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Family-wide analysis of poly(ADP-ribose) polymerase activity

Author

Listed:
  • Sejal Vyas

    (Koch Institute for Integrative Cancer Research
    Massachusetts Institute of Technology)

  • Ivan Matic

    (Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Sir James Black Centre
    Present address: Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Street 9b, D-50931 Köln/Cologne, Germany)

  • Lilen Uchima

    (Koch Institute for Integrative Cancer Research
    Massachusetts Institute of Technology)

  • Jenny Rood

    (Koch Institute for Integrative Cancer Research
    Massachusetts Institute of Technology)

  • Roko Zaja

    (Sir William Dunn School of Pathology, University of Oxford
    Rudjer Boskovic Institute)

  • Ronald T. Hay

    (Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Sir James Black Centre)

  • Ivan Ahel

    (Sir William Dunn School of Pathology, University of Oxford)

  • Paul Chang

    (Koch Institute for Integrative Cancer Research
    Massachusetts Institute of Technology)

Abstract

The poly(adenosine diphosphate (ADP)-ribose) polymerase (PARP) protein family generates ADP-ribose (ADPr) modifications onto target proteins using NAD+ as substrate. Based on the composition of three NAD+ coordinating amino acids, the H-Y-E motif, each PARP is predicted to generate either poly(ADPr) (PAR) or mono(ADPr) (MAR). However, the reaction product of each PARP has not been clearly defined, and is an important priority since PAR and MAR function via distinct mechanisms. Here we show that the majority of PARPs generate MAR, not PAR, and demonstrate that the H-Y-E motif is not the sole indicator of PARP activity. We identify automodification sites on seven PARPs, and demonstrate that MAR and PAR generating PARPs modify similar amino acids, suggesting that the sequence and structural constraints limiting PARPs to MAR synthesis do not limit their ability to modify canonical amino-acid targets. In addition, we identify cysteine as a novel amino-acid target for ADP-ribosylation on PARPs.

Suggested Citation

  • Sejal Vyas & Ivan Matic & Lilen Uchima & Jenny Rood & Roko Zaja & Ronald T. Hay & Ivan Ahel & Paul Chang, 2014. "Family-wide analysis of poly(ADP-ribose) polymerase activity," Nature Communications, Nature, vol. 5(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5426
    DOI: 10.1038/ncomms5426
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    Cited by:

    1. Edoardo José Longarini & Ivan Matić, 2024. "Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Marie-France Langelier & Ramya Billur & Aleksandr Sverzhinsky & Ben E. Black & John M. Pascal, 2021. "HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    3. Pietro Fontana & Sara C. Buch-Larsen & Osamu Suyari & Rebecca Smith & Marcin J. Suskiewicz & Kira Schützenhofer & Antonio Ariza & Johannes Gregor Matthias Rack & Michael L. Nielsen & Ivan Ahel, 2023. "Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    4. Daipayan Banerjee & Kurt Langberg & Salar Abbas & Eric Odermatt & Praveen Yerramothu & Martin Volaric & Matthew A. Reidenbach & Kathy J. Krentz & C. Dustin Rubinstein & David L. Brautigan & Tarek Abba, 2021. "A non-canonical, interferon-independent signaling activity of cGAMP triggers DNA damage response signaling," Nature Communications, Nature, vol. 12(1), pages 1-24, December.

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