Family-wide analysis of poly(ADP-ribose) polymerase activity.

The poly(adenosine diphosphate (ADP)-ribose) polymerase protein family generates ADP-ribose (ADPr) modifications onto target proteins using NAD(+) as substrate. Based on the composition of three NAD(+) coordinating amino acids, the H-Y-E motif, each is predicted to generate either poly(ADPr) (PAR) or mono(ADPr) (MAR). However, the reaction product of each Pduanyu37 has not been clearly defined, and is an important priority since PAR and MAR function via distinct mechanisms. Here we show that the majority of generate MAR, not PAR, and demonstrate that the H-Y-E motif is not the sole indicator of Pduanyu37 activity. We identify automodification sites on seven and demonstrate that MAR and PAR generating Pduanyu37s modify similar amino acids, suggesting that the sequence and structural constraints limiting Pduanyu37s to MAR synthesis do not limit their ability to modify canonical amino-acid targets. In addition, we identify cysteine as a novel amino-acid target for ADP-ribosylation on

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