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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/9962

Title: UBF蛋白結構與功能分析及魚類UBF基因鑑認
Structural and Functional Analysis of UBF & Fish UBF Gene Identification
Authors: 胡清華
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: RNA聚合?;轉錄因子;;基因分析
RNA polymerase;Transcription factor;Fish;Gene analysis
Date: 1994-02
Issue Date: 2011-06-28T07:18:01Z
Publisher: 行政院國家科學委員會
Abstract: 摘要:本研究工作依原擬計畫分二階段執行,目前已順利完成第一階段之進度,茲將其所獲之初步結果略述如后。 本計畫之第一階段研究目標在於對兩棲類RNA polymerase I之轉錄因子UBF其辨認DNA及蛋白耦合之結構與功能之分析。 結果:(1)順利將兩棲類UBF之主要DNA辨識功能區(DNA binding domain)-HMG box I及蛋白耦合功能區(dimerization domain)轉殖入E. coli表現及純化。(2)初步測試具有良好DNA辨識及附合能力與蛋白耦合能力。(3)已利用遺傳工程方法著手進行各種胺基酸轉換之工作,藉以探測各重要胺基酸之結構功能。 本計畫預期於第二階段完成後,將對UBF之DNA辨識與耦合等之結構機制將有較完整之認識。
Abstract:UBF is an general RNA polymerase I-specific transcription factor which assist other essential factors to assemble stable initiation complex in the promoter of ribosomal genes. We have shown that UBF recognize cross-over DNA structure by its multiple DNA binding domain motifs, named HMG box. In this study, we expressed the major DNA binding motif, HMG box-1, by E. coli overexpression system. We demonstrated that the recombinant peptide bound cross-over DNA. By making series of deletion from both ends, we could define the minimum DNA binding activity within the central 50 residues of this motif. We are making various point-mutations on the conserved amino acid residues and analyzing their DNA binding activities. In addition, we also expressed the N-terminal protein dimerization domain. Coexisting with cluster of basic amino acid residues, this peptide filled in entire double-stranded DNA and formed unique ladders in gel shift assay. We are making series of deletion from C-terminus and internal deletion to define its functional dimerization domain. In addition, we will make various point mutations in the amphipathic region to replace the hydrophobic residues and characterize the function of amphipathic region in protein homodimer formation.
Relation: NSC83-0209-B019-005
URI: http://ntour.ntou.edu.tw/ir/handle/987654321/9962
Appears in Collections:[生命科學暨生物科技學系] 研究計畫

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