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Poster

Session: Session 1 Presenting Authors at Posters (Odds)

P-085 - Structure determinants of DANGEROUS MIX 3, an alpha/beta hydrolase, for triggering NLR-mediated genetic incompatibility in plants

Monday, July 14, 2025
13:30 - 15:15  
Location: Confex Hall 3
Extracellular & Intracellular non-self recognition & signaling

    Presenting Author(s)

  • WW

    Wei-Lin Wan (he/him/his)

    Dr.
    Natl Univ of Singapore
    Singapore, Singapore

    • Author(s)

  • GK

    Gijeong Kim

    Institute of Plant and Microbial Biology, University of Zurich
    Zurich, Zurich, Switzerland

  • NK

    Nayun Kim

    Korea Advanced Institute of Science and Technology
    Daejeon, Ch'ungch'ong-namdo, Republic of Korea

  • YT

    Yi Yun Tan

    National University of Singapore
    Singapore, Singapore

  • NC

    Nuri Charoennit

    National University of Singapore
    Singapore, Singapore

  • RL

    Rachelle R. Q. Lee

    National University of Singapore
    Singapore, Singapore

  • YL

    Yin Yin Liew

    National University of Singapore
    Singapore, Singapore

  • SN

    Shen Kai Ng

    National University of Singapore
    Singapore, Singapore

  • YZ

    Yizhong Zhang

    National University of Singapore
    Singapore, Singapore

  • JS

    Ji-Joon Song

    Korea Advanced Institute of Science and Technology
    Daejeon, Ch'ungch'ong-namdo, Republic of Korea

  • EC

    Eunyoung Chae

    University of Oxford
    Oxford, England, United Kingdom

Genetic incompatibility occurs when a mismatched pair of plant immune components mounts autoimmune responses in hybrids. Highly diversified NLR receptors are main culprits of the genetic conflict, recognizing host proteins from different origin as immune trigger. Here, we report the molecular mechanism underlying a DANGEROUS MIX (DM) autoimmunity, comprising DM2h/RPP1 NLR and its incompatible partner DM3, an alpha/beta hydrolase. Cryo-electron microscopy reveals the oligomeric nature of two natural DM3 variants in a trimer of dimer configuration. The polymorphism triggering autoimmunity is located at the dimer interface, resulting in drastic structural differences such that dimerizing helix and loop reinforcing the interface is lost and disordered. Structure-function analysis shows that integrity of the dimer interface, but neither maintenance of hexamer nor its enzymatic activity, is the key factor contributing to autoimmunity. Our finding pinpoints checkpoints embedded in the oligomeric configuration of a host enzyme that controls the switching mechanism of NLR activity.