Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets

Dragomir B. Krastev, Stephen J. Pettitt, James Campbell, Feifei Song, Barbara E. Tanos, Stoyno S. Stoynov, Alan Ashworth () and Christopher J. Lord ()
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Dragomir B. Krastev: The Institute of Cancer Research
Stephen J. Pettitt: The Institute of Cancer Research
James Campbell: The Institute of Cancer Research
Feifei Song: The Institute of Cancer Research
Barbara E. Tanos: The Institute of Cancer Research
Stoyno S. Stoynov: Bulgarian Academy of Sciences
Alan Ashworth: The Institute of Cancer Research
Christopher J. Lord: The Institute of Cancer Research

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Poly (ADP-ribose)ylation is a dynamic protein modification that regulates multiple cellular processes. Here, we describe a system for identifying and characterizing PARylation events that exploits the ability of a PBZ (PAR-binding zinc finger) protein domain to bind PAR with high-affinity. By linking PBZ domains to bimolecular fluorescent complementation biosensors, we developed fluorescent PAR biosensors that allow the detection of temporal and spatial PARylation events in live cells. Exploiting transposon-mediated recombination, we integrate the PAR biosensor en masse into thousands of protein coding genes in living cells. Using these PAR-biosensor “tagged” cells in a genetic screen we carry out a large-scale identification of PARylation targets. This identifies CTIF (CBP80/CBP20-dependent translation initiation factor) as a novel PARylation target of the tankyrase enzymes in the centrosomal region of cells, which plays a role in the distribution of the centrosomal satellites.

Date: 2018
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DOI: 10.1038/s41467-018-04466-4

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