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dc.contributor.authorYeh, Chun-Linen_US
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dc.description.abstractS-adenosylmethionine (SAM)依賴型甲基轉移反應會釋出反應代謝產物S-adenosylhomocysteine (SAH),SAH也做為此類甲基轉移酶的競爭抑制物,而SAH水解酶(SAHH)則藉由分解SAH產生adenosine和homocysteine來維持甲基化反應的進行。嗜鹽甲烷太古生物Methanohalophilus portucalensis FDF1T可將glycine經由三次SAM依賴型甲基化反應生成並累積甜菜鹼作為滲透壓保護物質,因此細胞內應具有高效率的SAH水解活性以利於相容質甜菜鹼的持續生合成。以M. portucalensis FDF1T細胞粗萃取液測試SAH水解反應證實其胞內具有SAH水解活性。經由M. portucalensis FDF1T metagenomic sequence資料與比較基因體分析胺基酸發現Methanohalophilus有兩套不同型的sahh基因,分別位於glycine betaine生合成基因組的上下游,且由序列分析得知催化活性相關的胺基酸和功能區塊與其他物種的SAH水解酶有高度的相似性,推測兩套SAHH皆具有水解SAH的能力。序列比對與結構預測分析發現MpSAHH1具有多數真核生物與細菌SAHH特有的insertion sequence與C-terminal domain,MpSAHH2則與太古生物SAHH同樣缺少了這些序列。進一步演化歸群分析將MpSAHH1與阿拉伯芥和細菌SAHH歸群在一起,MpSAHH2則和其它甲烷太古生物的SAHH歸群在一起,顯示MpSAHH1可能藉由水平傳播的方式獲自其他物種。將已獲得全長的Mpsahh1基因構築在表現載體pET28a+,以E. coli strain BL21 (DE3)RIL大量表現蛋白並以鎳離子親合性層析純化蛋白並偵測活性,結果無法測得SAH水解活性。由於SAHH需形成四聚體結構才具有功能,因此需先獲得四聚體的MpSAHH1再分析SAH水解活性。本篇研究的結果顯示嗜鹽甲烷太古生物M. portucalensis FDF1T具有兩套SAHH蛋白參與胞內甲基化反應。zh_TW
dc.description.abstractS-adenosylhomocysteine hydrolase (SAHH) catalyzes the hydrolysis of SAH, which is an inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferase, to form adenosine and L-homocysteine. The halophilic methanogen Methanohalophilus portucalensis FDF1T could procee de novo synthesis of glycine betaine as osmolyte via three steps SAM-dependent methylation. This infers that an efficient regulation of SAHH must exist in this organism in order to accumulate and maintain the glycine betaine level under hypersaline environment. SAH hydrolytic activity was detected in the crude extract of M. portucalensis FDF1T. Metagenomic and comparative genomics analysis of genus Methanohalophilus revealed there are two sahh genes located up and down stream of glycine betaine synthesizing gene cluster, respectively. Amino acid sequence analysis and homology modeling structure of these two MpSAHHs exhibit conserved adenosine binding sites and cofactor NAD+ binding motifs with other species, suggesting both possess SAH hydrolyzed activities. Interestingly, sequence alignment and putative structure revealed MpSAHH1 displayed an insertion sequence and C-terminal domain which were conserved among most of eukaryotic and bacterial SAHHs, while MpSAHH2, as archaeal SAHHs, do not have insertion sequence and C-terminal domain. Phylogenetic analysis revealed MpSAHH1 was clustered with SAHHs from Arabidopsis thaliana and bacteria, and MpSAHH2 was clustered with SAHHs from methanogen. MpSAHH1 were cloned and expressed heterologously in E. coli strain BL21 (DE3) RIL, and SAH hydrolytic activity was tested with negative result. SAH hydrolysis activity required tetramer SAHH has been discussed. Oligomerization of MpSAHH1 may need for further activity assay. This study demonstrated that halophilic methanogen M. portucalensis FDF1T posses two SAHH from different origins for SAH hydrolysis.en_US
dc.description.tableofcontents中文摘要 i 英文摘要 ii 目次 iii 表目次 v 圖目次 vi 壹、前言 1 貳、前人研究 2 一、SAHH之催化機制與蛋白結構 3 二、太古生物SAHH蛋白 4 三、甲烷太古生物滲透壓之適應與調節 5 參、材料與方法 8 一、菌種與質體 8 二、高鹽甲烷太古生物之培養基製備、培養與菌種保存 8 (一) 除氧操作系統 (Hungate station) 8 (二) 厭氧培養基製備 8 (三) 還原劑與碳源製備 9 (四) 厭氧接菌培養 9 三、大腸桿菌培養基製備、培養與菌種保存 9 (一) 培養基製備 9 (二) 大腸桿菌的培養 10 (三) 大腸桿菌菌體長期保存 10 四、甲烷太古生物DNA萃取與定量 10 五、核酸電泳分析 11 六、質體抽取與純化 11 (一) 小量質體DNA純化 11 (二) 大量純化質體DNA (Midipreparation) 12 七、聚合酶連鎖反應(PCR) 12 八、DNA片段回收與純化 13 九、DNA黏合反應 (ligation) 13 十、勝任細胞之製備與轉型作用 14 (一)製備勝任細胞 14 (二) 轉型作用 14 十一、南方雜合分析 14 (一) 探針製備(DIG-DNA labeling) 15 (二) M. portucalensis染色體DNA的電泳與轉漬 15 (三) 雜合反應 16 (四) 轉漬尼龍膜洗滌 16 (五) 免疫偵測與呈色反應 16 十二、菌落雜合分析 17 十三、核酸定序樣品製備 17 十四、蛋白表現載體與表現系統之構築 17 十五、全細胞蛋白樣品之製備 18 十六、蛋白質電泳分析與膠片染色 18 十七、西方墨點分析 19 (一)蛋白樣品之電轉漬 19 (二)免疫偵測與呈色反應 20 十八、大量表現重組蛋白與純化 20 十九、甲烷太古生物細胞粗萃取液製備 21 二十、SAHH蛋白水解SAH能力測試 21 二十一、引子設計、核酸序列、胺基酸序列、演化樹與蛋白結構分析 22 肆、結果與討論 23 一、SAHH基因之選殖、胺基酸序列分析與結構預測 23 二、異源表現MpSAHH及純化重組蛋白 26 三、SAHH水解活性測試 27 伍、結論與展望 30 陸、圖與表 31 柒、參考文獻 49 捌、附錄 54 Appendix 1. Mpsahh1 deposited in NCBI Nucleotidedatabase 55 Appendix 2. Mpsahh2 deposited in NCBI Nucleotidedatabase 57zh_TW
dc.subjectS-adenosylhomocysteine hydrolaseen_US
dc.subjectS-adenosylhomocysteine metabolismen_US
dc.titleGene and putative protein structure of S-adenosylhomocysteine hydrolase from Methanohalophilus portucalensis FDF1Ten_US
dc.typeThesis and Dissertationzh_TW
item.openairetypeThesis and Dissertation-
item.fulltextno fulltext-
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