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

Science. 2019 Aug 23;365(6455):799-803. doi: 10.1126/science.aax1771.

Li Wan ^# ¹, Kow Essuman ^# ², Ryan G Anderson ¹, Yo Sasaki ², Freddy Monteiro ¹ ³, Eui-Hwan Chung ¹, Erin Osborne Nishimura ⁴, Aaron DiAntonio ⁵ ⁶, Jeffrey Milbrandt ⁷ ⁶ ⁸, Jeffery L Dangl ⁹, Marc T Nishimura ¹⁰

Affiliations

1 Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599, USA.
2 Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA.
3 Center for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, 08193 Barcelona, Spain.
4 Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
5 Department of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110, USA.
6 Needleman Center for Neurometabolism and Axonal Therapeutics, Washington University School of Medicine, St. Louis, MO 63110, USA.
7 Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110, USA. [email protected] [email protected] [email protected].
8 McDonnell Genome Institute, Washington University School of Medicine, St. Louis, MO 63108, USA.
9 Department of Biology and Howard Hughes Medical Institute, University of North Carolina, Chapel Hill, NC 27599, USA. [email protected] [email protected] [email protected].
10 Department of Biology, Colorado State University, Fort Collins, CO 80523, USA. [email protected] [email protected] [email protected].
# Contributed equally.

PMID: 31439793 DOI: 10.1126/science.aax1771

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.

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