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    Please use this identifier to cite or link to this item: http://ir.cnu.edu.tw/handle/310902800/26747


    標題: Mutational Analysis of Splicing Activities of Ribonucleotide Reductase α Subunit Protein from Lytic Bacteriophage P1201
    作者: Kan, Shu-Chen
    Yu, Liang-Kun
    Chen, Jiau-Hua
    Hu, Hui-Yu
    Hsu, Wen-Hwei
    貢獻者: 食品科技系
    日期: 2011-04
    上傳時間: 2013-06-26 15:34:39 (UTC+8)
    出版者: Springer-Verlag
    摘要: A CP1201 RIR1 intein is found in the ribonucleotide reductase alpha subunit (RNR α subunit) protein of lytic bacteriophage P1201 from Corynebacterium glutamicum NCHU 87078. This intein can be over-expressed and spliced in Escherichia coli NovaBlue cells. Mutations of C539, the N-terminal residue of the C-extein in the CP1201 RIR1 protein, led to the changes of pattern and level of protein-splicing activities. A G392S variant was found to be a temperature-sensitive protein with complete splicing activity at 17 and 28°C but not at 37°C or higher. We also found that the cleavage at the CP1201 RIR1 intein C-terminus of the double mutant G392S/C539G was blocked, but other cleavage activities could be efficiently performed at 17°C. G392S/C539G variant possessed the properties of low-temperature-induced cleavage at the intein N-terminus.
    關聯: Current Microbiology 62(4), pp.1282-1286
    Appears in Collections:[ 食品科技系 ] 期刊論文

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