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Multiple functional self-association interfaces in plant TIR domains.

Xiaoxiao Zhang1,2, Maud Bernoux3, Adam R Bentham1,4

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Plant immune receptors rely on Toll/interleukin-1 receptor/resistance protein (TIR) domain self-association. Both AE and DE interfaces are crucial for TIR domain self-association and cell-death signaling in diverse plant nucleotide-binding oligomerization domain-like receptors (NLRs).

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Area of Science:

  • Plant immunity
  • Molecular signaling
  • Structural biology

Background:

  • Self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains is critical for signaling in plant and animal immunity receptors.
  • Distinct TIR-domain dimerization interfaces are necessary for signaling in plant nucleotide-binding oligomerization domain-like receptors (NLRs), such as L6 and RPS4.

Purpose of the Study:

  • To investigate the structural basis and functional significance of TIR domain self-association interfaces in plant NLRs.
  • To determine if multiple TIR domain self-association interfaces are simultaneously required for signaling.

Main Methods:

  • Crystal structure determination of TIR domains from *Arabidopsis* NLRs SNC1 and RPP1.
  • Site-directed mutagenesis of identified TIR domain interfaces (AE and DE).
  • Assessment of cell-death signaling activity and self-association of mutated TIR domains and full-length NLRs.

Main Results:

  • The TIR domain of *Arabidopsis* NLR SNC1 possesses both L6-like (DE) and RPS4-like (AE) self-association interfaces.
  • Mutations in either the AE or DE interface disrupt cell-death signaling and self-association of SNC1, L6, and RPS4 TIR domains and full-length proteins.
  • Both AE and DE interfaces are present in the TIR domain of *Arabidopsis* NLR RPP1.

Conclusions:

  • Both AE and DE self-association interfaces are simultaneously required for the self-association and cell-death signaling function of diverse plant NLRs.
  • This finding highlights a conserved mechanism of TIR domain self-association critical for plant immune receptor function.