PARylation of the forkhead-associated domain protein DAWDLE regulates plant immunity

Baomin Feng, Shisong Ma, Sixue Chen, Ning Zhu, Shuxin Zhang, Bin Yu, Yu Yu, Brandon Le, Xuemei Chen, Savithramma P. Dinesh-Kumar, Libo Shan, Ping He

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Protein poly(ADP-ribosyl)ation (PARylation) primarily catalyzed by poly(ADP-ribose) polymerases (PARPs) plays a crucial role in controlling various cellular responses. However, PARylation targets and their functions remain largely elusive. Here, we deployed an Arabidopsis protein microarray coupled with in vitro PARylation assays to globally identify PARylation targets in plants. Consistent with the essential role of PARylation in plant immunity, the forkhead-associated (FHA) domain protein DAWDLE (DDL), one of PARP2 targets, positively regulates plant defense to both adapted and non-adapted pathogens. Arabidopsis PARP2 interacts with and PARylates DDL, which was enhanced upon treatment of bacterial flagellin. Mass spectrometry and mutagenesis analysis identified multiple PARylation sites of DDL by PARP2. Genetic complementation assays indicate that DDL PARylation is required for its function in plant immunity. In contrast, DDL PARylation appears to be dispensable for its previously reported function in plant development partially mediated by the regulation of microRNA biogenesis. Our study uncovers many previously unknown PARylation targets and points to the distinct functions of DDL in plant immunity and development mediated by protein PARylation and small RNA biogenesis, respectively.

Original languageEnglish (US)
Pages (from-to)1799-1813
Number of pages15
JournalEMBO Reports
Issue number12
StatePublished - Dec 1 2016


  • FHA domain protein
  • immune gene expression
  • plant immunity
  • protein poly(ADP-ribosyl)ation (PARylation)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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