Unknown

Dataset Information

0

The mammalian de novo DNA methyltransferases DNMT3A and DNMT3B are also DNA 5-hydroxymethylcytosine dehydroxymethylases.


ABSTRACT: For cytosine (C) demethylation of vertebrate DNA, it is known that the TET proteins could convert 5-methyl C (5-mC) to 5-hydroxymethyl C (5-hmC). However, DNA dehydroxymethylase(s), or enzymes able to directly convert 5-hmC to C, have been elusive. We present in vitro evidence that the mammalian de novo DNA methyltransferases DNMT3A and DNMT3B, but not the maintenance enzyme DNMT1, are also redox-dependent DNA dehydroxymethylases. Significantly, intactness of the C methylation catalytic sites of these de novo enzymes is also required for their 5-hmC dehydroxymethylation activity. That DNMT3A and DNMT3B function bidirectionally both as DNA methyltransferases and as dehydroxymethylases raises intriguing and new questions regarding the structural and functional aspects of these enzymes and their regulatory roles in the dynamic modifications of the vertebrate genomes during development, carcinogenesis, and gene regulation.

SUBMITTER: Chen CC 

PROVIDER: S-EPMC3460417 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

The mammalian de novo DNA methyltransferases DNMT3A and DNMT3B are also DNA 5-hydroxymethylcytosine dehydroxymethylases.

Chen Chun-Chang CC   Wang Keh-Yang KY   Shen Che-Kun James CK  

The Journal of biological chemistry 20120816 40


For cytosine (C) demethylation of vertebrate DNA, it is known that the TET proteins could convert 5-methyl C (5-mC) to 5-hydroxymethyl C (5-hmC). However, DNA dehydroxymethylase(s), or enzymes able to directly convert 5-hmC to C, have been elusive. We present in vitro evidence that the mammalian de novo DNA methyltransferases DNMT3A and DNMT3B, but not the maintenance enzyme DNMT1, are also redox-dependent DNA dehydroxymethylases. Significantly, intactness of the C methylation catalytic sites of  ...[more]

Similar Datasets

| S-EPMC84905 | biostudies-literature
| S-EPMC7314859 | biostudies-literature
| S-EPMC8452533 | biostudies-literature
| S-EPMC2756565 | biostudies-literature
2016-06-03 | GSE70722 | GEO
2016-06-03 | GSE70721 | GEO
2016-06-03 | GSE70720 | GEO
| S-EPMC7335073 | biostudies-literature
| S-EPMC18343 | biostudies-literature
| S-EPMC3093119 | biostudies-literature