Multiple functional self-association interfaces in plant TIR domains

Zhang, Xiaoxiao, Bernoux, Maud, Bentham, Adam R., Newman, Toby E., Ve, Thomas, Casey, Lachlan W., Raaymakers, Tom M., Hu, Jian, Croll, Tristan I., Schreiber, Karl J., Staskawicz, Brian J., Anderson, Peter A., Sohn, Kee Hoon, Williams, Simon J., Dodds, Peter N. and Kobe, Bostjan (2017) Multiple functional self-association interfaces in plant TIR domains. Proceedings of the National Academy of Sciences, 114 10: E2046-E2052. doi:10.1073/pnas.1621248114


Author Zhang, Xiaoxiao
Bernoux, Maud
Bentham, Adam R.
Newman, Toby E.
Ve, Thomas
Casey, Lachlan W.
Raaymakers, Tom M.
Hu, Jian
Croll, Tristan I.
Schreiber, Karl J.
Staskawicz, Brian J.
Anderson, Peter A.
Sohn, Kee Hoon
Williams, Simon J.
Dodds, Peter N.
Kobe, Bostjan
Title Multiple functional self-association interfaces in plant TIR domains
Journal name Proceedings of the National Academy of Sciences   Check publisher's open access policy
ISSN 1091-6490
0027-8424
Publication date 2017-02-03
Year available 2017
Sub-type Article (original research)
DOI 10.1073/pnas.1621248114
Open Access Status Not yet assessed
Volume 114
Issue 10
Start page E2046
End page E2052
Total pages 7
Place of publication Washington, DC, United States
Publisher National Academy of Sciences
Language eng
Subject 1000 General
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.
Formatted 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.
Keyword NLR
TIR domain
Plant disease resistance
Plant immunity
Signaling by cooperative assembly formation
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DP120100685
NSF-IOS-1146793
DE130101292
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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Created: Fri, 10 Feb 2017, 10:41:12 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences