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TIR domains of plant immune receptors are NAD+-cleaving enzymes that promote cell death.


ABSTRACT: Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors activate cell death and confer disease resistance by unknown mechanisms. We demonstrate that plant Toll/interleukin-1 receptor (TIR) domains of NLRs are enzymes capable of degrading nicotinamide adenine dinucleotide in its oxidized form (NAD+). Both cell death induction and NAD+ cleavage activity of plant TIR domains require known self-association interfaces and a putative catalytic glutamic acid that is conserved in both bacterial TIR NAD+-cleaving enzymes (NADases) and the mammalian SARM1 (sterile alpha and TIR motif containing 1) NADase. We identify a variant of cyclic adenosine diphosphate ribose as a biomarker of TIR enzymatic activity. TIR enzymatic activity is induced by pathogen recognition and functions upstream of the genes enhanced disease susceptibility 1 (EDS1) and N requirement gene 1 (NRG1), which encode regulators required for TIR immune function. Thus, plant TIR-NLR receptors require NADase function to transduce recognition of pathogens into a cell death response.

SUBMITTER: Wan L 

PROVIDER: S-EPMC7045805 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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TIR domains of plant immune receptors are NAD<sup>+</sup>-cleaving enzymes that promote cell death.

Wan Li L   Essuman Kow K   Anderson Ryan G RG   Sasaki Yo Y   Monteiro Freddy F   Chung Eui-Hwan EH   Osborne Nishimura Erin E   DiAntonio Aaron A   Milbrandt Jeffrey J   Dangl Jeffery L JL   Nishimura Marc T MT  

Science (New York, N.Y.) 20190801 6455


Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors activate cell death and confer disease resistance by unknown mechanisms. We demonstrate that plant Toll/interleukin-1 receptor (TIR) domains of NLRs are enzymes capable of degrading nicotinamide adenine dinucleotide in its oxidized form (NAD<sup>+</sup>). Both cell death induction and NAD<sup>+</sup> cleavage activity of plant TIR domains require known self-association interfaces and a putative catalytic glutamic acid that is co  ...[more]

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