Poly (ADP-ribose) polymerases (PARPs) catalyze the transfer of multiple poly(ADP-ribose) units onto target proteins. Poly(ADP-ribosyl)ation plays a crucial role in a variety of cellular processes including， most prominently， auto-activation of PARP at sites of DNA breaks to activate DNA repair processes. In humans， PARP1 (the founding and most characterized member of the PARP family) accounts for more than 90% of overall cellular PARP activity in response to DNA damage. We have found that， in contrast with animals， in Arabidopsis thaliana PARP2 (At4g02390)， rather than PARP1 (At2g31320)， makes the greatest contribution to PARP activity and organismal viability in response to genotoxic stresses cau... More
Poly (ADP-ribose) polymerases (PARPs) catalyze the transfer of multiple poly(ADP-ribose) units onto target proteins. Poly(ADP-ribosyl)ation plays a crucial role in a variety of cellular processes including， most prominently， auto-activation of PARP at sites of DNA breaks to activate DNA repair processes. In humans， PARP1 (the founding and most characterized member of the PARP family) accounts for more than 90% of overall cellular PARP activity in response to DNA damage. We have found that， in contrast with animals， in Arabidopsis thaliana PARP2 (At4g02390)， rather than PARP1 (At2g31320)， makes the greatest contribution to PARP activity and organismal viability in response to genotoxic stresses caused by bleomycin， mitomycin C or gamma-radiation. Plant PARP2 proteins carry SAP DNA binding motifs rather than the zinc finger domains common in plant and animal PARP1 proteins. PARP2 also makes stronger contributions than PARP1 to plant immune responses including restriction of pathogenic Pseudomonas syringae pv. tomato growth and reduction of infection-associated DNA double-strand break abundance. For poly(ADP-ribose) glycohydrolase (PARG) enzymes， we find that Arabidopsis PARG1 and not PARG2 is the major contributor to poly(ADP-ribose) removal from acceptor proteins. The activity or abundance of PARP2 is influenced by PARP1 and PARG1. PARP2 and PARP1 physically interact with each other， and with PARG1 and PARG2， suggesting relatively direct regulatory interactions among these mediators of the balance of poly(ADP-ribosyl)ation. As with plant PARP2， plant PARG proteins are also structurally distinct from their animal counterparts. Hence core aspects of plant poly(ADP-ribosyl)ation are mediated by substantially different enzymes than in animals， suggesting the likelihood of substantial differences in regulation.
