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Journal Article

Efficient cosubstrate enzyme pairs for sequence-specific methyltransferase-directed photolabile caging of DNA

MPS-Authors
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Heimes,  Michael
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kolmar,  Leonie
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Brieke,  Clara
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://pubs.rsc.org/en/content/articlepdf/2018/cc/c8cc05913f
(Any fulltext)

https://doi.org/10.1039/C8CC05913F
(Any fulltext)

http://www.rsc.org/suppdata/c8/cc/c8cc05913f/c8cc05913f1.pdf
(Supplementary material)

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Citation

Heimes, M., Kolmar, L., & Brieke, C. (2018). Efficient cosubstrate enzyme pairs for sequence-specific methyltransferase-directed photolabile caging of DNA. Chemical Communications, 54(90), 12718-12721. doi:10.1039/C8CC05913F.


Cite as: https://hdl.handle.net/21.11116/0000-0002-66B5-F
Abstract
Supplemented with synthetic surrogates of their natural cosubstrate S-adenosyl-L-methione (AdoMet), methyltransferases represent a powerful toolbox for the functionalization of biomolecules. By employing novel cosubstrate derivatives in combination with protein engineering, we show that this chemo-enzymatic method can be used to introduce photolabile protecting groups into DNA even in the presence of AdoMet. This approach enables optochemical control of gene expression in a straight-forward manner and we have termed it reversible methyltransferase directed transfer of photoactivatable groups (re-mTAG).