Download MendeleyStructure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ.
Martin, R., Qi, T., Zhang, H., Liu, F., King, M., Toth, C., Nogales, E., Staskawicz, B.J.(2020) Science 370
- PubMed: 33273074
- DOI: https://doi.org/10.1126/science.abd9993
- Primary Citation of Related Structures:
7JLU, 7JLV, 7JLX - PubMed Abstract:
Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to Nicotiana benthamiana with a Toll-like interleukin-1 receptor (TIR) domain bound to the Xanthomonas euvesicatoria effector XopQ ( Xanthomonas outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain.
Organizational Affiliation:
Biophysics Graduate Group, University of California, Berkeley, CA 94720, USA.
