4c6t
Crystal structure of the RPS4 and RRS1 TIR domain heterodimerCrystal structure of the RPS4 and RRS1 TIR domain heterodimer
Structural highlights
Publication Abstract from PubMedCytoplasmic 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. Structural basis for assembly and function of a heterodimeric plant immune receptor.,Williams SJ, Sohn KH, Wan L, Bernoux M, Sarris PF, Segonzac C, Ve T, Ma Y, Saucet SB, Ericsson DJ, Casey LW, Lonhienne T, Winzor DJ, Zhang X, Coerdt A, Parker JE, Dodds PN, Kobe B, Jones JD Science. 2014 Apr 18;344(6181):299-303. doi: 10.1126/science.1247357. PMID:24744375[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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