4.8 Article

Identification and receptor mechanism of TIR-catalyzed small molecules in plant immunity

Journal

SCIENCE
Volume 377, Issue 6605, Pages 487-+

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abq3297

Keywords

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Funding

  1. National Key Research and Development Program of China [2021YFA1300701]
  2. Alexander von Humboldt Foundation
  3. Max-Planck-Gesellschaft
  4. Deutsche Forschungsgemeinschaft [SFB-1403-414786233]
  5. Germany's Excellence Strategy CEPLAS (EXC-2048/1) [390686111]
  6. Max-Planck International PhD Research School (IMPRS)
  7. National Natural Science Foundation of China [82130103, U1804283]

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This article investigates the role of TIR domain in plant receptors in catalyzing the production of pRib-AMP and pRib-ADP, and finds that these molecules play a crucial role in plant immune signaling, involving the participation of other proteins.
Plant nucleotide-binding leucine-rich repeat-containing (NLR) receptors with an N-terminal Toll/ interleukin-1 receptor (TIR) domain sense pathogen effectors to enable TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) activity for immune signaling. TIR-NLR signaling requires the helper NLRs N requirement gene 1 (NRG1), Activated Disease Resistance 1 (ADR1), and Enhanced Disease Susceptibility 1 (EDS1), which forms a heterodimer with each of its paralogs Phytoalexin Deficient 4 (PAD4) and Senescence-Associated Gene 101 (SAG101). Here, we show that TIR-containing proteins catalyze the production of 2'-(5''-phosphoribosyl)-5'-adenosine monophosphate (pRib-AMP) and diphosphate (pRib-ADP) in vitro and in planta. Biochemical and structural data demonstrate that EDS1PAD4 is a receptor complex for pRib-AMP and pRib-ADP, which allosterically promote EDS1-PAD4 interaction with ADR1-L1 but not NRG1A. Our study identifies TIR-catalyzed pRib-AMP and pRib-ADP as a missing link in TIR signaling through EDS1-PAD4 and as likely second messengers for plant immunity.

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