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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 靳宗洛(Tsung-Luo Jinn) | |
dc.contributor.author | Shu-Fan Lin | en |
dc.contributor.author | 林書帆 | zh_TW |
dc.date.accessioned | 2021-06-17T00:28:38Z | - |
dc.date.available | 2017-03-19 | |
dc.date.copyright | 2012-03-19 | |
dc.date.issued | 2012 | |
dc.date.submitted | 2012-02-14 | |
dc.identifier.citation | Abreu, I.A., and Cabelli, D.E. (2010). Superoxide dismutases-a review of the metal-associated mechanistic variations. Biochimica et biophysica acta 1804, 263-274.
Allen, M.D., Kropat, J., Tottey, S., Del Campo, J.A., and Merchant, S.S. (2007). Manganese deficiency in Chlamydomonas results in loss of photosystem II and MnSOD function, sensitivity to peroxides, and secondary phosphorus and iron deficiency. Plant Physiol. 143, 263-277. Alscher, R.G., Erturk, N., and Heath, L.S. (2002). Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. Journal of experimental botany 53, 1331-1341. Archibald, F. (2003). Oxygen toxicity and the health and survival of eukaryote cells: a new piece is added to the puzzle. Proc. Natl. Acad. Sci. USA 100, 10141-10143. Balk, J., and Lobreaux, S. (2005). Biogenesis of iron-sulfur proteins in plants. Trends in plant science 10, 324-331. Bannister, J.V., Bannister, W.H., and Rotilio, G. (1987). Aspects of the structure, function, and applications of superoxide dismutase. Critical Reviews in Biochemistry 22, 111-180. Beinert, H. (2000). Iron-sulfur proteins: ancient structures, still full of surprises. Journal of Biological Inorganic Chemistry 5, 2-15. Bender, T., Lewrenz, I., Franken, S., Baitzel, C., and Voos, W. (2011). Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. Molecular biology of the cell 22, 541-554. Blokhina, O., and Fagerstedt, K.V. (2010). Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems. Physiologia plantarum 138, 447-462. Bowler, C., Montagu, M.V., and Inze, D. (1992). Superoxide dismutase and stress tolerance. Annu. Rev. Plant Physiol. 43, 83-116. Bowler, C., Van Camp, W., Van Montagu, M., Inzé, D., and Asada, K. (1994). Superoxide Dismutase in Plants. Critical Reviews in Plant Sciences 13, 199-218. Briat, J.F., Ravet, K., Arnaud, N., Duc, C., Boucherez, J., Touraine, B., Cellier, F., and Gaymard, F. (2010). New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Annals of botany 105, 811-822. Camp, W.V., Inze, D., and Vanmontagu, M. (1997). The regulation and function of tobacco superoxide dismutases. Free Radical Biology & Medicine 23, 515-520. Camp, W.V., Capiau, K., Montagu, M.V., Inzé, D., and Slooten, L. (1996). Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-Superoxide dismutase in chloroplasts. Plant Physiol. 112, 1703-1714. Camp, W.V., Hérouart, D., Willekens, H., Takahashi, H., Saito, K., Montagu, M.V., and lnzé, D. (1996). Tissue-Specific Activity of Two Manganese Superoxide Dismutase Promoters in Transgenic Tobacco. Plant Physiol. 112, 525-535. Camp, W.V., Willekens, H., Bowler, C., Montagu, M.V., Inze, D., Reupold-Popp, P., Jr, H.S., and Langebartels, C. (1994). Elevated levels of superoxide dismutase pretect transgenic plants against ozone damage. Biotechnology 12, 165-168. Chen, X. Z., Peng, J. B., Cohen, A., Nelson, H., Nelson, N., and Hediger, M. A. (1999). Yeast SMF1 mediates H(+)-coupled iron uptake with concomitant uncoupled cation currents.J. Biol. Chem. 274, 35089-35094. Chu, C.C., Lee, W.C., Guo, W.Y., Pan, S.M., Chen, L.J., Li, H.M., and Jinn, T.L. (2005). A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis. Plant Physiol. 139, 425-436. Clough, S.J., Bent A.F. (1998). Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-43. Frazzon, A.P., Ramirez, M.V., Warek, U., Balk, J., Frazzon, J., Dean, D.R., and Winkel, B.S. (2007). Functional analysis of Arabidopsis genes involved in mitochondrial iron-sulfur cluster assembly. Plant molecular biology 64, 225-240. Fridovich, I. (1978). The biology of oxygen radicals. Science 201, 875-880. Gao, X., Ren, Z., Zhao, Y., and Zhang, H. (2003). Overexpression of SOD2 increases salt tolerance of Arabidopsis. Plant Physiol. 133, 1873-1881. Giles, S.S., Batinic-Haberle, I., Perfect, J.R., and Cox, G.M. (2005). Cryptococcus neoformans mitochondrial superoxide dismutase: an essential link between antioxidant function and high-temperature growth. Eukaryotic cell 4, 46-54. Gill, T., Sreenivasulu, Y., Kumar, S., and Ahuja, P.S. (2010). Over-expression of superoxide dismutase exhibits lignification of vascular structures in Arabidopsis thaliana. Journal of plant physiology 167, 757-760. Halliwell, B. (1994). Free radicals, antioxidants, and human disease: curiosity, cause, or consequence? Lancet 344: 721-724. Halliwell, B., and Gutteridge, J.M.C. (1984). Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219, 1-14. Jeong, J., and Guerinot, M.L. (2009). Homing in on iron homeostasis in plants. Trends in plant science 14, 280-285. Juan, D., Zhen, Z., and Wan-Chen, L. (2006). Over-expression of Exotic Superoxide Dismutase Gene MnSOD in maize. Journal of Plant Physiology and Molecular Biology 32, 57-63. Kim, S.A., and Guerinot, M.L. (2007). Mining iron: iron uptake and transport in plants. FEBS letters 581, 2273-2280. Kliebenstein, D.J., Monde, R.-A., and Last, R.L. (1998). Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization. Plant Physiol. 118, 637-650. Koehler, C.M., Jarosch, E., Tokatlidis, K., Schmid, K., Schweyen, R.J., and Schatz, G. (1998). Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science 279, 369-373. Kunji, E.R.S. (2004). The role and structure of mitochondrial carriers. FEBS letters 564, 239-244. Lanquar, V., Ramos, M.S., Lelievre, F., Barbier-Brygoo, H., Krieger-Liszkay, A., Kramer, U., and Thomine, S. (2010). Export of vacuolar manganese by AtNRAMP3 and AtNRAMP4 is required for optimal photosynthesis and growth under manganese deficiency. Plant Physiol. 152, 1986-1999. Li, Y., Reuter, N.P., Li, X., Liu, Q., Zhang, J., and Martin, R.C. (2010). Colocalization of MnSOD expression in response to oxidative stress. Molecular carcinogenesis 49, 44-53. Li, W., Qi, L., Lin, X., Chen, H., Ma, Z., Wu, K., and Huang, S. (2009). The expression of manganese superoxide dismutase gene from Nelumbo nucifera responds strongly to chilling and oxidative stresses. Journal of integrative plant biology 51, 279-286. Lill, R. (2009). Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838. Loprasert, S., Vattanaviboon, P., Praituan, W., Chamnongpol, S., and Mongkolsuk, S. (1996). Regulation of the oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas- a review. Gene 179, 33-37. Luk, E.E., and Culotta, V.C. (2001). Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. The Journal of biological chemistry 276, 47556-47562. Luk, E., Carroll, M., Baker, M., and Culotta, V.C. (2003). Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family. Proc. Natl. Acad. Sci. USA 100, 10353-10357. Luk, E., Yang, M., Jensen, L.T., Bourbonnais, Y., and Culotta, V.C. (2005). Manganese activation of superoxide dismutase 2 in the mitochondria of Saccharomyces cerevisiae. The Journal of biological chemistry 280, 22715-22720. Maret, W. (2010). Metalloproteomics, metalloproteomes, and the annotation of metalloproteins. Metallomics : integrated biometal science 2, 117-125. Marschner H. (1995). Mineral nutrition of higher plants, 2nd edn. Academic, London McNaughton, R.L., Reddi, A.R., Clement, M.H.S., Sharma, A., Barnese, K., Rosenfeld, L., Gralla, E.B., Valentine, J.S., Culotta, V.C., and Hoffman, B.M. (2010). Probing in vivo Mn2+ speciation and oxidative stress resistance in yeast cells with electron-nuclear double resonance spectroscopy. Proc. Natl. Acad. Sci. USA 107, 15335-15339. Meier, B., Barra, D., Bossa, F., Calabrese, L., and Rotilio, G., (1982). Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied, J. Biol. Chem. 257, 13977-13980. Millar, A.H., and Heazlewood, J.L. (2003). Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis. Plant Physiol. 131, 443-453. Millar, A.H., Heazlewood, J.L., Kristensen, B.K., Braun, H.P., and Moller, I.M. (2005). The plant mitochondrial proteome. Trends in plant science 10, 36-43. Mills R.F., Doherty M.L., Lopez-Marques R.L., Weimar T., Dupree P., Palmgreen M.G., Pittman J.K., Williams L.E. (2008). ECA3, a golgi-localized P2A-type ATPase, plays a crucial role in manganese Nutrition in Arabidopsis. Plant Physiol. 146,116-128. Mittler, R., Vanderauwera, S., Gollery, M., and Van Breusegem, F. (2004). Reactive oxygen gene network of plants. Trends in plant science 9, 490-498. Mizuno, K., Whittaker, M.M., Bachinger, H.P., and Whittaker, J.W. (2004). Calorimetric studies on the tight binding metal interactions of Escherichia coli manganese superoxide dismutase. The Journal of biological chemistry 279, 27339-27344. Morgan, M.J., Lehmann, M., Schwarzlander, M., Baxter, C.J., Sienkiewicz-Porzucek, A., Williams, T.C., Schauer, N., Fernie, A.R., Fricker, M.D., Ratcliffe, R.G., Sweetlove, L.J., and Finkemeier, I. (2008). Decrease in manganese superoxide dismutase leads to reduced root growth and affects tricarboxylic acid cycle flux and mitochondrial redox homeostasis. Plant Physiol. 147, 101-114. Naranuntarat, A., Jensen, L.T., Pazicni, S., Penner-Hahn, J.E., and Culotta, V.C. (2009). The interaction of mitochondrial iron with manganese superoxide dismutase. The Journal of biological chemistry 284, 22633-22640. Nouet, C., Motte, P., and Hanikenne, M. (2011). Chloroplastic and mitochondrial metal homeostasis. Trends in plant science 16, 395-404. O’Halloran T.V., Culotta V.C. (2000). Metallochaperones: an intracellular shuttle service for metal ions. J Biol Chem 275, 25057-25060. Pan, S.M., Hwang, G.B., and Liu, H.C. (1999). Over-expression and characterization of copper/zinc-superoxide dismutase from rice in Escherichia coli. Bot. Bull. Acad. Sin. 40, 275-281. Peiter E., Montanini B., Gobert A., Pedas P., Husted S., Maathuis F.J.M., Blaudez D., Chalot M., Sanders D. (2007). A secretory pathway-localized cation diffusion facilitor confers plant manganese tolerance. Proc Natl Acad Sci USA 104, 8532-8537. Perry, J.J., Shin, D.S., Getzoff, E.D., and Tainer, J.A. (2010). The structural biochemistry of the superoxide dismutases. Biochimica et biophysica acta 1804, 245-262. Picault N., Hodges M., Palmieri L. and Palmieri F. (2004). The growing family of mitochondrial carriers in Arabidopsis. Trends in Plant Science 9, 138-146. Pilon, M., Ravet, K., and Tapken, W. (2011). The biogenesis and physiological function of chloroplast superoxide dismutases. Biochimica et biophysica acta 1807, 989-998. Pilon, M., Cohu, C.M., Ravet, K., Abdel-Ghany, S.E., and Gaymard, F. (2009). Essential transition metal homeostasis in plants. Current opinion in plant biology 12, 347-357. Portnoy M.E., Liu X.F. and Culotta V.C. (2000). Saccharomyces cerevisiae expresses three functionally distinct homologues of the nramp family of metal transporters. Mol Cell Biol 20, 7893-7902. Poschenrieder, C., Tolra, R., and Barcelo, J. (2006). Can metals defend plants against biotic stress? Trends in plant science 11, 288-295. Pugh S.Y. and Fridovich I. (1985). Induction of superoxide dismutases in Escherichia coli B by metal chelators. J Bacteriol 162, 196-202. Puig S. and Peñarrubia L. (2009). Placing metal micronutrients in context: transport and distribution in plants. Curr Opin Plant Biol 12, 299-306. Ramirez, L., Zabaleta, E.J., and Lamattina, L. (2010). Nitric oxide and frataxin: two players contributing to maintain cellular iron homeostasis. Annals of botany 105, 801-810. Rich, P.R., and Bonner, W.D. (1978). The sites of superoxide anion generation in higher plant mitochondria. Archives of Biochemistry and Biophysics 188, 206-213. Richardsona, D.R., Lanea, D.J.R., Beckera, E.M., Huanga, M.L.H., Whitnalla, M., Rahmantoa, Y.S., Sheftelb, A.D., and Ponkac, P. (2010). Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol. Proc Natl Acad Sci USA 107, 10775-10782. Rio, L.A.d., Sandalio, L.M., A, D., Altomare, and Zilinkas, B.A. (2003). Mitochondrial and peroxisomal manganese superoxode dismutase: differential expression during leaf senescence. Journal of experimental botany 54, 923-933. Robinson, A.J., and Kunji, E.R. (2006). Mitochondrial carriers in the cytoplasmic state have a common substrate binding site. Proc. Natl. Acad. Sci. USA 103, 2617-2622. Rodriguez-Serrano, M., Romero-Puertas, M.C., Pastori, G.M., Corpas, F.J., Sandalio, L.M., del Rio, L.A., and Palma, J.M. (2007). Peroxisomal membrane manganese superoxide dismutase: characterization of the isozyme from watermelon cotyledons. Journal of experimental botany 58, 2417-2427. Schwarzlander, M., Fricker, M.D., and Sweetlove, L.J. (2009). Monitoring the in vivo redox state of plant mitochondria: effect of respiratory inhibitors, abiotic stress and assessment of recovery from oxidative challenge. Biochimica et biophysica acta 1787, 468-475. Sevilla F., LoÂpez-Gorge J., del RõÂo LA. (1982). Characterization of a manganese superoxide dismutase from the higher plant Pisum sativum L. Plant Physiol. 70, 1321-1326. Sjöling, S., and Glaser, E. (1998). Mitochondrial targeting peptides in plants. Trends in plant science 3, 136-140. Slooten, L., Capiau, K., Camp, W.V., Montagu, M.V., Sybesma, C., and lnzé, D. (1995). Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing manganese superoxide dismutase in the chloroplasts. Plant Physiol. 107, 737-750. Stemmler, T.L., Lesuisse, E., Pain, D., and Dancis, A. (2010). Frataxin and mitochondrial FeS cluster biogenesis. The Journal of biological chemistry 285, 26737-26743. Su, Z., Chai, M.F., Lu, P.L., An, R., Chen, J., and Wang, X.C. (2007). AtMTM1, a novel mitochondrial protein, may be involved in activation of the manganese-containing superoxide dismutase in Arabidopsis. Planta 226, 1031-1039. Sweetlove, L.J., Fait, A., Nunes-Nesi, A., Williams, T., and Fernie, A.R. (2007). The mitochondrion: an integration point of cellular metabolism and signalling. Critical Reviews in Plant Sciences 26, 17-43. Takahashi, M.A., and Asada, K. (1983). Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch. Biochem. Biophys. 226, 558-566. Tan, Y.F., O'Toole, N., Taylor, N.L., and Millar, A.H. (2010). Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function. Plant Physiol. 152, 747-761. Teschner, J., Lachmann, N., Schulze, J., Geisler, M., Selbach, K., Santamaria-Araujo, J., Balk, J., Mendel, R.R., and Bittner, F. (2010). A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in molybdenum cofactor biosynthesis. The Plant cell 22, 468-480. Touati, D. (1988). Molecular genetics of superoxide dismutases. Free Radical Biology & Medicine 5, 393-402. Tsang, E.W.T., Bowler, C., Herouart, D., Camp, W.V., Villarroel, R., Genetello, C., Montagu, M.V., and Inze, D. (1991). Differential regulation of superoxide dismutases in plants exposed to environmental stress. The Plant cell 3, 783-792. Van Aken, O., Zhang, B., Carrie, C., Uggalla, V., Paynter, E., Giraud, E., and Whelan, J. (2009). Defining the mitochondrial stress response in Arabidopsis thaliana. Molecular plant 2, 1310-1324. Van Camp, W., H. Willekens, C. Bowler, M. Van Montagu, D. Inze, C. Langebartels and H. Sandermann (1994). Elevated levels of superoxide dismutase protect transgenic plants against ozone damage. Bio Technology 12, 165-8. Walker J.E., Runswick M. (1993). The mitochondrial transport protein superfamily. J Bioenerg Biomembr 25, 435-446. Wang, Y., Ying, Y., Chen, J., and Wang, X. (2004). Transgenic Arabidopsis overexpressing Mn-SOD enhanced salt-tolerance. Plant Science 167, 671-677. Wang, Y.C., Qu, G.Z., Li, H.Y., Wu, Y.J., Wang, C., Liu, G.F., and Yang, C.P. (2010). Enhanced salt tolerance of transgenic poplar plants expressing a manganese superoxide dismutase from Tamarix androssowii. Molecular biology reports 37, 1119-1124. Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., Yin, J., Mattson, M.P., Kao, J.P., Lakatta, E.G., Sheu, S.S., Ouyang, K., Chen, J., Dirksen, R.T., and Cheng, H. (2008). Superoxide flashes in single mitochondria. Cell 134, 279-290. Wintz, H. (2006). Iron homeostasis in plants: when transcription affects translocation. Cell research 16, 797-798. Witholt, R., Gwiazda, R.H. and Smith, D.R. (2000). The neurobehavioral effects of subchronic manganese exposure in the presence and absence of pre-parkinsonism. Neurotoxicol. Teratol. 22, 851-861. Yang, M., Cobine, P.A., Molik, S., Naranuntarat, A., Lill, R., Winge, D.R., and Culotta, V.C. (2006). The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2. The EMBO Journal 25, 1775-1783. Yoo, S.D., Cho, Y.H., and Sheen, J. (2007). Arabidopsis mesophyll protoplasts: a versatile cell system for transient gene expression analysis. Nature protocols 2, 1565-1572. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/66283 | - |
dc.description.abstract | 錳超氧歧化酶為對抗粒線體中氧化逆境的第一道防線,但對於其活化機制卻是所知甚少。目前已知在酵母菌中,存在著一個名為MTM1(manganese trafficking factor for mitochondrial SOD2)的蛋白質,其為參與運輸物質進出粒腺體的載體家族(Mitochondrial Carrier Family,MCF)成員之一,並發現MTM1對於錳超氧歧化酶的活性,有顯著的影響。在本研究中證實,兩個同屬於阿拉伯芥粒腺體中運送物質載體家族的成員,AtMTM1 (At4g27940)及AtMTM2 (At2g46320),與酵母菌yMTM1具有相似的功能。利用螢光蛋白標記的方法,我們證實了AtMTM1與AtMTM2均座落在粒線體中。此外,利用雙分子螢光互補系統,更加證實了阿拉伯芥的錳超氧歧化酶(AtMSD1),與AtMTM1、AtMTM2彼此存在著交互作用的關係。然而,AtMTM1和AtMTM2在不同器官的表現量及其在氧化逆境下的誘導量,均有顯著性的差異。在轉殖株的部分,相較於野生型,當AtMTM2剔除後,其在氧化逆境下根部的生長有延長的現象;當AtMTM1基因靜默時,其在氧化逆境下根部的生長有受阻的狀況。明顯的是,在AtMTM1和AtMTM2雙突變轉植株中,AtMSD1的活性顯著下降,伴隨葉綠體中鐵超氧歧化酶(AtFSD1)活性的上升。由上述結果我們可以得知,阿拉伯芥AtMTM1及AtMTM2均可以影響AtMSD1的活性,但二者功能並不完全相同;除了相互影響其表現量之外,也會參Mn及Fe離子的平衡機制,而此機制的調控則是跨越了粒線體與葉綠體不同胞器間的離子調節。這些結果都顯示植物中MnSOD的活化及離子平衡作用相較於酵母菌來得複雜許多。 | zh_TW |
dc.description.abstract | Manganese-containing superoxide dismutase (MnSOD) constitutes the first line of mitochondria defense against ROS, but the mechanism of the MnSOD activation still remains unclear. The MTM1 protein (manganese trafficking factor for mitochondrial SOD2) has been identified in yeast, which is a member of the mitochondrial carrier family (MCF), affecting the yeast mitochondrial MnSOD (SOD2) activity in an uncertain pathway. Two yeast MTM1-like genes, AtMTM1 (At4g27940) and AtMTM2 (At2g46320), were identified by sequence similarity, and both genes also encoded mitochondrial substrate carrier proteins in Arabidopsis (Arabidopsis thaliana). Here, we used genetic and transgenic approaches to study the molecular mechanism underlying the relationship between Arabidopsis MTMs (AtMTMs) and MnSOD (AtMSD1). We confirmed that expressing both AtMTM genes in a yeast MTM1-knockout strain can recover ySOD2 activity, implying AtMTMs functional similarity as with the yeast MTM1. We also found that the protein products of AtMTM1 and AtMTM2 were localized in mitochondria and an interactive relationship existed among AtMTM1, AtMTM2 and AtMSD1. The expression patterns of AtMTM1 and AtMTM2 were significantly different in various organs, and also differ to the response under oxidative stress. Besides, the root length was inhibited in the Atmtm1-RNAi lines but increased in Atmtm2-knockout mutants under oxidative stress. Notably, we observed the MnSOD activity was decreased and associated with an increase of FeSOD activity in the Atmtm1 and Atmtm2 double mutant lines. In summary, both AtMTM1 and AtMTM2 could affect the activity of MnSOD, but the functions between these two MCF proteins were not all the same. In Arabidopsis, they could not only interact to the one another, but participated in a complex mechanism of ion homeostasis. Moreover, the regulation of ionic balance mechanisms may stretch across mitochondria and chloroplast. These results demonstrated that the activation of MnSOD and ion homeostasis in plants were much complicated then in yeast. | en |
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dc.description.tableofcontents | Abstract in Chinese ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• Ⅰ
Abstract in English •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• Ⅱ Abbreviations •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• Ⅳ Introduction •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 1 MnSOD (MSD1) in A. thalian ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 1 Manganese Trafficking Factors •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 2 Manganese Trafficking Factors in A. thaliana ••••••••••••••••••••••••••••••••••••••••••••• 3 Post-translational Activation of MnSOD ••••••••••••••••••••••••••••••••••••••••••••••••••• 4 Mitochondrial Carrier Proteins•••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 6 Yeast MTM1 Homologues in A. thaliana ••••••••••••••••••••••••••••••••••••••••••••••••••• 6 Materials and Methods ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 8 Yeast Strains, Constructs, and Growth Condition ••••••••••••••••••••••••••••••••••••••••• 8 Plants Materials and Growth Condition ••••••••••••••••••••••••••••••••••••••••••••••••••••• 8 Statistical Analysis ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 9 Analyses of the AtMTMs Gene Sequence and Identification of AtMTMs Insertion Lines ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 9 Reverse Transcription PCR (RT-PCR) and Real-time Quantitative PCR ••••••••••••••• 9 Protein Extraction and Quantification ••••••••••••••••••••••••••••••••••••••••••••••••••••• 10 Electrophoresis, SOD Activity Analyses, Immunoblot Analysis, and CBB Staining •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 10 Subcellular Localization Analysis of Transiently Expressed Fusion Proteins •••••••• 10 Protoplast Preparation and PEG-Calcium Transfection ••••••••••••••••••••••••••••••••• 11 Construction of GUS Fusion Vector and β-glucuronidase Analyses ••••••••••••••••••• 11 Bimolecular Bluorescence Complementation (BiFC) Assays •••••••••••••••••••••••••• 12 Gene Construction and Plant Transformation •••••••••••••••••••••••••••••••••••••••••••• 12 Results •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 14 Yeast MTM-like Genes in Arabidopsis ••••••••••••••••••••••••••••••••••••••••••••••••••••• 14 AtMTM2, as AtMTM1, Is Localized to Mitochondria •••••••••••••••••••••••••••••••••• 14 Both of AtMTMs can Recover MnSOD Activity in Yeast mtm1 Mutant ••••••••••••• 15 AtMSD1, AtMTM1, and AtMTM2 can Interact with Each Other ••••••••••••••••••••• 15 Characterization of AtMTM1 and AtMTM2 T-DNA Insertion Lines ••••••••••••••••• 16 Root Growth Inhibition in Atmtm1-RNAi Lines Under Oxidative Stress •••••••••••• 18 Root Length of the Atmtm2-6 Mutant Is Slightly increased Under Oxidative Stress•••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 18 Atmtm1i or Atmtm2-6 Mutant Shows No Effect on MnSOD Activity ••••••••••••••••• 19 AtMTM2 Is Ubiquitous Expression and AtMTM1 Is Majorly Expressed in Roots Under Normal Condition •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 19 GUS Expression Profile of AtMTM2 Is Consistant with the Real-Time PCR Results •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 20 The Expression of AtMTM1 and AtMTM2 Show Differentially in Responses to Oxidative Stress ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 21 Atmtm1 and Atmtm2 Double Mutation Causes MnSOD Activity Decrease and FeSOD Activity Increase •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 22 Overexpression of the AtMTM1 and AtMTM2 Is Not to Affect MnSOD Activity ••• 23 Tables ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 25 Figures ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 27 Discussion •••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 45 Perspectives ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 49 References ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••• 52 | |
dc.language.iso | en | |
dc.title | 阿拉伯芥中MTM-like基因功能探討以及其對於錳超氧歧化酶活化機制的研究 | zh_TW |
dc.title | Functional Study of Yeast MTM-like Genes in MnSOD Activation of Arabidopsis | en |
dc.type | Thesis | |
dc.date.schoolyear | 100-1 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 林秋榮(Chu-Yung Lin),林讚標(Tsan-Piao Lin),鄭石通(Shih-Tong Jeng),葉國楨(Kuo-Chen Yeh) | |
dc.subject.keyword | 阿拉伯芥,超氧歧化酶,錳超氧歧化酶,金屬輔酶,氧化逆境,離子恆定作用, | zh_TW |
dc.subject.keyword | Arabidopsis,superoxide dismutase(SOD),MnSOD,metal cofactor,oxidative stress,ion homeostasis, | en |
dc.relation.page | 60 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2012-02-14 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 植物科學研究所 | zh_TW |
顯示於系所單位: | 植物科學研究所 |
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