跳到主要內容

臺灣博碩士論文加值系統

(34.204.180.223) 您好!臺灣時間:2021/07/31 18:18
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果 :::

詳目顯示

: 
twitterline
研究生:蔡育蓉
研究生(外文):Yu-Jung Tsai
論文名稱:探討仙人掌桿菌內Dps1於氧化性壓力與營養缺乏之調控
論文名稱(外文):Study of Dps1 of Bacillus cereus regulated by oxidative stress and nutrition starvation
指導教授:陳建成陳建成引用關係
指導教授(外文):Chien-Cheng Chen
學位類別:碩士
校院名稱:國立高雄師範大學
系所名稱:生物科技系
學門:生命科學學門
學類:生物科技學類
論文種類:學術論文
論文出版年:2015
畢業學年度:103
語文別:中文
論文頁數:95
中文關鍵詞:仙人掌桿菌DpsClpX
外文關鍵詞:Bacillus cereusDpsClpX
相關次數:
  • 被引用被引用:0
  • 點閱點閱:116
  • 評分評分:
  • 下載下載:25
  • 收藏至我的研究室書目清單書目收藏:0
仙人掌桿菌 (Bacillus cereus) 會編碼三種不同的Dps蛋白來保護細胞,其包含Dps1 (BC2011)、Dps2 (BC5044) 與Dps3 (BC1005)。目前已知Dps2藉由PerR誘導抵抗氧化性壓力,而Dps3藉由σB調控以反應一般的壓力。而對於Dps1的表現目前主要知道於生長階段會被誘導,但其詳細調控機制仍待探討。在先前的研究發現Dps1由PerR調控即使其並非為典型的PerR consensus sequence。本研究經由EMSA與DNase I Footprinting之試驗於in vitro證實dps1 coding region的上游區域具有PerR binding site。相反的,由西方墨點法偵測野生株與互補dps1不含PerR binding site的Δdps1,dps2剔除株,觀察其dps1的表現量,結果並不如前。此外,由β-galactosidase分析dps1的promoter於B. cereus ∆perR表現並沒有任何影響。而後,我們剔除ClpX來觀察ATP-depend的Clp protease在停滯期是否經由降解dps1來調節其表現量。本研究以rich medium與minimal medium做為環境調控,於minimal medium的狀態下,Dps1蛋白會進行表現;而ClpX protease會調控Dps2蛋白表現量,相較於rich medium,Dps1與Dps2於野生株與clpX剔除株之間的表現較難以區別。綜合上述研究顯示PerR與ClpX並沒有參與Dps1調控;而ClpX似乎在特定條件如營養限制下調控Dps2表現。
Three different Dps proteins including Dps1 (BC2011), Dps2 (BC5044) and Dps3 (BC1005) encoded in Bacillus cereus confer cell protection. Dps2 regulated by PerR can be induced against oxidative stress and Dps3 in response to general stress is controlled by σB. However, little is known about the regulation of Dps1 except Dps1 is known to be expressed following the growth stage. In the prior study, we proposed that Dps1 was regulated by PerR despite no typical PerR consensus sequence was found within the promoter of dps1. In this study, we demonstrated a PerR binding site upstream of dps1 coding region via EMSA and DNase I Footprinting in vitro. Inconsistently, Western blotting showed that the expression profile of Dps1 was comparable to the wild-type when dps1 under the control of a truncated promoter with loss of PerR binding site was complemented in B. cereus Δdps1,dps2. Moreover, analysis of β-galactosidase showed deletion of PerR did not affect expression of Dps1. Our data suggest that Dps1 is unlikely governed by PerR in vivo. Additionally, we generated clpX mutant to explore whether the ATP-depend Clp proteases regulate Dps1 through eliminating the degradation of Dps1 during the stationary phase. In consequence, Dps1 was constitutively expressed irrelevant to ClpX, while loss ClpX increased the expression of Dps2 under the minimal nutrition condition. On contrast, indistinguishable expressions of Dps1 and Dps2 in the wild-type and clpX mutant were found in rich medium. In summary, our results showed that PerR and ClpX might not be involved in Dps1 regulation. However, ClpX seems to regulate Dps2 at specific condition for example limited nutrition.


目錄
誌謝 I
摘要 III
Abstract IV
目錄 V
表目錄 VIII
圖目錄 VIII
附錄 IX
壹 、前言與文獻回顧 10
1.1 描述B. cereus的特徵 10
1.2 鐵與蛋白對儲存鐵與解毒作用 12
1.3 Dps蛋白之結構功能與調控機制 14
1.4 PerR蛋白 19
1.5 Clp protease 20
1.6 研究動機 20
貳 、材料方法 22
2.1 實驗菌株與質體來源 22
2.2 引子對設計與製備 22
2.3 染色體DNA抽取 23
2.4 溫度梯度聚合酶鏈連鎖反應與大量製備DNA產物 24
2.5 瓊脂凝膠電泳分析 24
2.6 DNA膠體萃取 25
2.7 DNA內切酶水解反應與接合作用 25
2.8 勝任細胞之熱休克轉型法 (Heat shock Transformation) 26
2.9 勝任細胞制作 (Competent cell) 26
2.10 質體DNA萃取 27
2.11 仙人掌桿菌同源序列質體pMAD-ΔclpX之構築 27
2.12 電穿孔法轉殖仙人掌桿菌 28
2.12.1 B. cereus ATCC14579勝任細胞製作 28
2.12.2 電穿孔 (Electroporation) 29
2.13 以40°C誘導基因互換 29
2.14 t-BOOH Stress 30
2.15 Minimal medium藥品配製 31
2.15.1 種菌 31
2.16 CCCP試驗 31
2.16.1 CCCP反應 32
2.17 以超音波破碎機破菌 32
2.18 蛋白質濃度測定 33
2.19 聚丙烯胺膠體配置 33
2.20 Western blot 34
2.20.1 聚丙烯胺膠體電泳 34
2.20.2 西方墨點法 (Western blot) 34
2.21 β-galatosidase assays 36
2.22 凝膠遷移率變動分析法 (EMSA) 36
2.23 DNase I足跡分析 (DNase I footprinting) 37
參 、結果 39
3.1 PerR蛋白與Dps1之關係 39
3.2 EMSA分析PerR蛋白與Dps1的關聯性 39
3.3 DNase I Footprinting分析 40
3.4 dps1之PerR binding site突變試驗 41
3.5 β-galactosidase分析dps1與dps2 promoter於氧化性壓力下之表現 43
3.6 B. cereus ∆clpX剔除株構築 44
3.7 以西方墨點法於B. cereus ∆clpX偵測Dps之表現量 46
3.8 以t-BOOH對B. cereus WT與∆clpX進行氧化壓力測試 46
3.9 ClpX蛋白酶於不同營養條件下對Dps之影響 47
3.10 以CCCP測定Dps之變化是否與ATP調節有關 49
肆 、討論 50
4.1 推測B. cereus的Dps1具PerR binding site之原因 50
4.2 以EMSA與Footprinting分析PerR與dps1上游基因關係 52
4.3 西方墨點法分析dps1 PerR binding site之作用 52
4.4 Dps1與Dps2抗體干擾 53
4.5 Dps1與Dps2 promoter的表現 54
4.6 推測Dps蛋白由其他因素進行調控 55
4.7 ClpX protease protein的調控之可能性 55
4.8 營養缺乏之試驗探討 56
4.9 Minimal medium與Rich medium之差別 58
4.10 Minimal medium與ATP之關係 59
伍 、結論 60
陸 、參考文獻 61
附錄 95

表目錄
表 1、實驗菌株與質體特性及來源 72
表 2、仙人掌桿菌同源序列質體構築之引子序列表 75
圖目錄

圖 1、pMAD-∆clpX與仙人掌桿菌染色體同源重組機制圖 76
圖 2、由EMSA分析dps1 promoter與PerR的相互作用 77
圖 3、由Footprinting分析dps1 promoter上所推測的perR box 78
圖 4、EMSA與Footprinting 分析的總體示意圖 79
圖 5、以西方墨點法分析Dps1 PerR binding site單點突變於t-BOOH壓力的表現量 80
圖 6、以西方墨點法分析Dps1 PerR binding site單點突變於t-BOOH壓力的表現量 81
圖 7、以西方墨點法分析dps1 promoter region truncated試驗其Dps1於t-BOOH壓力下的表現量 82
圖 8、以西方墨點法分析dps1 promoter region truncated試驗其Dps1於t-BOOH壓力下的表現量 83
圖 9、以西方墨點法分析Dps1於有無t-BOOH壓力下的表現量 84
圖 10、以西方墨點法分析Dps1於有無t-BOOH壓力下的表現量 85
圖 11、以β-galactosidase分析dps1與dps2 promoter轉錄表現量 86
圖 12、於LB Broth培養觀察∆clpX之Dps1生長趨勢 87
圖 13、於LB Broth培養觀察∆clpX之Dps2生長趨勢 88
圖 14、以西方墨點法分析∆clpX於t-BOOH氧化壓力下Dps1與Dps2的表現量 89
圖 15、B. cereus WT與∆clpX於minimal medium之生長趨勢 90
圖 16、B. cereus WT與∆clpX於rich medium之生長趨勢 91
圖 17、以西方墨點法分析∆clpX於不同生長條件下Dps1與Dps2的表現量之差異 92
圖 18、以西方墨點法分析∆clpX於rich medium培養進行CCCP藥劑試驗 93
圖 19、Dps與ClpX調控示意圖 94
附錄
附表 1、SDS配製表 95
Agaisse, H. & D. Lereclus, (1994) Structural and functional analysis of the promoter region involved in full expression of the cryIIIA toxin gene of Bacillus thuringiensis. Molecular microbiology 13: 97-107.
Agata, N., M. Ohta & M. Mori, (1996) Production of an emetic toxin, cereulide, is associated with a specific class of Bacillus cereus. Current microbiology 33: 67-69.
Agata, N., M. Ohta, M. Mori & M. Isobe, (1995) A novel dodecadepsipeptide, cereulide, is an emetic toxin of Bacillus cereus. FEMS microbiology letters 129: 17-19.
Almiron, M., A.J. Link, D. Furlong & R. Kolter, (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes & development 6: 2646-2654.
Anagnostopoulos, C. & J. Spizizen, (1961) Requirements for transformation in Bacillus subtilis. Journal of bacteriology 81: 741.
Antelmann, H., S. Engelmann, R. Schmid, A. Sorokin, A. Lapidus & M. Hecker, (1997) Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigmaB in Bacillus subtilis. Journal of bacteriology 179: 7251-7256.
Arantes, O. & D. Lereclus, (1991) Construction of cloning vectors for Bacillus thuringiensis. Gene 108: 115-119.
Arnaout, M.K., R.F. Tamburro, S.M. Bodner, J.T. Sandlund, G.K. Rivera, C.H. Pui & R.C. Ribeiro, (1999) Bacillus cereus causing fulminant sepsis and hemolysis in two patients with acute leukemia. Journal of pediatric hematology/oncology 21: 431-435.
Arnaud, M., A. Chastanet & M. Débarbouillé, (2004) New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Applied and environmental microbiology 70: 6887-6891.
Arnesen, L.P.S., A. Fagerlund & P.E. Granum, (2008) From soil to gut: Bacillus cereus and its food poisoning toxins. FEMS microbiology reviews 32: 579-606.
Arosio, P., R. Ingrassia & P. Cavadini, (2009) Ferritins: a family of molecules for iron storage, antioxidation and more. Biochimica et biophysica acta 1790: 589-599.
Baichoo, N. & J.D. Helmann, (2002) Recognition of DNA by Fur: a reinterpretation of the Fur box consensus sequence. Journal of bacteriology 184: 5826-5832.
Beecher, D.J., T.W. Olsen, E.B. Somers & A.C. Wong, (2000) Evidence for contribution of tripartite hemolysin BL, phosphatidylcholine-preferring phospholipase C, and collagenase to virulence of Bacillus cereus endophthalmitis. Infection and immunity 68: 5269-5276.
Beecher, D.J., J.L. Schoeni & A. Wong, (1995) Enterotoxic activity of hemolysin BL from Bacillus cereus. Infection and Immunity 63: 4423-4428.
Berthold-Pluta, A., A. Pluta & M. Garbowska, (2015) The effect of selected factors on the survival of Bacillus cereus in the human gastrointestinal tract. Microbial pathogenesis 82: 7-14.
Bhattacharyya, G. & A. Grove, (2007) The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer. The Journal of biological chemistry 282: 11921-11930.
Bozzi, M., G. Mignogna, S. Stefanini, D. Barra, C. Longhi, P. Valenti & E. Chiancone, (1997) A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. The Journal of biological chemistry 272: 3259-3265.
Brenot, A., K.Y. King & M.G. Caparon, (2005) The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Molecular microbiology 55: 221-234.
Bsat, N., L. Chen & J.D. Helmann, (1996) Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. Journal of bacteriology 178: 6579-6586.
Bsat, N., A. Herbig, L. Casillas-Martinez, P. Setlow & J.D. Helmann, (1998) Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Molecular microbiology 29: 189-198.
Calhoun, L.N. & Y.M. Kwon, (2011) Structure, function and regulation of the DNA-binding protein Dps and its role in acid and oxidative stress resistance in Escherichia coli: a review. Journal of applied microbiology 110: 375-386.
Ceci, P., A. Ilari, E. Falvo & E. Chiancone, (2003) The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. The Journal of biological chemistry 278: 20319-20326.
Ceci, P., L. Mangiarotti, C. Rivetti & E. Chiancone, (2007) The neutrophil-activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA. Nucleic acids research 35: 2247-2256.
Ceragioli, M., M. Mols, R. Moezelaar, E. Ghelardi, S. Senesi & T. Abee, (2010) Comparative transcriptomic and phenotypic analysis of the responses of Bacillus cereus to various disinfectant treatments. Appl Environ Microbiol 76: 3352-3360.
Chen, L. & J.D. Helmann, (1995) Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Molecular microbiology 18: 295-300.
Chen, L., L.P. James & J.D. Helmann, (1993) Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions. Journal of bacteriology 175: 5428-5437.
Chen, L., L. Keramati & J.D. Helmann, (1995) Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proceedings of the National Academy of Sciences of the United States of America 92: 8190-8194.
Chiancone, E. & P. Ceci, (2010) The multifaceted capacity of Dps proteins to combat bacterial stress conditions: Detoxification of iron and hydrogen peroxide and DNA binding. Biochimica et biophysica acta 1800: 798-805.
Cooksley, C., P.J. Jenks, A. Green, A. Cockayne, R.P. Logan & K.R. Hardie, (2003) NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. Journal of medical microbiology 52: 461-469.
Cornelissen, C.N. & P.F. Sparling, (1994) Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens. Molecular microbiology 14: 843-850.
Deneer, H.G., V. Healey & I. Boychuk, (1995) Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 141 ( Pt 8): 1985-1992.
Ehling‐Schulz, M., M. Fricker & S. Scherer, (2004) Bacillus cereus, the causative agent of an emetic type of food‐borne illness. Molecular nutrition & food research 48: 479-487.
Fiorini, F., S. Stefanini, P. Valenti, E. Chiancone & D. De Biase, (2008) Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator. Gene 410: 113-121.
Fouet, A., O. Namy & G. Lambert, (2000) Characterization of the operon encoding the alternative sigma(B) factor from Bacillus anthracis and its role in virulence. Journal of bacteriology 182: 5036-5045.
Frees, D., K. Savijoki, P. Varmanen & H. Ingmer, (2007) Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Molecular microbiology 63: 1285-1295.
Fuangthong, M. & J.D. Helmann, (2003) Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis. Journal of bacteriology 185: 6348-6357.
Fuangthong, M., A.F. Herbig, N. Bsat & J.D. Helmann, (2002) Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. Journal of bacteriology 184: 3276-3286.
Gauss, G.H., P. Benas, B. Wiedenheft, M. Young, T. Douglas & C.M. Lawrence, (2006) Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly. Biochemistry 45: 10815-10827.
Gould, G.W., (2000) Preservation: past, present and future. British medical bulletin 56: 84-96.
Grove, A. & S.P. Wilkinson, (2005) Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans. Journal of molecular biology 347: 495-508.
Gupta, S. & D. Chatterji, (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. The Journal of biological chemistry 278: 5235-5241.
Gupta, S., S.B. Pandit, N. Srinivasan & D. Chatterji, (2002) Proteomics analysis of carbon-starved Mycobacterium smegmatis: induction of Dps-like protein. Protein engineering 15: 503-512.
Haikarainen, T. & A.C. Papageorgiou, (2010) Dps-like proteins: structural and functional insights into a versatile protein family. Cellular and molecular life sciences : CMLS 67: 341-351.
Hansen, B.M. & N.B. Hendriksen, (2001) Detection of Enterotoxic Bacillus cereus and Bacillus thuringiensis Strains by PCR Analysis. Applied and Environmental Microbiology 67: 185-189.
Hardy, S.P., T. Lund & P.E. Granum, (2001) CytK toxin of Bacillus cereus forms pores in planar lipid bilayers and is cytotoxic to intestinal epithelia. FEMS microbiology letters 197: 47-51.
Hecker, M., W. Schumann & U. Volker, (1996) Heat-shock and general stress response in Bacillus subtilis. Molecular microbiology 19: 417-428.
Helgason, E., O.A. Økstad, D.A. Caugant, H.A. Johansen, A. Fouet, M. Mock, I. Hegna & A.-B. Kolstø, (2000) Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis—one species on the basis of genetic evidence. Applied and environmental microbiology 66: 2627-2630.
Herbig, A.F. & J.D. Helmann, (2001) Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Molecular microbiology 41: 849-859.
Hilliard, N.J., R.L. Schelonka & K.B. Waites, (2003) Bacillus cereus bacteremia in a preterm neonate. Journal of clinical microbiology 41: 3441-3444.
Horng, Y.-T., K.-C. Chang, Y.-N. Liu, H.-C. Lai & P.-C. Soo, (2010) The RssB/RssA two-component system regulates biosynthesis of the tripyrrole antibiotic, prodigiosin, in Serratia marcescens. International Journal of Medical Microbiology 300: 304-312.
Horsburgh, M.J., M.O. Clements, H. Crossley, E. Ingham & S.J. Foster, (2001) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69: 3744-3754.
Ilari, A., S. Stefanini, E. Chiancone & D. Tsernoglou, (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nature structural biology 7: 38-43.
Imlay, J.A., (2003) Pathways of oxidative damage. Annual review of microbiology 57: 395-418.
Imlay, J.A., (2008) Cellular defenses against superoxide and hydrogen peroxide. Annual review of biochemistry 77: 755-776.
Johnson, W., L. Varner & M. Poch, (1991) Acquisition of iron by Legionella pneumophila: role of iron reductase. Infect Immun 59: 2376-2381.
Kauko, A., S. Haataja, A.T. Pulliainen, J. Finne & A.C. Papageorgiou, (2004) Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation. Journal of molecular biology 338: 547-558.
Kim, S.G., G. Bhattacharyya, A. Grove & Y.H. Lee, (2006) Crystal structure of Dps-1, a functionally distinct Dps protein from Deinococcus radiodurans. Journal of molecular biology 361: 105-114.
King, K.Y., J.A. Horenstein & M.G. Caparon, (2000) Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes. Journal of bacteriology 182: 5290-5299.
Kohanski, M.A., D.J. Dwyer, B. Hayete, C.A. Lawrence & J.J. Collins, (2007) A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130: 797-810.
Kramer, J.M. & R.J. Gilbert, (1989) Bacillus cereus and other Bacillus species. Foodborne bacterial pathogens 19: 21-70.
Lechner, S., R. MAYR, K.P. Francis, B.M. PRÜ, T. KAPLAN, E. WIEßNER-GUNKEL, G.S. STEWART & S. SCHERER, (1998) Bacillus weihenstephanensis sp. nov. is a new psychrotolerant species of the Bacillus cereus group. International Journal of Systematic Bacteriology 48: 1373-1382.
Leskela, S., V.P. Kontinen & M. Sarvas, (1996) Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence. Microbiology 142 ( Pt 1): 71-77.
Lindblom, J., H.B. Schioth, H. Watanobe, T. Suda, J.E. Wikberg & L. Bergstrom, (2000) Downregulation of melanocortin receptors in brain areas involved in food intake and reward mechanisms in obese (OLETF) rats. Brain research 852: 180-185.
Linley, E., S.P. Denyer, G. McDonnell, C. Simons & J.Y. Maillard, (2012) Use of hydrogen peroxide as a biocide: new consideration of its mechanisms of biocidal action. The Journal of antimicrobial chemotherapy 67: 1589-1596.
Liu, X., K. Kim, T. Leighton & E.C. Theil, (2006) Paired Bacillus anthracis Dps (mini-ferritin) have different reactivities with peroxide. The Journal of biological chemistry 281: 27827-27835.
Lomovskaya, O.L., J.P. Kidwell & A. Matin, (1994) Characterization of the sigma 38-dependent expression of a core Escherichia coli starvation gene, pexB. Journal of bacteriology 176: 3928-3935.
Lund, T., M.L. De Buyser & P.E. Granum, (2000) A new cytotoxin from Bacillus cereus that may cause necrotic enteritis. Molecular microbiology 38: 254-261.
Mahler, H., A. Pasi, J.M. Kramer, P. Schulte, A.C. Scoging, W. Bär & S. Krähenbühl, (1997) Fulminant liver failure in association with the emetic toxin of Bacillus cereus. New England Journal of Medicine 336: 1142-1148.
Martinez, A. & R. Kolter, (1997) Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. Journal of bacteriology 179: 5188-5194.
Matin, A., (1991) The molecular basis of carbon-starvation-induced general resistance in Escherichia coli. Molecular microbiology 5: 3-10.
Mihaljevic, R.R., M. Sikic, A. Klancnik, G. Brumini, S.S. Mozina & M. Abram, (2007) Environmental stress factors affecting survival and virulence of Campylobacter jejuni. Microbial pathogenesis 43: 120-125.
Mirończuk, A.M., Á.T. Kovács & O.P. Kuipers, (2008) Induction of natural competence in Bacillus cereus ATCC14579. Microbial biotechnology 1: 226-235.
Mols, M. & T. Abee, (2011) Primary and secondary oxidative stress in Bacillus. Environ Microbiol 13: 1387-1394.
Mols, M., R. van Kranenburg, C.C. van Melis, R. Moezelaar & T. Abee, (2010) Analysis of acid-stressed Bacillus cereus reveals a major oxidative response and inactivation-associated radical formation. Environ Microbiol 12: 873-885.
Morikawa, K., R.L. Ohniwa, J. Kim, A. Maruyama, T. Ohta & K. Takeyasu, (2006) Bacterial nucleoid dynamics: oxidative stress response in Staphylococcus aureus. Genes to cells : devoted to molecular & cellular mechanisms 11: 409-423.
Nair, S. & S.E. Finkel, (2004) Dps protects cells against multiple stresses during stationary phase. Journal of bacteriology 186: 4192-4198.
Nicodeme, M., C. Perrin, P. Hols, P. Bracquart & J.L. Gaillard, (2004) Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus. Current microbiology 48: 51-56.
Olsen, K.N., M.H. Larsen, C.G. Gahan, B. Kallipolitis, X.A. Wolf, R. Rea, C. Hill & H. Ingmer, (2005) The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology 151: 925-933.
Papinutto, E., W.G. Dundon, N. Pitulis, R. Battistutta, C. Montecucco & G. Zanotti, (2002) Structure of two iron-binding proteins from Bacillus anthracis. The Journal of biological chemistry 277: 15093-15098.
Patra, G., A. Fouet, J. Vaissaire, J.-L. Guesdon & M. Mock, (2002) Variation in rRNA operon number as revealed by ribotyping of Bacillus anthracis strains. Research in microbiology 153: 139-148.
Pena, M.M. & G.S. Bullerjahn, (1995) The DpsA protein of Synechococcus sp. Strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families. The Journal of biological chemistry 270: 22478-22482.
Phadtare, S. & M. Inouye, (2004) Genome-wide transcriptional analysis of the cold shock response in wild-type and cold-sensitive, quadruple-csp-deletion strains of Escherichia coli. Journal of bacteriology 186: 7007-7014.
Pirttijärvi, T.S., M.A. Andersson, A.C. Scoging & M.S. Salkinoja-Salonen, (1999) Evaluation of methods for recognising strains of the Bacillus cereus group with food poisoning potential among industrial and environmental contaminants. Systematic and applied microbiology 22: 133-144.
Prüß, B.M., R. Dietrich, B. Nibler, E. Märtlbauer & S. Scherer, (1999) The Hemolytic Enterotoxin HBL Is Broadly Distributed among Species of the Bacillus cereus Group. Applied and Environmental Microbiology 65: 5436-5442.
Priest, F.G. & B. Alexander, (1988) A frequency matrix for probabilistic identification of some bacilli. Journal of general microbiology 134: 3011-3018.
Rea, R., C. Hill & C.G. Gahan, (2005) Listeria monocytogenes PerR mutants display a small-colony phenotype, increased sensitivity to hydrogen peroxide, and significantly reduced murine virulence. Appl Environ Microbiol 71: 8314-8322.
Rowan, N.J., G. Caldow, C.G. Gemmell & I.S. Hunter, (2003) Production of diarrheal enterotoxins and other potential virulence factors by veterinary isolates of Bacillus species associated with nongastrointestinal infections. Applied and environmental microbiology 69: 2372-2376.
Roy, S., R. Saraswathi, S. Gupta, K. Sekar, D. Chatterji & M. Vijayan, (2007) Role of N and C-terminal tails in DNA binding and assembly in Dps: structural studies of Mycobacterium smegmatis Dps deletion mutants. Journal of molecular biology 370: 752-767.
Schryvers, A.B. & I. Stojiljkovic, (1999) Iron acquisition systems in the pathogenic Neisseria. Molecular microbiology 32: 1117-1123.
Shinagawa, K., (1990) Analytical methods for Bacillus cereus and other Bacillus species. International journal of food microbiology 10: 125-141.
Shu, J.C., P.C. Soo, J.C. Chen, S.H. Hsu, L.C. Chen, C.Y. Chen, S.H. Liang, L.M. Buu & C.C. Chen, (2013) Differential regulation and activity against oxidative stress of Dps proteins in Bacillus cereus. International journal of medical microbiology : IJMM 303: 662-673.
Silo-Suh, L.A., B.J. Lethbridge, S.J. Raffel, H. He, J. Clardy & J. Handelsman, (1994) Biological activities of two fungistatic antibiotics produced by Bacillus cereus UW85. Appl Environ Microbiol 60: 2023-2030.
Soo, P.-C., Y.-T. Horng, J.-R. Wei, J.-C. Shu, C.-C. Lu & H.-C. Lai, (2008) Regulation of swarming motility and flhDCSm expression by RssAB signaling in Serratia marcescens. Journal of bacteriology 190: 2496-2504.
Stephani, K., D. Weichart & R. Hengge, (2003) Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Molecular microbiology 49: 1605-1614.
Stillman, T.J., M. Upadhyay, V.A. Norte, S.E. Sedelnikova, M. Carradus, S. Tzokov, P.A. Bullough, C.A. Shearman, M.J. Gasson, C.H. Williams, P.J. Artymiuk & J. Green, (2005) The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding. Molecular microbiology 57: 1101-1112.
Tonello, F., W.G. Dundon, B. Satin, M. Molinari, G. Tognon, G. Grandi, G. Del Giudice, R. Rappuoli & C. Montecucco, (1999) The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. Molecular microbiology 34: 238-246.
van Schaik, W., M.H. Tempelaars, J.A. Wouters, W.M. de Vos & T. Abee, (2004) The alternative sigma factor σB of Bacillus cereus: response to stress and role in heat adaptation. Journal of bacteriology 186: 316-325.
Van Vliet, A.H., M.-L.A. Baillon, C.W. Penn & J.M. Ketley, (1999) Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. Journal of bacteriology 181: 6371-6376.
Wandersman, C. & I. Stojiljkovic, (2000) Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Current opinion in microbiology 3: 215-220.
Wang, S.W., C.Y. Chen, J.T. Tseng, S.H. Liang, S.C. Chen, C. Hsieh, Y.H. Chen & C.C. Chen, (2009) orf4 of the Bacillus cereus sigB gene cluster encodes a general stress-inducible Dps-like bacterioferritin. Journal of bacteriology 191: 4522-4533.
Wolf, S.G., D. Frenkiel, T. Arad, S.E. Finkel, R. Kolter & A. Minsky, (1999) DNA protection by stress-induced biocrystallization. Nature 400: 83-85.
Yamamoto, Y., M. Higuchi, L.B. Poole & Y. Kamio, (2000) Role of the dpr product in oxygen tolerance in Streptococcus mutans. Journal of bacteriology 182: 3740-3747.
Yamamoto, Y., L.B. Poole, R.R. Hantgan & Y. Kamio, (2002) An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro. Journal of bacteriology 184: 2931-2939.
Zhao, G., P. Ceci, A. Ilari, L. Giangiacomo, T.M. Laue, E. Chiancone & N.D. Chasteen, (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. The Journal of biological chemistry 277: 27689-27696.
Zheng, M., F. Åslund & G. Storz, (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1722.
Zheng, W.J., Y.H. Hu & L. Sun, (2011) The two Dps of Edwardsiella tarda are involved in resistance against oxidative stress and host infection. Fish & shellfish immunology 31: 985-992.
Zotta, T., A. Ricciardi, F. Ciocia, R. Rossano & E. Parente, (2008) Diversity of stress responses in dairy thermophilic streptococci. International journal of food microbiology 124: 34-42.
連結至畢業學校之論文網頁點我開啟連結
註: 此連結為研究生畢業學校所提供,不一定有電子全文可供下載,若連結有誤,請點選上方之〝勘誤回報〞功能,我們會盡快修正,謝謝!
QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top
無相關論文
 
1. 張威克(1998)。運動經驗與人生。國民體育季刊,27(4),103-108。
2. 吳靖國(2011):小學師資培育課程中「海洋教育」教學內容之研究。教育資料與研究雙月刊。102,111-140。
3. 高麗娟,‹回首來時路:運動員聲員敘說之詩意結構›。《國民體育季刊》,63.4,(台
4. 楊晴絨,‹編纂成人教育的故事─詢敘研究法之介紹›《成人教育雙月刊》,34,(台北:2006)
5. 胡天玫、劉一民(1993)。運動身體經驗的雙重性–「是」與「有」的反省。體育學報,
6. 劉仿桂(2010):環境教育與海洋教育之檢視與比較。北縣教育期刊,73,26-30。
7. 鄭宗文(2009):淺論海洋教育主要精神及教師實施策略。屏縣教育季刊,38,26-30。
8. 吳靖國(2008):海洋通識課程之內涵:知識取向的探討。通識教育學刊。2,67-84。
9. 方力行(2000)。海洋性格的文化,海洋內涵的教育。研考雙月刊,24(6),37-39。
10. 劉一民,〈運動經驗的現象學考察-透過運動關照生命本體〉《台灣師大體育研究》,3,(台
11. 林美珠,〈敘事研究:從生命故事出發〉《輔導季刊》,36.4,(台北:2000)27-34。
12. 何粵東,‹敘說研究方法論初探›《應用心理研究》,25(台北:2005)。
13. 丁興祥、賴誠斌,‹心理傳記學的開展與應用: 典範與方法›《應用心理研究》, 12(台
14. 楊宇彥,〈女性生涯發展研究之質的取向—敘說研究法〉《測驗與輔導》,163,(台
15. 王人生,<大專籃球聯賽興革與規劃之建言>《大專體育》,45.10(台北,1999):13-16。
 
無相關點閱論文