在細胞中金屬感應轉錄因子(MTF-1)平常大多位於細胞質，當其受到活化會進入細胞核內，與啟動子上的金屬感應序列結合，活化下游基因表現，藉以調節細胞中鋅離子濃度恆定、或對抗重金屬毒性以及氧化、缺氧逆境。轉譯後修飾作用可能會影響並改變蛋白質的特性，但目前對於MTF-1蛋白質後修飾作用的研究尚不充足完善，然而透過我們先前的研究已得知小鼠MTF-1在lysine 627位置會被SUMO-1這後修飾蛋白進行修飾，並且以鋅離子刺激時被修飾的程度會明顯下降；而在本篇研究我們主要想探討MTF-1是否也會被另一SUMO成員SUMO-3進行修飾，並探討其蛋白質特性是否受到影響。經由我們的實驗結果證實MTF-1會被SUMO-3進行修飾且主要位置也在lysine 627；而當細胞以鋅離子的刺激時，與SUMO-1的修飾不同，MTF-1被SUMO-3修飾的程度略有上升，但不隨濃度增加而增加。透過即時定量PCR及報導基因檢測發現，SUMO-3的大量表現或修飾會抑制MTF-1的轉錄活性，但MTF-1在細胞中分布情形以及與DNA的結合能力卻不會受到SUMO-3影響；而我們也證明SUMO-3的大量表現或修飾會增加MTF-1蛋白質的穩定性，且比較被SUMO-3或SUMO-1修飾的MTF-1，發現被SUMO-3修飾的MTF-1有較高的蛋白質穩定性。

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