期刊
EMBO REPORTS
卷 17, 期 12, 页码 1799-1813出版社
WILEY-BLACKWELL
DOI: 10.15252/embr.201642486
关键词
FHA domain protein; immune gene expression; plant immunity; protein poly(ADP-ribosyl)ation (PARylation)
资金
- National Science Foundation (NSF) [IOS-1252539]
- National Institutes of Health (NIH) [R01GM092893]
- NIH [1R01GM097247]
- Robert A. Welch foundation [A-1795]
- NSF [DBI-0723722, DBI-1042344]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1252539] Funding Source: National Science Foundation
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 invitro 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.
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