The human Dnmt2 has residual DNA-(Cytosine-C5) methyltransferase activity.

被引：165

作者：

Hermann, A

Schmitt, S

Jeltsch, A

机构：

[1] Univ Giessen, Inst Biochem, FB 8, D-35392 Giessen, Germany

[2] Univ Giessen, Biochem Inst, FB 11, D-35392 Giessen, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2003年 / 278卷 / 34期

关键词：

D O I：

10.1074/jbc.M305448200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：31717 / 31721

页数：5

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