Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/22794
標題: 極端高鹽太古生物聚羥基烷酯生合成基因群組的選殖與特性分析
Identification and Analysis of Polyhydroxyalkanoate Biosynthesis Gene Clusters in the Extreme Halophilic Archaeon Haloterrigena sp. H13
作者: 林志鍵
Lin, Chih-Chien
關鍵字: Polyhydroxyalkanoate
極端高鹽太古生物
Haloterrigena
聚羥基烷酯
出版社: 生命科學系所
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摘要: 許多細菌及少數太古生物生長於營養不平衡的狀態下會將胞內多餘的碳源以聚羥基烷酯(Polyhydroxyalkanoate, PHA)的型式於細胞內累積。PHA具有好的生物相容性與生物降解性,所以在醫學與工業上的應用性。極端高鹽太古生物Haloterrigena sp. H13於低磷高糖誘導下能大量累積極端高鹽太古生物型聚酯顆粒 (hPHA),其單體組成為-[-O-CH(C≡CH)-CH(C2H5)-CHO-]n-,此新型的hPHA具有特殊的不飽和乙炔基(C≡C)。經細胞毒性與貼附性測試,發現hPHA為無毒性,相容性高,細胞貼附性強,顯示hPHA是高潛力的生醫材料。利用已知Haloarcula sp. HLR2 PHA合成酶的基因序列,phaCHLR2當作探針以南方墨漬法偵測Haloterrigena sp. H13中的PHA合成酶基因,從基因體中篩選出一限制酶酵素NotI切割的片段,全長為4599 bp,將序列與基因庫資料分析推測功能與命名,基因組成為maoC、phaR、phaT、phaD、phaC 和phaB。MaoC為enoyl-CoA hydratase,PhaBH13 為NADP-depenent acetoacetyl-CoA reductase,兩者皆是PHA生合成的上游途徑蛋白。PhaRH13 為AbrB-like蛋白質,為轉錄調控蛋白質。PhaCH13為PHA 合成酶,經由序列比對結果,與細菌的第三型PHA 合成酶相似度較高,phaCH13上游為phaDH13,與phaCH13有4 bp的重疊,且只在phaDH13上游有發現推測為啟動子的區域。而第三型或第四型的PHA 合成酶是需要由phaEC或phaRC基因組成分別encode 出的酵素為hetero-subunits PHA 合成酶,所以初步判斷PhaDH13是扮演PhaE或PhaR角色。分析PhaC H13胺基酸序列發現具有PHA合成酶進行聚合反應須具備的胺基酸殘基(Cys-151)-(Asp-306)-(His-335)所組成的活化中心。以北方墨漬法分析發現,phaC與phaD是共轉錄表現。而phaR與phaT也是共轉錄表現。比較營養豐富或不平衡(低磷高醣)的環境下,這些基因的轉錄量,配合PHA合成酶活性測試,分析發現在營養豐富或不平衡的環境下,phaDC的轉錄都會持續表現,轉錄量差異不大,可是在營養不平衡的環境,測試PHA合成酶的活性,比較營養豐富的環境下,PHA合成酶活性卻會大大的提升3倍。而maoC、phaRT和phaB在營養不平衡環境基因轉錄量均會提升0.5~2倍。結果顯示在Haloterrigena sp. H13 PHA生合成受基因轉錄與蛋白質活性的調控,亦可能受PHA合成酶受質的影響。利用大腸桿菌異源表現出PhaDCH13蛋白質與純化,利用3-Hydroxybutyryl-CoA為受質,進行PhaDCH13PHA合成酶特性分析,結果發現只有PhaD H13和PhaC H13同時存在才有活性,PhaDC H13比活性約為5 U/mg。不同溫度測試,PhaDCH13在45℃為最適反應溫度,在熱穩定測試,發現PhaDCH13經過75℃處理5分鐘,依然保有50%的酵素活性。不同離子濃度測試,發現PhaDCH13在1~4M的鉀離子或鈉離子存在下,都有保有活性,在4 M的鉀離子濃度下,有最高的酵素活性。在高鹽環境下經過長時間(三週)的保存,PhaDCH13仍保有90%的活性。綜合上述結果顯示自Haloterrigena sp. H13的PHA生合成酶具有耐高鹽蛋白質的特性,可適應高離子濃度等低水活性的環境,且對熱也有良好的穩定性,適合工業與胞外生產應用,所以對將來在PHA生產與開發上有很好的應用性。
Polyhydroxyalkanoates (PHAs) are a class of biodegradable polyesters of (R)-hydroxyalkanoates. These biopolymers are accumulated by a wide variety of bacteria and haloarchaea when the carbon source is available in excess but other nutrients are growth limiting. PHAs can be used as biodegradable thermoplastics for a wide range of industrial and medical applications. The extremely halophilic Haloterrigena sp. H13 is capable of accumulating large amounts of hPHA under conditions of nitrogen limitation and abundant carbon source. The monomer of hPHA as -[-O-CH(C≡CH)-CH(C2H5)-CHO-]n- is a novel PHA with C≡C bonding. In this study, Southern blot was performed and a 4.6-kb NotI restriction fragment contained PHA biosynthetic gene cluster was cloned from genomic DNA of Haloterrigena sp. H13. This PHA biosynthetic gene cluster included six open reading frames encoding enoyl-CoA hydratase (MaoCH13), AbrB protein (PhaRH13), transducer protein (PhaTH13), polyhydroxyalkanoate synthase subunit (PhaDH13), polyhydroxyalkanoate synthase (PhaCH13), NADPH-dependent acetoacetyl coenzyme A reductase (PhaBH13) and two putative promoter regions. PhaC H13 and PhaD H13 were composed of 538 and 182 amino acid residues respectively and showed low amino acid identity with other class III type PHA synthases. There were 4 bp overlapping of phaDH13 and phaCH13 and a putative promoter regions located upstream of phaDH13. Result of Northern blot hybridization also demonstrated that phaCH13 and phaDH13 were co-transcribed. The amino acids of (Cys-151)-(Asp-306)-(His-335) were proposed as the catalytic nucleoplile for PHA polymerization at PhaCH13. The PHA biosynthetic gene cluster we identified from Haloterrigena sp. H13 should broaden our knowledge in archaeal PHA biosynthesis.
URI: http://hdl.handle.net/11455/22794
其他識別: U0005-2907200817554800
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