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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/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









    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:[生命科學研究所] 學位論文

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