Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.06.25.546318v1?rss=1

Authors: Đukic, N., Stromland, O., Munnur, D., Zhu, K., Schuller, M., Chatrin, C., Kar, P., Rack, J. G. M., Baretic, D., Schüler, H., Wijngaarden, S., Filippov, D. V., Sanyal, S., Smith, R., Ahel, D., Ahel, I.

Abstract:
PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. Here we show that PARP14 is dual function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a dramatic increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.

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