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.
journal_name
Proc Natl Acad Sci U S Aauthors
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 Bdoi
10.1073/pnas.1621248114subject
Has Abstractpub_date
2017-03-07 00:00:00pages
E2046-E2052issue
10eissn
0027-8424issn
1091-6490pii
1621248114journal_volume
114pub_type
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