淡江大學機構典藏:Item 987654321/51816
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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/51816


    Title: 啤酒酵母菌JHD1p去甲基酶之選殖及專一性探討
    Other Titles: Cloning and specificity of saccharomyces cerevisiae JHD1p demethylase.
    Authors: 莊登發;Chuang, Teng-fa
    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;去甲基酶;JHD1p;Saccharomyces cerevisiae;demethylase;JHD1p
    Date: 2010
    Issue Date: 2010-09-23 16:10:25 (UTC+8)
    Abstract: 染色體的基本組成單元是由H2A、H2B、H3、H4各二分子所組成

    的核心組蛋白纏繞著146 鹼基對DNA而成。核心組蛋白的共價修飾藉

    由貢獻額外的遺傳訊息來調節基因組的功能。現階段，組蛋白常見

    的共價修飾之一是甲基化。近年來，確定甲基化是具有可逆性的，

    因此發現了另一種機動性組蛋白共價修飾，即去甲基化。所以，組

    蛋白的共價修飾在基因表現的遺傳控制上扮演一個極關鍵的角色。

    本研究探討啤酒酵母菌去甲基酶JHD1p的受質專一性研究，基

    於報導在酵母菌的胞外去甲基酶JHD1p為具活性的酵素，而且大部份

    研究都以組蛋白上的受質為主要研究目標，所以本實驗想利用啤酒

    酵母菌去甲基酶JHD1p的胞外活性測試，尋找是否還有非組蛋白的功

    能性受質存在。
    The basic unit of chromatin consists of 146 bps of DNA

    wrapped around a histone octamer, which is composed of two

    copies of each of the four core histones: H2A, H2B, H3 and

    H4. The covalent modification of core histones modulates

    genome function by contributing additional epigenetic

    information. At this stage, one of the common covalent

    histone modification is methylation. In recent years ,

    methylation is determined to be reversible and another

    dynamic group protein covalent modification,

    demethylation, is established. Therefore,the covalent

    modification of histones plays a pivotal role in the

    epigenetic control of gene expression.

    In this study, substrate specificity of Saccharomyces

    cerevisiae JHD1p demethylase is studied. Based on the

    information known from literature, Saccharomyces

    cerevisiae JHD1p demethylase is an enzyme

    with activity in vitro, and most of the studies have

    focused on the substrate role of histone proteins as the

    main research goal. Nevertheless, this study would like to

    use the in vitro activity of enzyme JHD1p to

    find out whether there is any functional non-histone

    substrates existing in Saccharomyces cerevisiae.
    Appears in Collections:[Graduate Institue of Life Sciences] Thesis

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