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, Donald J., Zhang, Xiaoxiao, Coerdt, Anne, Parker, Jane E., Dodds, Peter N., Kobe, Bostjan and Jones, Jonathan D. G. (2014) Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor. Science, 344 (6181). pp. 299-303. ISSN 0036-8075

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Abstract

Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll–interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: Pure Connector
Date Deposited: 28 Apr 2016 09:01
Last Modified: 06 Nov 2019 15:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/58461
DOI: 10.1126/science.1247357

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