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TitleTIR domains of plant immune receptors are 2',3'-cAMP/cGMP synthetases mediating cell death.
Journal, issue, pagesCell, Vol. 185, Issue 13, Page 2370-2386.e18, Year 2022
Publish dateJun 23, 2022
AuthorsDongli Yu / Wen Song / Eddie Yong Jun Tan / Li Liu / Yu Cao / Jan Jirschitzka / Ertong Li / Elke Logemann / Chenrui Xu / Shijia Huang / Aolin Jia / Xiaoyu Chang / Zhifu Han / Bin Wu / Paul Schulze-Lefert / Jijie Chai /
PubMed Abstract2',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). ...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.
External linksCell / PubMed:35597242
MethodsEM (helical sym.) / EM (single particle)
Resolution3.0 - 3.8 Å
Structure data

32121

7x5k

EMDB-32121: TIR-dsDNA initial state complex
PDB-7x5k: Tir-dsDNA complex, the initial binding state
Method: EM (helical sym.) / Resolution: 3.4 Å

32125

7x5l

EMDB-32125: L7-TIR nucleic acids complex intermediate complex
PDB-7x5l: Tir-dsDNA complex, the initial binding state
Method: EM (helical sym.) / Resolution: 3.5 Å

32126

7vu8

7x5m

EMDB-32126: L7-TIR-nucleic acid End State Complex
PDB-7vu8: L7-Tir domain with bound ligand
PDB-7x5m: Tir-dsDNA complex, the initial binding state
Method: EM (helical sym.) / Resolution: 3.0 Å

Chemicals

ChemComp-ACK:
2',3'- cyclic AMP

Source
  • linum usitatissimum (flax)
  • dna molecule (others)
KeywordsHYDROLASE / Nucleic acid hydrolysis complex / HYDROLASE/DNA / plant innate immune receptor / nucleic acids / 2' / 3'cNMP / HYDROLASE-DNA COMPLEX

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