The human Dnmt2 has residual DNA-(Cytosine-C5) methyltransferase activity.
The human Dnmt2 has residual DNA-(Cytosine-C5) methyltransferase activity.
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DOI：
10.1074/jbc.m305448200
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发表时间：
2003-08-22
影响因子：
4.8
通讯作者：
Jeltsch, A
中科院分区：
文献类型：
--
作者：
Hermann, A;Schmitt, S;Jeltsch, A
人Dnmt 2蛋白是从粟酒裂殖酵母和黑腹果蝇到小家鼠和智人保守的蛋白家族的一个成员。它含有DNA-（胞嘧啶-C5）甲基转移酶的所有特征性氨基酸基序，其结构与原核DNA甲基转移酶非常相似。然而，到目前为止，所有试图检测这种蛋白质的催化活性都失败了。我们在这里通过两个独立的测定系统表明，纯化的Dnmt 2蛋白具有弱的DNA甲基转移酶活性。在一个松散的ttnCG（ga（g/a））共有序列中的CG位点观察到甲基化，表明Dnmt 2具有比其他哺乳动物DNA甲基转移酶更专门的作用。
The human Dnmt2 protein is one member of a protein family conserved from Schizosaccharomyces pombe and Drosophila Melanogaster to Mus musculus and Homo sapiens. It contains all of the amino acid motifs characteristic for DNA-(Cytosine-C5) methyltransferases, and its structure is very similar to prokaryotic DNA methyltransferases. Nevertheless, so far all attempts to detect catalytic activity of this protein have failed. We show here by two independent assay systems that the purified Dnmt2 protein has weak DNA methyltransferase activity. Methylation was observed a CG sites in a loose ttnCG(ga(g/a)) consensus sequence, suggesting that Dnmt2 has a more specialized role than other mammalian DNA methyltransferases.