請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/27027
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 吳蕙芬 | |
dc.contributor.author | Chun-Yang Chang | en |
dc.contributor.author | 張鈞暘 | zh_TW |
dc.date.accessioned | 2021-06-12T17:54:06Z | - |
dc.date.available | 2010-02-18 | |
dc.date.copyright | 2008-02-18 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-02-05 | |
dc.identifier.citation | 1. Achebach, S., Q. H. Tran, A. Vlamis-Gardikas, M. Mullner, A. Holmgren, and G. Unden. 2004. Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro. FEBS Lett 565:203-6.
2. Ahn, B. Y., and B. Moss. 1992. Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities. Proc Natl Acad Sci U S A 89:7060-4. 3. Aiba, H. 2007. Mechanism of RNA silencing by Hfq-binding small RNAs. Curr Opin Microbiol 10:134-9. 4. Aldea, M., C. Hernandez-Chico, A. G. de la Campa, S. R. Kushner, and M. Vicente. 1988. Identification, cloning, and expression of bolA, an ftsZ-dependent morphogene of Escherichia coli. J Bacteriol 170:5169-76. 5. Altuvia, S., M. Almiron, G. Huisman, R. Kolter, and G. Storz. 1994. The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol Microbiol 13:265-72. 6. Andrews, S. C., A. K. Robinson, and F. Rodriguez-Quinones. 2003. Bacterial iron homeostasis. FEMS Microbiol Rev 27:215-37. 7. Argaman, L., R. Hershberg, J. Vogel, G. Bejerano, E. G. Wagner, H. Margalit, and S. Altuvia. 2001. Novel small RNA-encoding genes in the intergenic regions of Escherichia coli. Curr Biol 11:941-50. 8. Aristarkhov, A., A. Mikulskis, J. G. Belasco, and E. C. Lin. 1996. Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli. J Bacteriol 178:4327-32. 9. Aslund, F., and J. Beckwith. 1999. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96:751-3. 10. Aslund, F., B. Ehn, A. Miranda-Vizuete, C. Pueyo, and A. Holmgren. 1994. Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. Proc Natl Acad Sci U S A 91:9813-7. 11. Aslund, F., M. Zheng, J. Beckwith, and G. Storz. 1999. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A 96:6161-5. 12. Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2:2006 0008. 13. Bagg, A., and J. B. Neilands. 1987. Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26:5471-7. 14. Balk, J., and S. Lobreaux. 2005. Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci 10:324-31. 15. Bodenmiller, D. M., and S. Spiro. 2006. The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator. J Bacteriol 188:874-81. 16. Carlioz, A., and D. Touati. 1986. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5:623-30. 17. Coy, M., and J. B. Neilands. 1991. Structural dynamics and functional domains of the fur protein. Biochemistry 30:8201-10. 18. Cunningham, L., M. J. Gruer, and J. R. Guest. 1997. Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli. Microbiology 143 ( Pt 12):3795-805. 19. Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97:6640-5. 20. Dubrac, S., and D. Touati. 2000. Fur positive regulation of iron superoxide dismutase in Escherichia coli: functional analysis of the sodB promoter. J Bacteriol 182:3802-8. 21. Dukan, S., A. Farewell, M. Ballesteros, F. Taddei, M. Radman, and T. Nystrom. 2000. Protein oxidation in response to increased transcriptional or translational errors. Proc Natl Acad Sci U S A 97:5746-9. 22. Dukan, S., and T. Nystrom. 1998. Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev 12:3431-41. 23. Ebina, Y., Y. Takahara, F. Kishi, A. Nakazawa, and R. Brent. 1983. LexA protein is a repressor of the colicin E1 gene. J Biol Chem 258:13258-61. 24. Escolar, L., J. Perez-Martin, and V. de Lorenzo. 1998. Coordinated repression in vitro of the divergent fepA-fes promoters of Escherichia coli by the iron uptake regulation (Fur) protein. J Bacteriol 180:2579-82. 25. Escolar, L., J. Perez-Martin, and V. de Lorenzo. 1999. Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181:6223-9. 26. Fernandes, A. P., M. Fladvad, C. Berndt, C. Andresen, C. H. Lillig, P. Neubauer, M. Sunnerhagen, A. Holmgren, and A. Vlamis-Gardikas. 2005. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. J Biol Chem 280:24544-52. 27. Fernandes, A. P., and A. Holmgren. 2004. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid Redox Signal 6:63-74. 28. Fladvad, M., M. Bellanda, A. P. Fernandes, S. Mammi, A. Vlamis-Gardikas, A. Holmgren, and M. Sunnerhagen. 2005. Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli. J Biol Chem 280:24553-61. 29. Flint, D. H., J. F. Tuminello, and M. H. Emptage. 1993. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 268:22369-76. 30. Freire, P., H. L. Vieira, A. R. Furtado, M. A. de Pedro, and C. M. Arraiano. 2006. Effect of the morphogene bolA on the permeability of the Escherichia coli outer membrane. FEMS Microbiol Lett 260:106-11. 31. Gan, Z. R., M. A. Polokoff, J. W. Jacobs, and M. K. Sardana. 1990. Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Biochem Biophys Res Commun 168:944-51. 32. Geissmann, T. A., and D. Touati. 2004. Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator. EMBO J 23:396-405. 33. Gerdes, S. Y., M. D. Scholle, J. W. Campbell, G. Balazsi, E. Ravasz, M. D. Daugherty, A. L. Somera, N. C. Kyrpides, I. Anderson, M. S. Gelfand, A. Bhattacharya, V. Kapatral, M. D'Souza, M. V. Baev, Y. Grechkin, F. Mseeh, M. Y. Fonstein, R. Overbeek, A. L. Barabasi, Z. N. Oltvai, and A. L. Osterman. 2003. Experimental determination and system level analysis of essential genes in Escherichia coli MG1655. J Bacteriol 185:5673-84. 34. Gimeno, R. E., P. Espenshade, and C. A. Kaiser. 1995. SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. J Cell Biol 131:325-38. 35. Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177:4121-30. 36. Gyuris, J., E. Golemis, H. Chertkov, and R. Brent. 1993. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75:791-803. 37. Hantke, K. 2001. Iron and metal regulation in bacteria. Curr Opin Microbiol 4:172-7. 38. Hantke, K. 1981. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol Gen Genet 182:288-92. 39. Herrero, E., and M. A. de la Torre-Ruiz. 2007. Monothiol glutaredoxins: a common domain for multiple functions. Cell Mol Life Sci 64:1518-30. 40. Holmgren, A. 1979. Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. J Biol Chem 254:3672-8. 41. Holmgren, A. 1979. Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli. J Biol Chem 254:3664-71. 42. Holmgren, A. 1976. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci U S A 73:2275-9. 43. Holmgren, A., B. O. Soderberg, H. Eklund, and C. I. Branden. 1975. Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Proc Natl Acad Sci U S A 72:2305-9. 44. Huynen, M. A., C. A. Spronk, T. Gabaldon, and B. Snel. 2005. Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin. FEBS Lett 579:591-6. 45. Ilari, A., P. Ceci, D. Ferrari, G. L. Rossi, and E. Chiancone. 2002. Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J Biol Chem 277:37619-23. 46. Jaurin, B., T. Grundstrom, and S. Normark. 1982. Sequence elements determining ampC promoter strength in E. coli. EMBO J 1:875-81. 47. Jervis, A. J., and J. Green. 2007. In vivo demonstration of FNR dimers in response to lower O2 availability. J Bacteriol 189:2930-2. 48. Kasai, T., M. Inoue, S. Koshiba, T. Yabuki, M. Aoki, E. Nunokawa, E. Seki, T. Matsuda, N. Matsuda, Y. Tomo, M. Shirouzu, T. Terada, N. Obayashi, H. Hamana, N. Shinya, A. Tatsuguchi, S. Yasuda, M. Yoshida, H. Hirota, Y. Matsuo, K. Tani, H. Suzuki, T. Arakawa, P. Carninci, J. Kawai, Y. Hayashizaki, T. Kigawa, and S. Yokoyama. 2004. Solution structure of a BolA-like protein from Mus musculus. Protein Sci 13:545-8. 49. Keyer, K., and J. A. Imlay. 1997. Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite. J Biol Chem 272:27652-9. 50. Keyer, K., and J. A. Imlay. 1996. Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci U S A 93:13635-40. 51. Kiley, P. J., and H. Beinert. 1998. Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. FEMS Microbiol Rev 22:341-52. 52. Kiley, P. J., and H. Beinert. 2003. The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol 6:181-5. 53. Kim, S. O., K. Merchant, R. Nudelman, W. F. Beyer, Jr., T. Keng, J. DeAngelo, A. Hausladen, and J. S. Stamler. 2002. OxyR: a molecular code for redox-related signaling. Cell 109:383-96. 54. Lambden, P. R., and J. R. Guest. 1976. Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor. J Gen Microbiol 97:145-60. 55. Luikenhuis, S., G. Perrone, I. W. Dawes, and C. M. Grant. 1998. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell 9:1081-91. 56. Ma, J., and M. Ptashne. 1987. A new class of yeast transcriptional activators. Cell 51:113-9. 57. Masse, E., F. E. Escorcia, and S. Gottesman. 2003. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev 17:2374-83. 58. Masse, E., and S. Gottesman. 2002. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci. USA 99:4620-5. 59. Masse, E., H. Salvail, G. Desnoyers, and M. Arguin. 2007. Small RNAs controlling iron metabolism. Curr Opin Microbiol 10:140-5. 60. Masse, E., C. K. Vanderpool, and S. Gottesman. 2005. Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187:6962-71. 61. McCord, J. M., B. B. Keele, Jr., and I. Fridovich. 1971. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci U S A 68:1024-7. 62. Membrillo-Hernandez, J., and E. C. Lin. 1999. Regulation of expression of the adhE gene, encoding ethanol oxidoreductase in Escherichia coli: transcription from a downstream promoter and regulation by fnr and RpoS. J Bacteriol 181:7571-9. 63. Mesecke, N., S. Mittler, E. Eckers, J. M. Herrmann, and M. Deponte. 2008. Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry. 64. Mettert, E. L., and P. J. Kiley. 2007. Contributions of [4Fe-4S]-FNR and integration host factor to fnr transcriptional regulation. J Bacteriol 189:3036-43. 65. Molina-Navarro, M. M., C. Casas, L. Piedrafita, G. Belli, and E. Herrero. 2006. Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria. FEBS Lett 580:2273-80. 66. Outten, F. W. 2007. Iron-sulfur clusters as oxygen-responsive molecular switches. Nat Chem Biol 3:206-7. 67. Paniker, N. V., S. K. Srivastava, and E. Beutler. 1970. Glutathione metabolism of the red cells. Effect of glutathione reductase deficiency on the stimulation of hexose monophosphate shunt under oxidative stress. Biochim Biophys Acta 215:456-60. 68. Potamitou, A., A. Holmgren, and A. Vlamis-Gardikas. 2002. Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function. J Biol Chem 277:18561-7. 69. Rahlfs, S., M. Fischer, and K. Becker. 2001. Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain. J Biol Chem 276:37133-40. 70. Rodriguez-Manzaneque, M. T., J. Ros, E. Cabiscol, A. Sorribas, and E. Herrero. 1999. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19:8180-90. 71. Rodriguez-Manzaneque, M. T., J. Tamarit, G. Belli, J. Ros, and E. Herrero. 2002. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13:1109-21. 72. Rouhier, N., E. Gelhaye, P. E. Sautiere, and J. P. Jacquot. 2002. Enhancement of poplar glutaredoxin expression by optimization of the cDNA sequence. Protein Expr Purif 24:234-41. 73. Russel, M., and P. Model. 1988. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263:9015-9019. 74. Santos, J. M., P. Freire, M. Vicente, and C. M. Arraiano. 1999. The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth. Mol Microbiol 32:789-98. 75. Santos, J. M., M. Lobo, A. P. Matos, M. A. De Pedro, and C. M. Arraiano. 2002. The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli. Mol Microbiol 45:1729-40. 76. Schaible, U. E., and S. H. Kaufmann. 2004. Iron and microbial infection. Nat Rev Microbiol 2:946-53. 77. Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53:85-96. 78. Tamarit, J., G. Belli, E. Cabiscol, E. Herrero, and J. Ros. 2003. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278:25745-51. 79. Tsang, M. L. 1981. Assimilatory sulfate reduction in Escherichia coli: identification of the alternate cofactor for adenosine 3'-phosphate 5'-phosphosulfate reductase as glutaredoxin. J Bacteriol 146:1059-66. 80. Vecerek, B., I. Moll, and U. Blasi. 2007. Control of Fur synthesis by the non-coding RNA RyhB and iron-responsive decoding. Embo J 26:965-75. 81. Vieira, H. L., P. Freire, and C. M. Arraiano. 2004. Effect of Escherichia coli morphogene bolA on biofilms. Appl Environ Microbiol 70:5682-4. 82. Vlamis-Gardikas, A., F. Aslund, G. Spyrou, T. Bergman, and A. Holmgren. 1997. Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli. J Biol Chem 272:11236-43. 83. Vlamis-Gardikas, A., and A. Holmgren. 2002. Thioredoxin and glutaredoxin isoforms. Methods Enzymol 347:286-96. 84. Wassarman, K. M., F. Repoila, C. Rosenow, G. Storz, and S. Gottesman. 2001. Identification of novel small RNAs using comparative genomics and microarrays. Genes Dev 15:1637-51. 85. Weber, H., T. Polen, J. Heuveling, V. F. Wendisch, and R. Hengge. 2005. Genome-wide analysis of the general stress response network in Escherichia coli: sigmaS-dependent genes, promoters, and sigma factor selectivity. J Bacteriol 187:1591-603. 86. Winterbourn, C. C., and D. Metodiewa. 1999. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 27:322-8. 87. Xu, X. M., and S. G. Moller. 2006. AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis. EMBO J 25:900-9. 88. Yang, Y. F., and W. W. Wells. 1991. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J Biol Chem 266:12759-65. 89. Zheng, M., F. Aslund, and G. Storz. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279:1718-21. 90. 陳圭芃. 2007. 大腸桿菌中 Grx4 蛋白質之研究. 臺灣大學農業化學研究所. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/27027 | - |
dc.description.abstract | 本研究探討大腸桿菌之 grxD 基因在菌體內所受到的調控。藉由不同長度的 grxD 基因上游未轉譯區,與 lacZ 基因進行 operon 及 protein fusion。首先,發現 grxD-lacZ 融合基因於對數期的表現量逐漸增加,並於靜止期前達到最高量,繼而稍降維持平穩表現。將預測之啟動子 P1grxD 的 -35 位置及 P2grxD 的 -10 處突變後,可發現此融合基因的表現量均會降低,故推測 grxD 基因表現受到一個以上的啟動子調控。而上游啟動子 P1grxD 主導對數期表現量的增加,下游啟動子 P2grxD 則維持基因的基本表現。
厭氧狀態時,此融合基因表現量下降,且兩個啟動子均受到抑制。但將保守區域 UCR 刪除後,其於厭氧狀態時的表現量提升;又在厭氧狀態下, fnr- 缺失突變株的表現量不會受到抑制。故推測 grxD 的基因表現於厭氧狀態下,受到調控因子 FNR 直接的抑制,且上游序列包含了一個以上的 FNR cis-binding site 。 本研究於 fur- 、 ryhB- 及此二基因的雙重缺失的情況下,發現 grxD-lacZ 融合基因的表現固然受到 small RNA RyhB 的抑制,但轉錄因子 Fur 仍具有正向調控的作用,甚至是在鐵缺失的情況下。則當刪除 UCR 區域後,不論是於LB 培養基或鐵缺失狀態下,RyhB 均不會影響融合基因的表現量,所以此段 UCR 區域有可能為 RyhB 的 binding site。 除此之外,為了瞭解 Grx4 扮演的角色,我們使用酵母菌雙雜交系統測試了可能有交互作用產生的對象。於細胞體內 (in vivo) 我們證實了 Grx4 與 Grx1 及 TrxB 可能存在的交互作用。此外還發現 Grx4 自己本身,以及與 BolA 之間有很強的交互作用現象。 | zh_TW |
dc.description.abstract | This study was investigated the regulation of grxD gene expression in Escherichia coli. Based on different lengths of promoter fragment in grxD-lacZ operon and protein fusion, we have found that the gene expression was increased upon entry into stationary phase, and the expression of grxD was enhanced by two promoters P1grxD and P2grxD. While either promoter mutated at the location of -35 (P1grxD) and -10 (P2grxD) respectively, the promoter activity was decreased. In log phase, the grxD was more activated with P1grxD promoter than that with P2grxD.
Under anaerobic condition, the grxD-lacZ gene expression is reduced with both promoters P1grxD and P2grxD. However, it is up-regulated with the one carrying a deletion of unknown conserved region (UCR). In fnr- strain, the expression of grxD-lacZ gene is increased and we suggest that the grxD gene expression is directly repressed by FNR. These findings implied that more than one FNR cis-acting sites are present in the promoter region of grxD. In fur-, ryhB- or double mutant, we found that the grxD-lacZ gene expression is reduced by RyhB, but Fur still up-regulates the expression even upon iron depletion. When deleted the UCR region, RyhB do not affect the expression level even under iron depletion or LB condtion. We suggest that the UCR region is a RyhB binding site. Furthermore, we use yeast two-hybrid method to reveal the Grx4 function in vivo. We confirmed that Grx4 interact with Grx1 and TrxB in vivo, and also found Grx4 interact strongly with itself and BolA, and slightly interact with Grx2 and TrxA. | en |
dc.description.provenance | Made available in DSpace on 2021-06-12T17:54:06Z (GMT). No. of bitstreams: 1 ntu-97-R94623023-1.pdf: 4788515 bytes, checksum: c794c339f5a2e3225a93d98bcbe3b661 (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | 口試委員會審定書 i
誌謝 ii 中文摘要 iv Abstract v 圖目錄 x 附圖目錄 xi 第一章、前人研究 1 1.1 氧化壓力 (Oxidative Stress) 1 1.2 氧化還原調控 (Redox regulation) 2 1.3 Glutaredoxin系統 3 1.4 Glutaredoxin 之調控 6 1.5 Grx4 簡介 7 1.6 E. coli 中鐵之調控 8 1.7 E. coli 呼吸路徑之調控因子 – FNR 10 1.8 E. coli Grx4可能的交互作用蛋白質 – BolA 11 1.9 研究動機與目的 11 第二章、材料與方法 12 2.1 一般研究材料 12 2.2 一般實驗方法 14 2.3 選殖基因表現系統之建立 19 2.4 噬菌體一般實驗方法 22 2.5 建構 fur- 、 ryhB- 突變株 27 2.6 B-galactosidase 活性分析 29 2.7 快速增幅 cDNA 末端 (rapid amplification of cDNA ends, RACE) 31 第三章、結果 32 3.1 分析 grxD 上游的 promoter 區域及 cis-element 位置 32 3.2 分析 grxD 的基因表現圖譜 (gene expression profile) 34 3.3 grxD 受到FNR轉錄因子的調控 35 3.4 grxD 受到Fur轉錄因子及sRNA RyhB的共同調控 36 3.5 Grx4 的蛋白之交互作用 38 第四章、討論 39 4.1 grxD promoter 之位置 39 4.2 grxD 具有一個以上 promoter 之意義 40 4.3 grxD 於厭氧情形下受抑制的意義 40 4.4 grxD 為何受到 Fur 及 RyhB 共同調控 41 4.5 Grx4 的蛋白質交互作用 43 第五章、參考文獻 44 | |
dc.language.iso | zh-TW | |
dc.title | 大腸桿菌grxD基因表現之調控 | zh_TW |
dc.title | Regulation of grxD gene expression in Escherichia coli | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-1 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 張傳雄,洪俊雄,洪傳揚,徐駿森 | |
dc.subject.keyword | 大腸桿菌,glutaredoxin,grxD,Grx4,FNR,Fur,RyhB, | zh_TW |
dc.subject.keyword | eshcerichia coli,glutaredoxin,grxD,Grx4,FNR,Fur,RyhB, | en |
dc.relation.page | 71 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2008-02-05 | |
dc.contributor.author-college | 生物資源暨農學院 | zh_TW |
dc.contributor.author-dept | 農業化學研究所 | zh_TW |
顯示於系所單位: | 農業化學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-97-1.pdf 目前未授權公開取用 | 4.68 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。