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

Li Wan, Kow Essuman, Ryan G Anderson, Yo Sasaki, Freddy Monteiro, Eui-Hwan Chung, Erin Osborne Nishimura, Aaron DiAntonio, Jeffrey Milbrandt, Jeffery L Dangl, Marc T Nishimura

Science. 2019 Aug 23;365(6455):799-803.

PMID: 31439793

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP119340533 Cyclic adenosine diphosphate-ribose Cyclic adenosine diphosphate-ribose 119340-53-3 Price
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