Multiple functional self-association interfaces in plant TIR domains.

Abstract:

: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 αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (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.

authors

Zhang X,Bernoux M,Bentham AR,Newman TE,Ve T,Casey LW,Raaymakers TM,Hu J,Croll TI,Schreiber KJ,Staskawicz BJ,Anderson PA,Sohn KH,Williams SJ,Dodds PN,Kobe B

doi

10.1073/pnas.1621248114

subject

Has Abstract

pub_date

2017-03-07 00:00:00

pages

E2046-E2052

issue

10

eissn

0027-8424

issn

1091-6490

pii

1621248114

journal_volume

114

pub_type

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