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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0002-66B5-F Version Permalink: https://hdl.handle.net/21.11116/0000-0002-CCDF-E
Genre: Journal Article

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 Creators:
Heimes, Michael1, Author           
Kolmar, Leonie1, Author           
Brieke, Clara1, Author           
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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).

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Language(s): eng - English
 Dates: 2018-07-202018-10-182018-10-192018-10
 Publication Status: Issued
 Pages: 4
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 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C8CC05913F
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Title: Chemical Communications
  Other : Chem. Commun.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 54 (90) Sequence Number: - Start / End Page: 12718 - 12721 Identifier: ISSN: 1359-7345
CoNE: https://pure.mpg.de/cone/journals/resource/954928495413