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  • Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor

    Author(s)
    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
    Jones, Jonathan DG
    Griffith University Author(s)
    Ve, Thomas
    Year published
    2014
    Metadata
    Show full item record
    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 ...
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    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.
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    Journal Title
    Science
    Volume
    344
    Issue
    6181
    DOI
    https://doi.org/10.1126/science.1247357
    Subject
    Biochemistry and cell biology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/173334
    Collection
    • Journal articles

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