請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/39006
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張世宗助理教授 | |
dc.contributor.author | Yung-Cheng Shin | en |
dc.contributor.author | 辛永誠 | zh_TW |
dc.date.accessioned | 2021-06-13T16:57:03Z | - |
dc.date.available | 2011-07-27 | |
dc.date.copyright | 2011-07-27 | |
dc.date.issued | 2011 | |
dc.date.submitted | 2011-07-14 | |
dc.identifier.citation | 參考文獻
Amerik, A.Y., Li, S.J., and Hochstrasser, M. (2000). Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol Chem 381, 981-992. Baba, D., Maita, N., Jee, J.G., Uchimura, Y., Saitoh, H., Sugasawa, K., Hanaoka, F., Tochio, H., Hiroaki, H., and Shirakawa, M. (2005). Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Nature 435, 979-982. Baba, D., Maita, N., Jee, J.G., Uchimura, Y., Saitoh, H., Sugasawa, K., Hanaoka, F., Tochio, H., Hiroaki, H., and Shirakawa, M. (2006). Crystal structure of SUMO-3-modified thymine-DNA glycosylase. J Mol Biol 359, 137-147. Boggio, R., and Chiocca, S. (2006). Viruses and sumoylation: recent highlights. Curr Opin Microbiol 9, 430-436. Chen, A., Wang, P.Y., Yang, Y.C., Huang, Y.H., Yeh, J.J., Chou, Y.H., Cheng, J.T., Hong, Y.R., and Li, S.S. (2006). SUMO regulates the cytoplasmonuclear transport of its target protein Daxx. J Cell Biochem 98, 895-911. Chosed, R., Mukherjee, S., Lois, L.M., and Orth, K. (2006). Evolution of a signalling system that incorporates both redundancy and diversity: Arabidopsis SUMOylation. Biochem J 398, 521-529. Chosed, R., Tomchick, D.R., Brautigam, C.A., Mukherjee, S., Negi, V.S., Machius, M., and Orth, K. (2007). Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases. J Biol Chem 282, 6773-6782. Colby, T., Matthai, A., Boeckelmann, A., and Stuible, H.P. (2006). SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis. Plant Physiol 142, 318-332. Desterro, J.M., Rodriguez, M.S., and Hay, R.T. (1998). SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 2, 233-239. Desterro, J.M., Rodriguez, M.S., Kemp, G.D., and Hay, R.T. (1999). Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J Biol Chem 274, 10618-10624. Desterro, J.M., Thomson, J., and Hay, R.T. (1997). Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett 417, 297-300. Dohmen, R.J. (2004). SUMO protein modification. Biochim Biophys Acta 1695, 113-131. Dorval, V., and Fraser, P.E. (2007). SUMO on the road to neurodegeneration. Biochim Biophys Acta 1773, 694-706. Geoffroy, M.C., Jaffray, E.G., Walker, K.J., and Hay, R.T. (2010). Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell 21, 4227-4239. Gutierrez, G.J., and Ronai, Z. (2006). Ubiquitin and SUMO systems in the regulation of mitotic checkpoints. Trends Biochem Sci 31, 324-332. Harder, Z., Zunino, R., and McBride, H. (2004). Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 14, 340-345. Hay, R.T. (2004). Modifying NEMO. Nat Cell Biol 6, 89-91. Hay, R.T. (2005). SUMO: a history of modification. Mol Cell 18, 1-12. Hay, R.T. (2006). Role of ubiquitin-like proteins in transcriptional regulation. Ernst Schering Res Found Workshop, 173-192. Hay, R.T. (2007). SUMO-specific proteases: a twist in the tail. Trends Cell Biol 17, 370-376. Herrmann, J., Lerman, L.O., and Lerman, A. (2007). Ubiquitin and ubiquitin-like proteins in protein regulation. Circ Res 100, 1276-1291. Holmstrom, S.R., Chupreta, S., So, A.Y., and Iniguez-Lluhi, J.A. (2008). SUMO-mediated inhibition of glucocorticoid receptor synergistic activity depends on stable assembly at the promoter but not on DAXX. Mol Endocrinol 22, 2061-2075. Hotson, A., Chosed, R., Shu, H., Orth, K., and Mudgett, M.B. (2003). Xanthomonas type III effector XopD targets SUMO-conjugated proteins in planta. Mol Microbiol 50, 377-389. Huang, T.T., Wuerzberger-Davis, S.M., Wu, Z.H., and Miyamoto, S. (2003). Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 115, 565-576. Jackson, P.K. (2001). A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases. Genes Dev 15, 3053-3058. Ji, Z., Degerny, C., Vintonenko, N., Deheuninck, J., Foveau, B., Leroy, C., Coll, J., Tulasne, D., Baert, J.L., and Fafeur, V. (2007). Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation. Oncogene 26, 395-406. Jin, J.B., Jin, Y.H., Lee, J., Miura, K., Yoo, C.Y., Kim, W.Y., Van Oosten, M., Hyun, Y., Somers, D.E., Lee, I., et al. (2008). The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affects on FLC chromatin structure. Plant J 53, 530-540. Johnson, E.S. (2004). Protein modification by SUMO. Annu Rev Biochem 73, 355-382. Johnson, E.S., and Blobel, G. (1997). Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J Biol Chem 272, 26799-26802. Johnson, E.S., and Gupta, A.A. (2001). An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106, 735-744. Johnson, E.S., Schwienhorst, I., Dohmen, R.J., and Blobel, G. (1997). The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J 16, 5509-5519. Kagey, M.H., Melhuish, T.A., Powers, S.E., and Wotton, D. (2005). Multiple activities contribute to Pc2 E3 function. EMBO J 24, 108-119. Kagey, M.H., Melhuish, T.A., and Wotton, D. (2003). The polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137. Kerscher, O., Felberbaum, R., and Hochstrasser, M. (2006). Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22, 159-180. Kim, J.H., Choi, H.J., Kim, B., Kim, M.H., Lee, J.M., Kim, I.S., Lee, M.H., Choi, S.J., Kim, K.I., Kim, S.I., et al. (2006). Roles of sumoylation of a reptin chromatin-remodelling complex in cancer metastasis. Nat Cell Biol 8, 631-639. Kim, J.H., Lee, J.M., Nam, H.J., Choi, H.J., Yang, J.W., Lee, J.S., Kim, M.H., Kim, S.I., Chung, C.H., Kim, K.I., et al. (2007). SUMOylation of pontin chromatin-remodeling complex reveals a signal integration code in prostate cancer cells. Proc Natl Acad Sci U S A 104, 20793-20798. Kim, K.I., and Baek, S.H. (2006). SUMOylation code in cancer development and metastasis. Mol Cells 22, 247-253. Kirsh, O., Seeler, J.S., Pichler, A., Gast, A., Muller, S., Miska, E., Mathieu, M., Harel-Bellan, A., Kouzarides, T., Melchior, F., et al. (2002). The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J 21, 2682-2691. Kotaja, N., Karvonen, U., Janne, O.A., and Palvimo, J.J. (2002). PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol Cell Biol 22, 5222-5234. Kretz-Remy, C., and Tanguay, R.M. (1999). SUMO/sentrin: protein modifiers regulating important cellular functions. Biochem Cell Biol 77, 299-309. Kuo, H.Y., Chang, C.C., Jeng, J.C., Hu, H.M., Lin, D.Y., Maul, G.G., Kwok, R.P., and Shih, H.M. (2005). SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc Natl Acad Sci U S A 102, 16973-16978. Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Peres, L., Zhou, J., Zhu, J., Raught, B., and de The, H. (2008). Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat Cell Biol 10, 547-555. Lee, J., Nam, J., Park, H.C., Na, G., Miura, K., Jin, J.B., Yoo, C.Y., Baek, D., Kim, D.H., Jeong, J.C., et al. (2007). Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase. Plant J 49, 79-90. Li, S.J., and Hochstrasser, M. (1999). A new protease required for cell-cycle progression in yeast. Nature 398, 246-251. Li, S.J., and Hochstrasser, M. (2000). The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol Cell Biol 20, 2367-2377. Li, W., and Ye, Y. (2008). Polyubiquitin chains: functions, structures, and mechanisms. Cell Mol Life Sci 65, 2397-2406. Lin, D.Y., Huang, Y.S., Jeng, J.C., Kuo, H.Y., Chang, C.C., Chao, T.T., Ho, C.C., Chen, Y.C., Lin, T.P., Fang, H.I., et al. (2006). Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol Cell 24, 341-354. Lin, J.Y., Ohshima, T., and Shimotohno, K. (2004). Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53. FEBS Lett 573, 15-18. Ling, Y., Sankpal, U.T., Robertson, A.K., McNally, J.G., Karpova, T., and Robertson, K.D. (2004). Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription. Nucleic Acids Res 32, 598-610. Liu, B., and Shuai, K. (2008). Targeting the PIAS1 SUMO ligase pathway to control inflammation. Trends Pharmacol Sci 29, 505-509. Lois, L.M., Lima, C.D., and Chua, N.H. (2003). Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell 15, 1347-1359. Mabb, A.M., Wuerzberger-Davis, S.M., and Miyamoto, S. (2006). PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress. Nat Cell Biol 8, 986-993. Macauley, M.S., Errington, W.J., Scharpf, M., Mackereth, C.D., Blaszczak, A.G., Graves, B.J., and McIntosh, L.P. (2006). Beads-on-a-string, characterization of ETS-1 sumoylated within its flexible N-terminal sequence. J Biol Chem 281, 4164-4172. Mahajan, R., Delphin, C., Guan, T., Gerace, L., and Melchior, F. (1997). A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107. Matunis, M.J., Coutavas, E., and Blobel, G. (1996). A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 135, 1457-1470. Meulmeester, E., Kunze, M., Hsiao, H.H., Urlaub, H., and Melchior, F. (2008). Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell 30, 610-619. Mikolajczyk, J., Drag, M., Bekes, M., Cao, J.T., Ronai, Z., and Salvesen, G.S. (2007). Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs. J Biol Chem 282, 26217-26224. Miura, K., Jin, J.B., and Hasegawa, P.M. (2007a). Sumoylation, a post-translational regulatory process in plants. Curr Opin Plant Biol 10, 495-502. Miura, K., Jin, J.B., Lee, J., Yoo, C.Y., Stirm, V., Miura, T., Ashworth, E.N., Bressan, R.A., Yun, D.J., and Hasegawa, P.M. (2007b). SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and freezing tolerance in Arabidopsis. Plant Cell 19, 1403-1414. Miura, K., Rus, A., Sharkhuu, A., Yokoi, S., Karthikeyan, A.S., Raghothama, K.G., Baek, D., Koo, Y.D., Jin, J.B., Bressan, R.A., et al. (2005). The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses. Proc Natl Acad Sci U S A 102, 7760-7765. Mohan, R.D., Rao, A., Gagliardi, J., and Tini, M. (2007). SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol Cell Biol 27, 229-243. Mohideen, F., and Lima, C.D. (2008). SUMO takes control of a ubiquitin-specific protease. Mol Cell 30, 539-540. Moschos, S.J., and Mo, Y.Y. (2006). Role of SUMO/Ubc9 in DNA damage repair and tumorigenesis. J Mol Histol 37, 309-319. Mukhopadhyay, D., and Dasso, M. (2007). Modification in reverse: the SUMO proteases. Trends Biochem Sci 32, 286-295. Muller, S., Berger, M., Lehembre, F., Seeler, J.S., Haupt, Y., and Dejean, A. (2000). c-Jun and p53 activity is modulated by SUMO-1 modification. J Biol Chem 275, 13321-13329. Muller, S., Ledl, A., and Schmidt, D. (2004). SUMO: a regulator of gene expression and genome integrity. Oncogene 23, 1998-2008. Nacerddine, K., Lehembre, F., Bhaumik, M., Artus, J., Cohen-Tannoudji, M., Babinet, C., Pandolfi, P.P., and Dejean, A. (2005). The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev Cell 9, 769-779. Nishida, T., Terashima, M., and Fukami, K. (2006). PIASy-mediated repression of the Ets-1 is independent of its sumoylation. Biochem Biophys Res Commun 345, 1536-1546. Novatchkova, M., Budhiraja, R., Coupland, G., Eisenhaber, F., and Bachmair, A. (2004). SUMO conjugation in plants. Planta 220, 1-8. Okuma, T., Honda, R., Ichikawa, G., Tsumagari, N., and Yasuda, H. (1999). In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. Biochem Biophys Res Commun 254, 693-698. Orth, K., Xu, Z., Mudgett, M.B., Bao, Z.Q., Palmer, L.E., Bliska, J.B., Mangel, W.F., Staskawicz, B., and Dixon, J.E. (2000). Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science 290, 1594-1597. Percherancier, Y., Germain-Desprez, D., Galisson, F., Mascle, X.H., Dianoux, L., Estephan, P., Chelbi-Alix, M.K., and Aubry, M. (2009). Role of SUMO in RNF4-mediated promyelocytic leukemia protein (PML) degradation: sumoylation of PML and phospho-switch control of its SUMO binding domain dissected in living cells. J Biol Chem 284, 16595-16608. Perry, J.J., Tainer, J.A., and Boddy, M.N. (2008). A SIM-ultaneous role for SUMO and ubiquitin. Trends Biochem Sci 33, 201-208. Pichler, A., Gast, A., Seeler, J.S., Dejean, A., and Melchior, F. (2002). The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120. Pichler, A., Knipscheer, P., Oberhofer, E., van Dijk, W.J., Korner, R., Olsen, J.V., Jentsch, S., Melchior, F., and Sixma, T.K. (2005). SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nat Struct Mol Biol 12, 264-269. Pickart, C.M. (2001). Mechanisms underlying ubiquitination. Annu Rev Biochem 70, 503-533. Prudden, J., Pebernard, S., Raffa, G., Slavin, D.A., Perry, J.J., Tainer, J.A., McGowan, C.H., and Boddy, M.N. (2007). SUMO-targeted ubiquitin ligases in genome stability. EMBO J 26, 4089-4101. Reverter, D., and Lima, C.D. (2005). Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435, 687-692. Riquelme, C., Barthel, K.K., and Liu, X. (2006). SUMO-1 modification of MEF2A regulates its transcriptional activity. J Cell Mol Med 10, 132-144. Roden, J., Eardley, L., Hotson, A., Cao, Y., and Mudgett, M.B. (2004). Characterization of the Xanthomonas AvrXv4 effector, a SUMO protease translocated into plant cells. Mol Plant Microbe Interact 17, 633-643. Rodriguez, M.S., Dargemont, C., and Hay, R.T. (2001). SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem 276, 12654-12659. Rodriguez, M.S., Desterro, J.M., Lain, S., Midgley, C.A., Lane, D.P., and Hay, R.T. (1999). SUMO-1 modification activates the transcriptional response of p53. EMBO J 18, 6455-6461. Ross, S., Best, J.L., Zon, L.I., and Gill, G. (2002). SUMO-1 modification represses Sp3 transcriptional activation and modulates its subnuclear localization. Mol Cell 10, 831-842. Saitoh, H., Pu, R., Cavenagh, M., and Dasso, M. (1997). RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proc Natl Acad Sci U S A 94, 3736-3741. Saitoh, H., Sparrow, D.B., Shiomi, T., Pu, R.T., Nishimoto, T., Mohun, T.J., and Dasso, M. (1998). Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2. Curr Biol 8, 121-124. Sampson, D.A., Wang, M., and Matunis, M.J. (2001). The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 276, 21664-21669. Santiago, A., Godsey, A.C., Hossain, J., Zhao, L.Y., and Liao, D. (2009). Identification of two independent SUMO-interacting motifs in Daxx: Evolutionary conservation from Drosophila to humans and their biochemical functions. Cell Cycle 8. Sapetschnig, A., Rischitor, G., Braun, H., Doll, A., Schergaut, M., Melchior, F., and Suske, G. (2002). Transcription factor Sp3 is silenced through SUMO modification by PIAS1. EMBO J 21, 5206-5215. Schimmel, J., Larsen, K.M., Matic, I., van Hagen, M., Cox, J., Mann, M., Andersen, J.S., and Vertegaal, A.C. (2008). The ubiquitin-proteasome system is a key component of the SUMO-2/3 cycle. Mol Cell Proteomics 7, 2107-2122. Schmidt, D., and Muller, S. (2002). Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc Natl Acad Sci U S A 99, 2872-2877. Schmidt, D., and Muller, S. (2003). PIAS/SUMO: new partners in transcriptional regulation. Cell Mol Life Sci 60, 2561-2574. Schwienhorst, I., Johnson, E.S., and Dohmen, R.J. (2000). SUMO conjugation and deconjugation. Mol Gen Genet 263, 771-786. Shih, H.M., Chang, C.C., Kuo, H.Y., and Lin, D.Y. (2007). Daxx mediates SUMO-dependent transcriptional control and subnuclear compartmentalization. Biochem Soc Trans 35, 1397-1400. Shin, Y.-C., Liu, B.-Y., Tsai, J.-Y., Wu, J.-T., Chang, L.-K., and Chang, S.-C. (2010). Biochemical characterization of the small ubiquitin-like modifiers of Chlamydomonas reinhardtii. Planta 232, 649-662. Song, J., Durrin, L.K., Wilkinson, T.A., Krontiris, T.G., and Chen, Y. (2004). Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc Natl Acad Sci U S A 101, 14373-14378. Stade, K., Vogel, F., Schwienhorst, I., Meusser, B., Volkwein, C., Nentwig, B., Dohmen, R.J., and Sommer, T. (2002). A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast. J Biol Chem 277, 49554-49561. Steinacher, R., and Schar, P. (2005). Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr Biol 15, 616-623. Stielow, B., Sapetschnig, A., Wink, C., Kruger, I., and Suske, G. (2008). SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing. EMBO Rep 9, 899-906. Su, H.L., and Li, S.S. (2002). Molecular features of human ubiquitin-like SUMO genes and their encoded proteins. Gene 296, 65-73. Sun, H., Leverson, J.D., and Hunter, T. (2007). Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J 26, 4102-4112. Suzuki, T., Ichiyama, A., Saitoh, H., Kawakami, T., Omata, M., Chung, C.H., Kimura, M., Shimbara, N., and Tanaka, K. (1999). A new 30-kDa ubiquitin-related SUMO-1 hydrolase from bovine brain. J Biol Chem 274, 31131-31134. Takahashi, H., Hatakeyama, S., Saitoh, H., and Nakayama, K.I. (2005). Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J Biol Chem 280, 5611-5621. Tatham, M.H., Geoffroy, M.C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E.G., Palvimo, J.J., and Hay, R.T. (2008). RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10, 538-546. Tatham, M.H., Jaffray, E., Vaughan, O.A., Desterro, J.M., Botting, C.H., Naismith, J.H., and Hay, R.T. (2001). Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem 276, 35368-35374. Ungureanu, D., Vanhatupa, S., Kotaja, N., Yang, J., Aittomaki, S., Janne, O.A., Palvimo, J.J., and Silvennoinen, O. (2003). PIAS proteins promote SUMO-1 conjugation to STAT1. Blood 102, 3311-3313. Valin, A., and Gill, G. (2007). Regulation of the dual-function transcription factor Sp3 by SUMO. Biochem Soc Trans 35, 1393-1396. Verger, A., Perdomo, J., and Crossley, M. (2003). Modification with SUMO. A role in transcriptional regulation. EMBO Rep 4, 137-142. von Gromoff, E.D., Schroda, M., Oster, U., and Beck, C.F. (2006). Identification of a plastid response element that acts as an enhancer within the Chlamydomonas HSP70A promoter. Nucleic Acids Res 34, 4767-4779. Wang, Y., Ladunga, I., Miller, A.R., Horken, K.M., Plucinak, T., Weeks, D.P., and Bailey, C.P. (2008). The small ubiquitin-like modifier (SUMO) and SUMO-conjugating system of Chlamydomonas reinhardtii. Genetics 179, 177-192. Weisshaar, S.R., Keusekotten, K., Krause, A., Horst, C., Springer, H.M., Gottsche, K., Dohmen, R.J., and Praefcke, G.J. (2008). Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML. FEBS Lett 582, 3174-3178. Welchman, R.L., Gordon, C., and Mayer, R.J. (2005). Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6, 599-609. Wotton, D., and Merrill, J.C. (2007). Pc2 and SUMOylation. Biochem Soc Trans 35, 1401-1404. Wuerzberger-Davis, S.M., Nakamura, Y., Seufzer, B.J., and Miyamoto, S. (2007). NF-kappaB activation by combinations of NEMO SUMOylation and ATM activation stresses in the absence of DNA damage. Oncogene 26, 641-651. Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X., Nicosia, S.V., Bhalla, K., and Bai, W. (2007). SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat Cell Biol 9, 1253-1262. Yeh, E.T. (2008). SUMOylation and de-SUMOylation: Wrestling with life's processes. J Biol Chem. Yoo, C.Y., Miura, K., Jin, J.B., Lee, J., Park, H.C., Salt, D.E., Yun, D.J., Bressan, R.A., and Hasegawa, P.M. (2006). SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid. Plant Physiol 142, 1548-1558. Zheng, G., and Yang, Y.C. (2004). ZNF76, a novel transcriptional repressor targeting TATA-binding protein, is modulated by sumoylation. J Biol Chem 279, 42410-42421. Zheng, G., and Yang, Y.C. (2006). Acetylation and alternative splicing regulate ZNF76-mediated transcription. Biochem Biophys Res Commun 339, 1069-1075. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/39006 | - |
dc.description.abstract | SUMO (small ubiquitin-like modifier) 在1996年被第一次發現,當時它被當成是附在RanGAP1 (Ran GTPase-activating protein 1) 上的一段多肽。後來更多的研究顯示SUMO可以修飾細胞中許多的蛋白質,進而影響真核細胞中各種重要的基因表現與訊息傳導等路徑。然而,對植物系統之SUMO化的研究仍然不足,尤其是單細胞綠藻。因此本研究擬建立單胞微藻Chlamydomonas reinhardtii的SUMO化系統來進行初步的研究。經由選殖出單胞微藻三種SUMO (CrSUMO96、CrSUMO97與CrSUMO148) 的DNA序列,將其表現純化並利用哺乳類SUMO系統中的 E1 (SAE1/SAE2 or Aos1/Uba2) 與E2 (Ubc9) 來進行其生化性質的鑑定。實驗結果顯示不管是在胞外或在大腸桿菌內進行 SUMO化測試,C-端為di-glycine motif的CrSUMO96或CrSUMO97皆會形成polySUMO chain;而C-端不是以di-glycine motif結尾時則沒有此現象發生,證明露出C端di-glycine motif為進行SUMO化的必要條件。而在SUMO protease的活性測試中也可以看到,SENP1 (human SUMO protease) 可以對CrSUMO96與CrSUMO97進行processing,使CrSUMO96與CrSUMO97形成可以進行SUMO化修飾且C-端為di-glycine motif的型態,並發現SENP1對CrSUMO97 processing的活性比CrSUMO96來的強。而CrSUMO148在其C端具有四個序列重複的di-glycine motif,這個特色並不出現於其他物種的SUMO,在經過SENP1作用後,不管是何種長度的CrSUMO148都只會形成CrSUMO1481-83,即只含有一個di-glycine motif的型態。而經由建構不同長度的CrSUMO148所進行之胞外SUMO化測試發現,也只有CrSUMO1481-83才真正具有進行SUMO化的功能。此外本研究也進行了三種CrSUMO 的desumoylation活性測試。將三種CrSUMO的poly-chain與SENP1進行反應。發現所有的polySUMO chain在經SENP1作用下皆幾乎完全形成只有monoSUMO存在的型態。 | zh_TW |
dc.description.abstract | SUMO (small ubiquitin-like modifier) was originally discovered in 1996, as a peptide associating with RanGAP1 (Ran GTPase-activating protein 1). More studies subsequently found that SUMO can modify many proteins and influence many cellular processes of gene expression and signal transduction in eukaryotes. However, investigation of sumoylation on plant systems, especially on unicellular green algae, remains little. Thus, this work was aimed to study the SUMO system in Chlamydomonas reinhardtii and also characterize their biochemical properties. Three genes encoding for SUMO proteins from Chlamydomonas reinhardtii have been identified and named CrSUMO96, CrSUMO97 and CrSUMO148. Using the E1 activating enzyme (SAE1/SAE2 or Aos1/Uba2) and E2 conjugating enzyme (Ubc9) of the animal SUMO system, the present data reveal that CrSUMO96 and CrSUMO97 with an exposed di-glycine motif at the C-terminus can form polymeric chains, whereas the polymeric chain was not observed by using the full length of CrSUMO96 or CrSUMO97 as the assay substrate. It clearly demonstrates that the exposed C-terminal di-glycine end is required for sumoylation. In SUMO processing activity assay, human SENP1 showed greater processing activity toward CrSUMO97 than CrSUMO96. Interestingly, CrSUMO148 have four repeated di-glycine motif at the C-terminus, which are not found in other SUMO proteins. SENP1 specifically digests CrSUMO148 at the first di-glycine motif to generate CrSUMO1481-83. Furthermore, only CrSUMO1481-83 can form polymeric chain in the in vitro sumoylation assay. The deconjugation activity of SENP1 towards poly-SUMO chains showed that all polyCrSUMO chains can be completely deconjugated to form SUMO monomers. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T16:57:03Z (GMT). No. of bitstreams: 1 ntu-100-R98b47203-1.pdf: 2125758 bytes, checksum: b25bf1feff8afad112402544be6c37ab (MD5) Previous issue date: 2011 | en |
dc.description.tableofcontents | 目錄
摘要 i Abstract ii 縮寫表 iii 第一章 緒論 1 1.1 SUMO簡介 1 1.2 SUMO化與去SUMO化 2 1.3 SUMO化修飾參與之生理功能 4 1.4 SUMO之聚合反應 7 1.5 SUMO化共有基序 8 1.6 植物之SUMO系統 9 1.7 研究動機與方向 10 第二章 材料與方法 12 2.1 單胞微藻 (Chlamydomonas reinhardtii) 與培養條件 12 2.2 大腸桿菌菌株 12 2.3 表現載體之建構 13 2.3.1 原核表現系統載體 13 2.3.2 Total mRNA 分離及反轉錄聚合酶連鎖反應 (RT-PCR) 13 2.3.3 聚合酶連鎖反應 14 2.3.4 限制酶切反應 15 2.3.5 接合反應 15 2.3.6 勝任細胞之製備 (Competent cell preparation) 15 2.3.7 質體之轉型 16 2.3.8 質體DNA製備 (Miniprep) 16 2.3.9 洋菜膠電泳 17 2.3.10 DNA片段之分離純化法 (Gel extraction) 17 2.3.11 DNA定量 18 2.4 重組蛋白質誘導表現 18 2.5 重組蛋白質之純化方法 19 2.5.1 6x-His重組蛋白質親和性層析法 19 2.5.2 GST重組蛋白質親和性層析法 19 2.5.3 蛋白質脫鹽與濃縮 20 2.6 蛋白質相關基本操作方法 20 2.6.1 蛋白質定量 20 2.6.2 蛋白質電泳檢定 20 2.6.2.1 SDS-PAGE膠體電泳 21 2.6.2.2 梯度膠體電泳 21 2.6.3 Coomassie Brilliant Blue R-250 (CBR) 蛋白質染色法 22 2.6.4 蛋白質電泳轉印 22 2.6.5 酵素免疫染色法 (Immunoblotting) 23 2.7 CrSUMO生理性質測試 23 2.7.1 胞外SUMO化反應 23 2.7.2 胞內SUMO化反應 24 2.7.3 SUMO protease活性分析 24 2.8 CrSUMO多株抗體製備 25 第三章 結果與討論 26 3.1 CrSUMO96、CrSUMO97與CrSUMO148基因選殖 26 3.1.1 CrSUMO96、CrSUMO97與CrSUMO148表現載體之建構與確認 26 3.1.2 CrSUMO96GG、CrSUMO97GG與CrSUMO148GG表現載體之建構與確認 27 3.2 CrSUMO96GG、CrSUMO97GG與CrSUMO148-1~4GG生理性質測試 28 3.2.1 SUMO與in vitro SUMO化酵素之蛋白質表現 28 3.2.2 in vitro SUMO化系統之建立 30 3.2.3 大腸桿菌內SUMO化修飾系統之建立與分析 31 3.2.4 SUMO蛋白酶SENP1對CrSUMO processing之活性分析 32 3.2.5 SUMO蛋白酶SENP1對poly-CrSUMO deconjugation之活性分析 35 3.3 檢視熱處理後單胞綠藻SUMO化修飾量的改變 35 第四章 未來展望 37 參考文獻 38 圖與表 49 附錄 66 碩士論文口試問答摘要 72 | |
dc.language.iso | zh-TW | |
dc.title | 單胞微藻Chlamydomonas reinhardtii SUMO之生化性質分析 | zh_TW |
dc.title | Biochemical characterization of the small ubiquitin-like modifiers of Chlamydomonas reinhardtii | en |
dc.type | Thesis | |
dc.date.schoolyear | 99-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 莊榮輝教授,陳威戎副教授,張麗冠副教授,鄭貽生助理教授 | |
dc.subject.keyword | 類泛素小蛋白質修飾物,類泛素小蛋白質修飾物蛋白酶,雙胱胺酸基序,人類類泛素小蛋白質修飾物活化酶,小鼠類泛素小蛋白質修飾物活化酶,類泛素小蛋白質修飾物銜接酶, | zh_TW |
dc.subject.keyword | SUMO,SENP1,di-glycine motif,SAE1/SAE2,Aos1/Uba2,Ubc9, | en |
dc.relation.page | 75 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2011-07-14 | |
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-100-1.pdf 目前未授權公開取用 | 2.08 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。