Journal
CELL
Volume 185, Issue 13, Pages 2370-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2022.04.032
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Funding
- Alexander von Humboldt Foundation
- Max-Planck-Gesellschaft (a Max Planck fellowship)
- Deutsche Forschungsgemeinschaft [SFB-1403-414786233, EXC-2048/1, 390686111]
- Ministry of Health - Singapore, NMRC-OFIRG grant [MOH-000382-00]
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This study reveals that plant Toll/interleukin-1 receptor (TIR) proteins not only have NADase function, but also act as 2',3'-cAMP/cGMP synthetases. These cyclic nucleotide monophosphates (cNMPs) play a critical role in plant immune responses.
2',3'-cAMP is a positional isomer of the well-established second messenger 3',5'-cAMP, but little is known about the biology of this noncanonical cyclic nucleotide monophosphate (cNMP). Toll/interleukin-1 receptor (TIR) domains of nucleotide-binding leucine-rich repeat (NLR) immune receptors have the NADase function necessary but insufficient to activate plant immune responses. Here, we show that plant TIR proteins, besides being NADases, act as 2',3'-cAMP/cGMP synthetases by hydrolyzing RNA/DNA. Structural data show that a TIR domain adopts distinct oligomers with mutually exclusive NADase and synthetase activity. Mutations specifically disrupting the synthetase activity abrogate TIR-mediated cell death in Nicotiana benthamiana (Nb), supporting an important role for these cNMPs in TIR signaling. Furthermore, the Arabidopsis negative regulator of TIR-NLR signaling, NUDT7, displays 2',3'-cAMP/cGMP but not 3',5'-cAMP/cGMP phosphodiesterase activity and suppresses cell death activity of TIRs in Nb. Our study identifies a family of 2',3'-cAMP/cGMP synthetases and establishes a critical role for them in plant immune responses.
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