitt lymphoma cells. J Bacteriol 92, 275-276. Leznicki, P., Kulathu, Y., 2017. Mechanisms of regulation and diversification of deubiquitylating enzyme function. J Cell Sci 130, 1997-2006. Li, M., Brooks, C.L., Wu-Baer, F., Chen, D., Baer, R., Gu, W., 2003. Mono- versus polyubiquitination: differential control of p53 fate by Mdm2. Science 302, 1972-1975. Li, W., Ye, Y., 2008. Polyubiquitin chains: functions, structures, and mechanisms. Cell Mol Life Sci 65, 2397-2406. Li, X., Yeung, D.F., Fiegen, A.M., Sodroski, J., 2011. Determinants of the higher order association of the restriction factor TRIM5alpha and other tripartite motif (TRIM) proteins. J Biol Chem 286, 27959-27970. Lieberman, P.M., Hardwick, J.M., Sample, J., Hayward, G.S., Hayward, S.D., 1990. The zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions. J Virol 64, 1143-1155. Lin, T.Y., Chu, Y.Y., Yang, Y.C., Hsu, S.W., Liu, S.T., Chang, L.K., 2014. MCAF1 and Rta-activated BZLF1 transcription in Epstein-Barr virus. PLoS One 9, e90698. Liu, C., Sista, N.D., Pagano, J.S., 1996. Activation of the Epstein-Barr virus DNA polymerase promoter by the BRLF1 immediate-early protein is mediated through USF and E2F. J Virol 70, 2545-2555. Liu, P., Speck, S.H., 2003. Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta. Virology 310, 199-206. Manet, E., Gruffat, H., Trescol-Biemont, M.C., Moreno, N., Chambard, P., Giot, J.F., Sergeant, A., 1989. Epstein-Barr virus bicistronic mRNAs generated by facultative splicing code for two transcriptional trans-activators. EMBO J 8, 1819-1826. Manet, E., Rigolet, A., Gruffat, H., Giot, J.F., Sergeant, A., 1991. Domains of the Epstein-Barr virus (EBV) transcription factor R required for dimerization, DNA binding and activation. Nucleic Acids Res 19, 2661-2667. McKenzie, J., Lopez-Giraldez, F., Delecluse, H.J., Walsh, A., El-Guindy, A., 2016. The Epstein-Barr virus immunoevasins BCRF1 and BPLF1 are expressed by a mechanism independent of the canonical late pre-initiation complex. PLoS Pathog 12, e1006008. Metzger, M.B., Pruneda, J.N., Klevit, R.E., Weissman, A.M., 2014. RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim Biophys Acta 1843, 47-60. Michel, M.A., Swatek, K.N., Hospenthal, M.K., Komander, D., 2017. Ubiquitin linkage-specific affimers reveal insights into K6-linked ubiquitin signaling. Mol Cell 68, 233-246 e235. Nemerow, G.R., Mold, C., Schwend, V.K., Tollefson, V., Cooper, N.R., 1987. Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: sequence homology of gp350 and C3 complement fragment C3d. J Virol 61, 1416-1420. Nijman, S.M., Luna-Vargas, M.P., Velds, A., Brummelkamp, T.R., Dirac, A.M., Sixma, T.K., Bernards, R., 2005. A genomic and functional inventory of deubiquitinating enzymes. Cell 123, 773-786. Ohtake, F., Saeki, Y., Ishido, S., Kanno, J., Tanaka, K., 2016. The K48-K63 branched ubiquitin chain regulates NF-kappaB signaling. Mol Cell 64, 251-266. Ohtake, F., Saeki, Y., Sakamoto, K., Ohtake, K., Nishikawa, H., Tsuchiya, H., Ohta, T., Tanaka, K., Kanno, J., 2015. Ubiquitin acetylation inhibits polyubiquitin chain elongation. EMBO Rep 16, 192-201. Palombella, V.J., Rando, O.J., Goldberg, A.L., Maniatis, T., 1994. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78, 773-785. Peng, J., Schwartz, D., Elias, J.E., Thoreen, C.C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S.P., 2003. A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21, 921-926. Perron, M.J., Stremlau, M., Song, B., Ulm, W., Mulligan, R.C., Sodroski, J., 2004. TRIM5alpha mediates the postentry block to N-tropic murine leukemia viruses in human cells. Proc Natl Acad Sci U S A 101, 11827-11832. Pfuller, R., Hammerschmidt, W., 1996. Plasmid-like replicative intermediates of the Epstein-Barr virus lytic origin of DNA replication. J Virol 70, 3423-3431. Pickart, C.M., Fushman, D., 2004. Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 8, 610-616. Quinlivan, E.B., Holley-Guthrie, E.A., Norris, M., Gutsch, D., Bachenheimer, S.L., Kenney, S.C., 1993. Direct BRLF1 binding is required for cooperative BZLF1/BRLF1 activation of the Epstein-Barr virus early promoter, BMRF1. Nucleic Acids Res 21, 1999-2007. Ragoczy, T., Heston, L., Miller, G., 1998. The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes. J Virol 72, 7978-7984. Ragoczy, T., Miller, G., 1999. Role of the epstein-barr virus RTA protein in activation of distinct classes of viral lytic cycle genes. J Virol 73, 9858-9866. Ragoczy, T., Miller, G., 2001. Autostimulation of the Epstein-Barr virus BRLF1 promoter is mediated through consensus Sp1 and Sp3 binding sites. J Virol 75, 5240-5251. Rennekamp, A.J., Lieberman, P.M., 2011. Initiation of Epstein-Barr virus lytic replication requires transcription and the formation of a stable RNA-DNA hybrid molecule at OriLyt. J Virol 85, 2837-2850. Rhodes, D.A., de Bono, B., Trowsdale, J., 2005. Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence? Immunology 116, 411-417. Robinson, A.R., Kwek, S.S., Hagemeier, S.R., Wille, C.K., Kenney, S.C., 2011. Cellular transcription factor Oct-1 interacts with the Epstein-Barr virus BRLF1 protein to promote disruption of viral latency. J Virol 85, 8940-8953. Ronau, J.A., Beckmann, J.F., Hochstrasser, M., 2016. Substrate specificity of the ubiquitin and Ubl proteases. Cell Res 26, 441-456. Saito, S., Murata, T., Kanda, T., Isomura, H., Narita, Y., Sugimoto, A., Kawashima, D., Tsurumi, T., 2013. Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication. J Virol 87, 4060-4070. Sanchez, J.G., Okreglicka, K., Chandrasekaran, V., Welker, J.M., Sundquist, W.I., Pornillos, O., 2014. The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer. Proc Natl Acad Sci U S A 111, 2494-2499. Sastri, J., O'Connor, C., Danielson, C.M., McRaven, M., Perez, P., Diaz-Griffero, F., Campbell, E.M., 2010. Identification of residues within the L2 region of rhesus TRIM5alpha that are required for retroviral restriction and cytoplasmic body localization. Virology 405, 259-266. Scheffner, M., Kumar, S., 2014. Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects. Biochim Biophys Acta 1843, 61-74. Schepers, A., Pich, D., Hammerschmidt, W., 1996. Activation of oriLyt, the lytic origin of DNA replication of Epstein-Barr virus, by BZLF1. Virology 220, 367-376. Schlieker, C., Korbel, G.A., Kattenhorn, L.M., Ploegh, H.L., 2005. A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae. J Virol 79, 15582-15585. Shibata, D., Weiss, L.M., 1992. Epstein-Barr virus-associated gastric adenocarcinoma. Am J Pathol 140, 769-774. Smith, D.B., Johnson, K.S., 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40. Sompallae, R., Gastaldello, S., Hildebrand, S., Zinin, N., Hassink, G., Lindsten, K., Haas, J., Persson, B., Masucci, M.G., 2008. Epstein-barr virus encodes three bona fide ubiquitin-specific proteases. J Virol 82, 10477-10486. Spence, J., Sadis, S., Haas, A.L., Finley, D., 1995. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 15, 1265-1273. Spratt, D.E., Walden, H., Shaw, G.S., 2014. RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem J 458, 421-437. Stremlau, M., Owens, C.M., Perron, M.J., Kiessling, M., Autissier, P., Sodroski, J., 2004. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427, 848-853. Studier, F.W., Moffatt, B.A., 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189, 113-130. Sun, L., Chen, Z.J., 2004. The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 16, 119-126. Sun, Z.W., Allis, C.D., 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108. Takeuchi, O., Akira, S., 2009. Innate immunity to virus infection. Immunol Rev 227, 75-86. Tansey, W.P., 2007. Denaturing protein immunoprecipitation from Mammalian cells. CSH Protoc 2007, pdb prot4619. Tareen, S.U., Emerman, M., 2011. Human Trim5alpha has additional activities that are uncoupled from retroviral capsid recognition. Virology 409, 113-120. Thorley-Lawson, D.A., 2001. Epstein-Barr virus: exploiting the immune system. Nat Rev Immunol 1, 75-82. Tsurumi, T., 2001. EBV replication enzymes. Curr Top Microbiol Immunol 258, 65-87. van Gent, M., Braem, S.G., de Jong, A., Delagic, N., Peeters, J.G., Boer, I.G., Moynagh, P.N., Kremmer, E., Wiertz, E.J., Ovaa, H., Griffin, B.D., Ressing, M.E., 2014. Epstein-Barr virus large tegument protein BPLF1 contributes to innate immune evasion through interference with toll-like receptor signaling. PLoS Pathog 10, e1003960. Ventii, K.H., Wilkinson, K.D., 2008. Protein partners of deubiquitinating enzymes. Biochem J 414, 161-175. Vijay-Kumar, S., Bugg, C.E., Cook, W.J., 1987. Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194, 531-544. Wang, W.H., Chang, L.K., Liu, S.T., 2011. Molecular interactions of Epstein-Barr virus capsid proteins. J Virol 85, 1615-1624. Wang, W.H., Kuo, C.W., Chang, L.K., Hung, C.C., Chang, T.H., Liu, S.T., 2015. Assembly of Epstein-Barr virus capsid in promyelocytic leukemia nuclear bodies. J Virol 89, 8922-8931. Warner, H.B., Carp, R.I., 1981. Multiple sclerosis and Epstein-Barr virus. Lancet 2, 1290. Weiss, L.M., Movahed, L.A., Warnke, R.A., Sklar, J., 1989. Detection of Epstein-Barr viral genomes in Reed-Sternberg cells of Hodgkin's disease. N Engl J Med 320, 502-506. Weissman, A.M., 2001. Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2, 169-178. Whitehurst, C.B., Ning, S., Bentz, G.L., Dufour, F., Gershburg, E., Shackelford, J., Langelier, Y., Pagano, J.S., 2009. The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity. J Virol 83, 4345-4353. Whitehurst, C.B., Vaziri, C., Shackelford, J., Pagano, J.S., 2012. Epstein-Barr virus BPLF1 deubiquitinates PCNA and attenuates polymerase eta recruitment to DNA damage sites. J Virol 86, 8097-8106. Wild, J., Hradecna, Z., Szybalski, W., 2002. Conditionally amplifiable BACs: switching from single-copy to high-copy vectors and genomic clones. Genome Res 12, 1434-1444. Winberg, G., Matskova, L., Chen, F., Plant, P., Rotin, D., Gish, G., Ingham, R., Ernberg, I., Pawson, T., 2000. Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. Mol Cell Biol 20, 8526-8535. Wolf, H., zur Hausen, H., Becker, V., 1973. EB viral genomes in epithelial nasopharyngeal carcinoma cells. Nat New Biol 244, 245-247. Wu, X., Anderson, J.L., Campbell, E.M., Joseph, A.M., Hope, T.J., 2006. Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infection. Proc Natl Acad Sci U S A 103, 7465-7470. Yamano, K., Matsuda, N., Tanaka, K., 2016. The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation. EMBO reports 17, 300-316. Yamauchi, K., Wada, K., Tanji, K., Tanaka, M., Kamitani, T., 2008. Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential role. FEBS J 275, 1540-1555. Yang, Y.C., Feng, T.H., Chen, T.Y., Huang, H.H., Hung, C.C., Liu, S.T., Chang, L.K., 2015. RanBPM regulates Zta-mediated transcriptional activity in Epstein-Barr virus. J Gen Virol 96, 2336-2348. Yang, Y.C., Yoshikai, Y., Hsu, S.W., Saitoh, H., Chang, L.K., 2013. Role of RNF4 in the ubiquitination of Rta of Epstein-Barr virus. J Biol Chem 288, 12866-12879. Young, L.S., Murray, P.G., 2003. Epstein-Barr virus and oncogenesis: from latent genes to tumours. Oncogene 22, 5108-5121. Zhang, Q., Hong, Y., Dorsky, D., Holley-Guthrie, E., Zalani, S., Elshiekh, N.A., Kiehl, A., Le, T., Kenney, S., 1996. Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: Effects on EBV transcription and lytic replication. J Virol 70, 5131-5142. Zimber-Strobl, U., Strobl, L.J., 2001. EBNA2 and Notch signalling in Epstein-Barr virus mediated immortalization of B lymphocytes. Semin Cancer Biol 11, 423-434. 李宇群, 2012. Involvement of MCAF1 in Epstein-Barr virus lytic replication. 臺灣大學生命科學院生化科技學系碩士論文. 林庭羽, 2013. Functional analysis of BSLF1 of Epstein-Barr virus. 臺灣大學生命科學院生化科技學系碩士論文. 徐詩媁, 2013. Role of TRIM5α in the lytic progression of Epstein-Barr virus. 臺灣大學生命科學院生化科技學系碩士論文. 黃筱茜, 2014. Effects of BSLF1 on capsid proteins of Epstein-Barr virus. 臺灣大學生命科學院生化科技學系碩士論文. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/72275 | - |
dc.description.abstract | Epstein-Barr virus (EB病毒) 又稱人類皰疹病毒第四型,隸屬於人類皰疹病毒科,是一種感染人類鼻咽上皮細胞及B淋巴細胞的致癌病毒。宿主細胞為了抵抗病毒,會透過胞內蛋白質對入侵病毒蛋白質進行修飾與降解,進而抑制病毒感染。在先前的研究發現,宿主細胞中的E3泛素連接酶TRIM5α與EB病毒顆粒的產生有關,並會將EB病毒溶裂期的極早期蛋白質Rta及外鞘蛋白質BORF1泛素化,此修飾會進而影響到EB病毒的基因表現與病毒組裝,使病毒生產效率下降。然而先前研究發現,作為引子合成酶的EB病毒溶裂期早期蛋白質BSLF1具有去泛素化酶的活性,並能將Rta與BORF1蛋白質去泛素化,顯示BSLF1除了參與EB病毒基因複製外甚至能抵禦宿主細胞對病毒蛋白質進行的修飾。因此,本研究對BSLF1是否與TRIM5α彼此之間具有拮抗關係進行驗證。首先利用免疫螢光染色法及GST pull-down分析證明BSLF1與TRIM5α之間的結合。接著以變性免疫沉澱法證實了BSLF1會去除TRIM5α在Rta及BORF1上增加的泛素化修飾。但在冷光報導基因分析實驗中則發現BSLF1並不能使Rta被TRIM5α抑制的轉錄活性恢復,顯示BSLF1與TRIM5α並非在抑制Rta的轉錄活性上具有拮抗關係。而在分析BORF1蛋白質穩定性後,發現BSLF1會延長其半衰期,但卻無法使BORF1蛋白質的表現顯著增加,顯示BORF1與Rta上的泛素化修飾可能具有除了穩定性與抑制轉錄活性外的影響,因此本研究進一步檢驗BSLF1與TRIM5α彼此拮抗的泛素化修飾形式,結果發現BSLF1主要去除BORF1上K63鏈結多泛素鏈。綜上所述,本研究發現BSLF1會拮抗TRIM5α對於Rta及BORF1的泛素化修飾,並能夠使Rta和BORF1出現修飾型態上的改變,雖然不同修飾型態對EB病毒生活史的影響有待進一步研究,但病毒與宿主轉譯後修飾之間的拮抗確實存在,並可能作為病毒抵禦宿主細胞抑制作用的重要機制。 | zh_TW |
dc.description.abstract | EBV, also known as Human Herpesvirus 4 (HHV-4), is a member of Herpesviridae. EBV infects epithelial cells and B cells, since its association with several cancers, it is known as an oncovirus. To protect themselves from infection by viruses, host cells usually degrade viral proteins to inhibit viral replication. Earlier research showed that TRIM5α, an E3 ubiquitin ligase, is important to EBV virion assembly. Also, it has been found that immediate-early protein Rta and late protein BORF1, both important in replication of EBV, are ubiquitinated by TRIM5α. Ubiquitination of Rta and BORF1 affect EBV DNA replication and viral capsid assembly, which decrease efficiency of virus production. In a previous study, BSLF1 protein of EBV was found to have deubiquitinase activity although it was widely known as a primase. BSLF1 is able to deubiquitinate Rta and BORF1, suggesting that BSLF1 plays a role in defending host modification. The aim of this study is to elucidate the antagonism between BSLF1 and E3 ubiquitin ligase TRIM5α. First, GST pull-down assay and immunofluorescence analysis revealed that BSLF1 interacts directly with TRIM5α. To examine the deubiquitination of Rta and BORF1 by BSLF1, I used denature immunoprecipitation and demonstrated that BSLF1 deubiquitinates Rta and BORF1 that are ubiquitinated by TRIM5α. Moreover, this study found that overexpressing BSLF1 decreased the transcriptional activity of Rta in a transient transfection assay. By using a HEK293T cell clone that expresses BORF1, this study found that overexpressing of BSLF1 increases the half-life of BORF1, but overexpression of BSLF1 did not rescue the levels of BORF1 in cells. This study also showed that deubiquitination of Rta or BORF1 does not influence the transactivation activity or increase the stability. Therefore, I further investigated which types of poly-ubiquitin chain did BSLF1 counteract against TRIM5α. Through expressing of K63-only or K48-only types of HA-Ub, this study found that although TRIM5α added both K48 and K63 poly-ubiquitin chains to BORF1, BSLF1 mainly deubiquitinated K63 poly-ubiquitin chain. Together, this study reveals BSLF1 deubiquitination activity and the antagonistic relationship between BSLF1 and TRIM5α. Although more research on how different types of poly-ubiquitin chain affect EBV life cycle is needed, the counteraction between EBV viral protein and host’s post-translational modification is likely important for EBV to escape from inhibition of host cells. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T06:32:43Z (GMT). No. of bitstreams: 1 ntu-107-R05b22019-1.pdf: 2499380 bytes, checksum: ce6e596745caeebea4f8bbb5fea5105d (MD5) Previous issue date: 2018 | en |
dc.description.tableofcontents | 目錄
摘要 i Abstract ii 壹、背景資料 1 一、Epstein-Barr virus (EB病毒) 的發現及關聯病症 1 二、EB病毒的結構及遺傳物質 2 三、EB病毒的生活史 2 四、EB病毒溶裂期的極早期蛋白質 4 五、EB病毒的溶裂期複製 6 六、BSLF1蛋白質 7 七、EB病毒的結構蛋白質 8 八、蛋白質的泛素化 (ubiquitination) 與去泛素化 (deubiquitination) 修飾 8 九、E3泛素連接酶TRIM5α 13 十、EB病毒與泛素化修飾 13 貳、研究目的 15 參、材料與方法 16 一、細胞株培養與繼代 16 二、細胞培養與收取 17 三、細菌表達系統 17 四、質體DNA萃取 17 五、質體與抗體 17 六、細胞轉染 (Tranfection) 18 七、西方點墨法分析 (Western blot analysis) 18 八、變性免疫沉澱法 (Denature Immunoprecipitation, deIP ) 18 九、GST融合蛋白沉降分析 (Glutathione S-transferase pull-down assay) 19 十、冷光報導基因分析 (Luciferase reporter assay) 20 十一、免疫螢光染色法 (Immunofluorescence staining) 20 肆、結果 22 一、BSLF1與TRIM5α在細胞體外及體內的結合 22 二、BSLF1對Rta與BORF1蛋白質的去泛素化並拮抗TRIM5α的活性 23 三、BSLF1蛋白質會與BORF1蛋白質直接結合 24 四、BSLF1會使Rta的轉錄活性下降 24 五、BSLF1使BORF1在細胞內的半衰期延長 25 六、BSLF1對TRIM5α修飾上BORF1的K63鏈結多泛素鏈進行去泛素化 26 伍、討論 28 一、BSLF1蛋白質拮抗宿主E3泛素連接酶TRIM5α之泛素化修飾 28 二、BSLF1蛋白質可以去泛素化修飾Rta及BORF1 30 三、BSLF1蛋白質對Rta進行去泛素化修飾而使轉錄活性下降 31 四、BSLF1蛋白質對BORF1進行去泛素化修飾而延長其半衰期 33 五、BSLF1蛋白質偏好去除BORF1上的K63鏈結多泛素鏈 33 陸、圖表 35 圖1、EB病毒的溶裂期生活史 35 圖2、泛素化修飾與去泛素化修飾 36 圖3、BSLF1可以和TRIM5α在細胞體外直接結合 37 圖4、BSLF1可以和TRIM5α在細胞體內共定位 38 圖5、BSLF1可以對BORF1進行去泛素化修飾 39 圖6、BSLF1可以去除TRIM5α對Rta的泛素化修飾 40 圖7、BSLF1可以去除TRIM5α對BORF1的泛素化修飾 41 圖8、BSLF1可以和BORF1直接結合 42 圖9、BSLF1使Rta轉錄活性下降 43 圖10、BSLF1使BORF1的半衰期延長 45 圖11、BSLF1可以去除TRIM5α對BORF1加上的K63鏈結多泛素鏈 47 表1:本研究所使用的質體 48 表2:本研究所使用的抗體 50 柒、參考資料 51 捌、附錄 64 附錄1、TRIM5α蛋白質結構與作用機制 64 附錄2、BPLF1去泛素酶活性干擾宿主細胞內生免疫系統之機制 65 | |
dc.language.iso | zh-TW | |
dc.title | EB病毒BSLF1蛋白質的去泛素酶活性與E3泛素連接酶TRIM5α的拮抗 | zh_TW |
dc.title | Counteracting E3 Ubiquitin Ligase TRIM5α by the Deubiquitinase Activity of BSLF1 of Epstein-Barr Virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 106-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉世東(Shih-Tung Liu),林晉玄(Ching-Hsuan Lin),張世宗(Shih-Chung Chang),羅凱尹(Kai-Yin Lo) | |
dc.subject.keyword | EB病毒,BSLF1,去泛素化修飾,TRIM5α, | zh_TW |
dc.subject.keyword | Epstein-Barr virus,BSLF1,deubiquitination,TRIM5α, | en |
dc.relation.page | 65 | |
dc.identifier.doi | 10.6342/NTU201803743 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2018-08-16 | |
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 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-107-1.pdf 目前未授權公開取用 | 2.44 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。