Multiple Functional Self-Association Interfaces in Plant TIR Domains

Xiaoxiao Zhang, Maud Bernoux, Adam Bentham, Toby Newman, Thomas Ve, Lachlan Casey, Tom Raaymakers, Jian Hu, Tristan Croll, Karl Schreiber, Brian Staskawicz, Peter Anderson, Kee Sohn, Simon Williams, Peter Dodds, Bostjan Kobe

    Research output: Contribution to journalArticlepeer-review

    101 Citations (Scopus)


    The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Arabidopsis. Here we show that the crystal structure of the TIR domain from the Arabidopsis NLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from the Arabidopsis NLR recognition of Peronospora parasitica 1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs.

    Original languageEnglish
    Pages (from-to)E2046-E2052
    Number of pages7
    JournalProceedings of the National Academy of Sciences of the United States of America
    Issue number10
    Early online date2017
    Publication statusPublished - 7 Mar 2017


    • NLR
    • Plant disease resistance
    • Plant immunity
    • Signaling by cooperative assembly formation
    • TIR domain


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