TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity
Copyright policy )TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity
Plant pathogen–activated immune signaling by nucleotide-binding leucine-rich repeat (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain converges on Enhanced Disease Susceptibility 1 (EDS1) and its direct partners, Phytoalexin Deficient 4 (PAD4) or Senescence-Associated Gene 101 (SAG101). TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) produces signaling molecules to promote exclusive EDS1-PAD4 and EDS1-SAG101 interactions with helper NLR subclasses. In this work, we show that TIR-containing proteins catalyze adenosine diphosphate (ADP)–ribosylation of adenosine triphosphate (ATP) and ADP ribose (ADPR) through ADPR polymerase–like and NADase activity, forming ADP-ribosylated ATP (ADPr-ATP) and ADPr-ADPR (di-ADPR), respectively. Specific binding of ADPr-ATP or di-ADPR allosterically promotes EDS1-SAG101 interaction with helper NLR N requirement gene 1A (NRG1A) in vitro and in planta. Our data reveal an enzymatic activity of TIRs that enables specific activation of the EDS1-SAG101-NRG1 immunity branch.
- Max Planck Institute for Plant Breeding Research Germany
- University of Cologne Germany
- Zhengzhou University China (People's Republic of)
- Henan Normal University China (People's Republic of)
- Tsinghua University China (People's Republic of)
Adenosine Diphosphate, DNA-Binding Proteins, ADP-Ribosylation, Adenosine Triphosphate, NAD+ Nucleosidase, Arabidopsis Proteins, Arabidopsis, Intracellular Signaling Peptides and Proteins, Plant Immunity, Carboxylic Ester Hydrolases
Adenosine Diphosphate, DNA-Binding Proteins, ADP-Ribosylation, Adenosine Triphosphate, NAD+ Nucleosidase, Arabidopsis Proteins, Arabidopsis, Intracellular Signaling Peptides and Proteins, Plant Immunity, Carboxylic Ester Hydrolases
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