Two substrates are better than one: dual specificities for Dnmt2 methyltransferases

被引：81

作者：

Jeltsch, Albert

Nellen, Wolfgang

Lyko, Frank

机构：

[1] Univ Kassel, Div Genet, FB 18, D-34132 Kassel, Germany

[2] Int Jacobs Univ Bremen, Sch Sci & Engn, D-28759 Bremen, Germany

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2006年 / 31卷 / 06期

关键词：

D O I：

10.1016/j.tibs.2006.04.005

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：

Dnmt2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases; however, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought. This finding has important implications for understanding the evolutionary relationships among these enzymes.

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收藏

页码：306 / 308

页数：3

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