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Multiple functional self-association interfaces in plant TIR domains
Zhang, Xiaoxiao,Bernoux, Maud,Bentham, Adam R.,Newman, Toby E.,Ve, Thomas,Casey, Lachlan W.,Raaymakers, Tom M.,Hu, Jian,Croll, Tristan I.,Schreiber, Karl J.,Staskawicz, Brian J.,Anderson, Peter A.,Soh National Academy of Sciences 2017 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.114 No.10
<P>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 alpha D and alpha E (DE interface) and an RPS4-like interface involving helices alpha A and alpha E (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.</P>
Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor
Williams, Simon J.,Sohn, Kee Hoon,Wan, Li,Bernoux, Maud,Sarris, Panagiotis F.,Segonzac, Cecile,Ve, Thomas,Ma, Yan,Saucet, Simon B.,Ericsson, Daniel J.,Casey, Lachlan W.,Lonhienne, Thierry,Winzor, Dona American Association for the Advancement of Scienc 2014 Science Vol.344 No.6181
<P><B>Universal Immune Function</B></P><P>Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of <I>Arabidopsis</I> receptors, <B>Williams <I>et al.</I></B> (p. 299; see the Perspective by <B>Nishimura and Dangl</B>) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest the molecular mechanisms may translate broadly.</P>