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    Title: 啤酒酵母菌假設性甲基轉移酶YJR129Cp之體外活性研究
    Other Titles: In vitro study of the activity of YJR129Cp, a putative methyltransferase from saccharomyces cerevisiae
    Authors: 溫淑萍;Wen, Shu-ping
    Contributors: 淡江大學生命科學研究所碩士班
    陳銘凱;Chern, Ming-kai
    Keywords: 啤酒酵母菌;甲基轉移酶;S-腺苷甲硫氨酸;Saccharomyces cerevisiae;methylltransferase;S-adenosyl-L-methionine
    Date: 2007
    Issue Date: 2010-01-11 02:29:37 (UTC+8)
    Abstract: 現今因為生物醫學對模式生物的基因序列研究已具有相當的代表性,使得蛋白質體學的研究價值快速提升,其中又以蛋白質的修飾及轉錄調控兩部分為主要研究指標。蛋白質的甲基化在這兩部份佔了重要的位置,它是一種常見的轉譯後修飾行為,已知有些蛋白質甲基化扮演重要的細胞調控角色,然而大部分的蛋白質甲基化所產生的功能目前還所知有限。近年來,組蛋白的離胺酸甲基化被發現在基因的表現及染色質的重塑上具有決定性的調控作用。雖然如此,但還有許多蛋白質甲基化所需的轉移酶尚未找到。
    啤酒酵母菌(Saccharomyces cerevisiae)的開放讀碼框YJR129C具有甲基轉移酶之特徵序列,且在資料庫中與幽門螺旋菌(Helicobacter pylori)的核糖體蛋白L11甲基轉移酶最為相似;而幽門螺旋菌的L11則與啤酒酵母菌核糖體蛋白L12及粒線體核糖體蛋白L19(MRPL19)具有同源關係。為找出離胺酸甲基化所扮演的功能,以及YJR129Cp之可能的甲基轉移酶活性,因此先測定YJR129Cp是否具有甲基化L12或MRPL19p或MRPL11p之活性。本研究利用His-tag融合純化出所需之YJR129Cp、MRPRL19p及MRPL11p,並以L12、MRPL19p、MRPL11p及ΔYJR129C為基質,以S-腺苷甲硫氨酸(S-adenosyl-L-methionine)為輔基質來測定YJR129Cp之活性。本實驗證實YJR129Cp確實具有甲基轉移酶活性,也證實L12、MRPL19p及MRPL11p不是YJR129Cp的基質。
    With genome sequencing for the model organisms used in biomedical research, there is a rapidly growing appreciation that proteomics, the study of modification to proteins, and transcriptional regulation will likely dominate the research headlines. Protein methylation plays a central role in both of these fields, and it is a post-translation modification which is frequent occurrence. Although in many cases the roles of protein methylation are poorly understood, some have been known for positive to play regulatory roles. Recently, the lysine methylation of histone has been found to play an important role in regulating gene expression and chromatin remodeling. However, many proteins have been long known to be methylated but still miss their methylltransferase partners.
    The ORF YJR129C of Saccharomyces cerevisiae has closest match with the methyltransferase of lysine in ribosomal protein L11 of Helicobacter pylori on database. The ribosomal protein L11 of H. pylori is homologous to yeast ribosomal protein L12 and mitochondrial ribosomal protein MRPL19 of S. cerevisiae. In order to find the role of lysine methylation on L12 and the putative methylltransferase activity of YJR129Cp, we manage to determine whether YJR129Cp is an enzyme that methylates L12 or MRPL19p or MRPL11p. Thus YJR129Cp, MRPL19p and MRPL11p fused with his-tag were purified. The activity is determined by a reaction containing YJR129Cp, protein substrates L12, MRPL19, MRPL11, ΔYJR129C and cosubstrate S-adenosyl-L-methionine.
    Appears in Collections:[Graduate Institue of Life Sciences] Thesis

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