Structural studies of signalling domains from plant NLRs.
A. Bentham (1), X. Zhang (2), L. Casey (3), P. Lavrencic (2), S. Cesari (4), D. Ericsson (5), P. Anderson (1), M. Mobli (6), M. Bernoux (4), P. Dodds (4), B. Kobe (2), S. Williams (7) (1) School of Biological Sciences, Flinders University, Australia; (2) School of Chemistry and Molecular Biosciences, University of Queensland, Australia; (3) School of Chemistry and Molecular Biosciences, University of Queensland, Australia; (4) CSIRO Agriculture Flagship, Australia; (5) MX Beamlines, Australian Synchrotron, Australia; (6) Centre for Advanced Imaging, University of Queensland, Australia; (7) Research School of Biology, Australian National University, Australia

Plant nucleotide-binding oligomerisation domain (NOD)-like receptors (NLRs) recognise specific pathogen effector proteins and initiate immune responses. Their multi-domain architecture includes a central nucleotide-binding domain, a C-terminal leucine-rich repeat and either a N-terminal coiled-coil (CC) or Toll–interleukin-1 receptor/resistance (TIR) domain. The CC and TIR domains are involved in defence signalling and have been implicated in homotypic interactions to facilitate defence responses. We have now solved a number of structures of both CC (Sr33 and Mla10) and TIR (SNC1 and RPP1) domains from plant NLRs. Our subsequent structural and biophysical investigations of these domains suggest that for TIR domains two previously identified interfaces may cooperate to facilitate self-association and signalling. In addition our studies of CC domains, suggest that regions outside of those that have been structurally determined previously are involved in self-association. These recent findings contribute new and alternative insights into our structural and functional understanding of the signalling domain from plant NLR proteins.

Abstract Number: C24-3, P17-650
Session Type: Concurrent