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Title: | Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets |
Authors: | Krastev, DB Pettitt, SJ Campbell, J Song, F Tanos, BE Stoynov, SS Ashworth, A Lord, CJ |
Keywords: | fluorescent proteins;polyADP-ribosylation |
Issue Date: | 22-May-2018 |
Publisher: | Springer Nature |
Citation: | Krastev, D.B., Pettitt, S.J., Campbell, J., Song, F., Tanos, B.E., Stoynov, S.S., Ashworth, A. and Lord, C.J. (2018) 'Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets', Nature Communications, 9 (1), 2016, pp. 1-14. doi: 10.1038/s41467-018-04466-4. |
Abstract: | Copyright © The Author(s) 2018. 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. |
URI: | https://bura.brunel.ac.uk/handle/2438/23953 |
DOI: | https://doi.org/10.1038/s41467-018-04466-4 |
Other Identifiers: | 2016 |
Appears in Collections: | Dept of Life Sciences Research Papers |
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