Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation.

摘要: ADP-ribosylation controls many processes, including transcription, DNA repair, and bacterial toxicity. ADP-ribosyltransferases poly-ADP-ribose polymerases (PARPs) catalyze mono- poly-ADP-ribosylation, respectively, depend on a highly conserved glutamate residue in the active center for catalysis. However, there is an apparent absence of this recently described PARP6-PARP16, raising questions about how these enzymes function. We find that PARP10, contrast to PARP1, lacks catalytic has transferase rather than polymerase activity. Despite fundamental difference, PARP10 also modifies acidic residues. Consequently, we propose alternative mechanism compared PARP1 which target substrate functionally substitutes by using substrate-assisted catalysis transfer ADP-ribose. This explains why novel PARPs are unable function as polymerases. discovery will help illuminate different biological functions versus poly-ADP-ribosylation cells.