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Hydrolysis of ADP-Ribosylation by Macrodomains

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ADP-ribosylation and NAD+ Utilizing Enzymes

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1813))

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Abstract

ADP-ribosylation is the process of transferring the ADP-ribose moiety from NAD+ to a substrate. While a number of proteins represent well described substrates accepting ADP-ribose modification, a recent report demonstrated biological role for DNA ADP-ribosylation as well. The conserved macrodomain fold of several known hydrolyses was found to possess de-ADP-ribosylating activity and the ability to hydrolyze (reverse) ADP-ribosylation. Here we summarize the methods that can be employed to study mono-ADP-ribosylation hydrolysis by macrodomains.

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Acknowledgments

The work in Ahel lab is supported by Wellcome Trust (grant number 101794), the European Research Council (grant number 281739) and by Cancer Research UK (grant number C35050/A22284). MPM is financed by Croatian National Centre of Research Excellence in Personalized Healthcare grant.

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Authors and Affiliations

  1. University of Zagreb, Zagreb, Croatia

    Melanija Posavec Marjanovic´

  2. Sir William Dunn School of Pathology, University of Oxford, Oxford, UK

    Gytis Jankevicius & Ivan Ahel

Authors
  1. Melanija Posavec Marjanovic´
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  2. Gytis Jankevicius
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  3. Ivan Ahel
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Correspondence to Ivan Ahel .

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Editors and Affiliations

  1. Department of Biology, Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA

    Paul Chang

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Posavec Marjanovic´, M., Jankevicius, G., Ahel, I. (2018). Hydrolysis of ADP-Ribosylation by Macrodomains. In: Chang, P. (eds) ADP-ribosylation and NAD+ Utilizing Enzymes. Methods in Molecular Biology, vol 1813. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-8588-3_14

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  • DOI: https://doi.org/10.1007/978-1-4939-8588-3_14

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-4939-8587-6

  • Online ISBN: 978-1-4939-8588-3

  • eBook Packages: Springer Protocols

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