Real-Time Cellular Imaging of Protein Poly(ADP-ribos)ylation

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Angewandte Chemie International Edition. 2016, 55(37), pp. 11256-11260. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201605282
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Poly(ADP-ribos)ylation (PARylation) is an important posttranslational protein modification, and is involved in major cellular processes such as gene regulation and DNA repair. Its dysregulation has been linked to several diseases, including cancer. Despite its importance, methods to observe PARylation dynamics within cells are rare. By following a chemical biology approach, we developed a fluorescent NAD(+) analogue that proved to be a competitive building block for protein PARylation in vitro and in cells. This allowed us to directly monitor the turnover of PAR in living cells at DNA damage sites after near-infrared (NIR) microirradiation. Additionally, covalent and noncovalent interactions of selected target proteins with PAR chains were visualized in cells by using FLIM-FRET microscopy. Our results open up new opportunities for the study of protein PARylation in real time and in live cells, and will thus contribute to a better understanding of its significance in a cellular context.

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ISO 690BUNTZ, Annette, Sarah WALLRODT, Eva GWOSCH, Michael SCHMALZ, Sascha BENEKE, Elisa FERRANDO-MAY, Andreas MARX, Andreas ZUMBUSCH, 2016. Real-Time Cellular Imaging of Protein Poly(ADP-ribos)ylation. In: Angewandte Chemie International Edition. 2016, 55(37), pp. 11256-11260. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201605282
BibTex
@article{Buntz2016RealT-35181,
  year={2016},
  doi={10.1002/anie.201605282},
  title={Real-Time Cellular Imaging of Protein Poly(ADP-ribos)ylation},
  number={37},
  volume={55},
  issn={1433-7851},
  journal={Angewandte Chemie International Edition},
  pages={11256--11260},
  author={Buntz, Annette and Wallrodt, Sarah and Gwosch, Eva and Schmalz, Michael and Beneke, Sascha and Ferrando-May, Elisa and Marx, Andreas and Zumbusch, Andreas},
  note={Annette Buntz and Sarah Wallrodt contributed equally.}
}
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Annette Buntz and Sarah Wallrodt contributed equally.
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