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

Author(s)
Vyas, Sejal; Matic, Ivan; Uchima, Lilen; Rood, Jenny; Zaja, Roko; Hay, Ronald T.; Ahel, Ivan; Chang, Paul; ... Show more Show less
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Abstract
The poly(adenosine diphosphate (ADP)-ribose) polymerase (PARP) protein family generates ​ADP-ribose (​ADPr) modifications onto target proteins using ​NAD[superscript +] as substrate. Based on the composition of three ​NAD[superscript +] coordinating amino acids, the H-Y-E motif, each PARP is predicted to generate either poly(ADPr) (PAR) or mono(ADPr) (MAR). However, the reaction product of each PARP 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 PARPs generate MAR, not PAR, and demonstrate that the H-Y-E motif is not the sole indicator of PARP activity. We identify automodification sites on seven PARPs, and demonstrate that MAR and PAR generating PARPs modify similar amino acids, suggesting that the sequence and structural constraints limiting PARPs 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 PARPs.
Date issued
2014-07
URI
http://hdl.handle.net/1721.1/96282
Department
Massachusetts Institute of Technology. Department of Biology; Koch Institute for Integrative Cancer Research at MIT
Journal
Nature Communications
Publisher
Nature Publishing Group
Citation
Vyas, Sejal, Ivan Matic, Lilen Uchima, Jenny Rood, Roko Zaja, Ronald T. Hay, Ivan Ahel, and Paul Chang. “Family-Wide Analysis of poly(ADP-Ribose) Polymerase Activity.” Nature Communications 5 (July 21, 2014).
Version: Author's final manuscript
ISSN
2041-1723

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