Journal
NATURE CHEMICAL BIOLOGY
Volume 5, Issue 6, Pages 400-402Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.172
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- Lithuanian State Science and Study Foundation
- Ministry of Education and Science of Lithuania
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Targeted methylation of cytosine residues by S-adenosylmethionine-dependent DNA methyltransferases modulates gene expression in vertebrates. Here we show that cytosine-5-methyltransferases catalyze reversible covalent addition of exogenous aliphatic aldehydes to their target residues in DNA, thus yielding corresponding 5-alpha-hydroxyalkylcytosines. Such atypical enzymatic reactions with non-cofactor-like substrates open new ways for sequence-specific derivatization of DNA and demonstrate enzymatic exchange of 5-hydroxymethyl groups on cytosine in support of an oxidative mechanism of DNA demethylation.
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