PARylation of the forkhead-associated domain protein DAWDLE regulates plant immunity.
Baomin FengShisong MaSixue ChenNing ZhuShuxin ZhangBin YuYu YuBrandon LeXuemei ChenSavithramma P Dinesh-KumarLibo ShanPing HePublished in: EMBO reports (2016)
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.
Keyphrases
- mass spectrometry
- transcription factor
- protein protein
- cell wall
- binding protein
- dna damage
- dna repair
- gene expression
- magnetic resonance
- small molecule
- crispr cas
- high throughput
- plant growth
- liquid chromatography
- ms ms
- multidrug resistant
- smoking cessation
- copy number
- contrast enhanced
- capillary electrophoresis
- nucleic acid