Structure and function of the TIR domain from the grape NLR protein RPV1

Williams, Simon J., Yin, Ling, Foley, Gabriel, Casey, Lachlan W., Outram, Megan A., Ericsson, Daniel J., Lu, Jiang, Boden, Mikael, Dry, Ian B. and Kobe, Bostjan (2016) Structure and function of the TIR domain from the grape NLR protein RPV1. Frontiers in Plant Science, 7 DECEMBER2016: . doi:10.3389/fpls.2016.01850


Author Williams, Simon J.
Yin, Ling
Foley, Gabriel
Casey, Lachlan W.
Outram, Megan A.
Ericsson, Daniel J.
Lu, Jiang
Boden, Mikael
Dry, Ian B.
Kobe, Bostjan
Title Structure and function of the TIR domain from the grape NLR protein RPV1
Journal name Frontiers in Plant Science   Check publisher's open access policy
ISSN 1664-462X
Publication date 2016-12-08
Sub-type Article (original research)
DOI 10.3389/fpls.2016.01850
Open Access Status DOI
Volume 7
Issue DECEMBER2016
Total pages 13
Place of publication Lausanne, Switzerland
Publisher Frontiers Research Foundation
Language eng
Formatted abstract
The N-terminal Toll/interleukin-1 receptor/resistance protein (TIR) domain has been shown to be both necessary and sufficient for defense signaling in the model plants flax and Arabidopsis. In examples from these organisms, TIR domain self-association is required for signaling function, albeit through distinct interfaces. Here, we investigate these properties in the TIR domain containing resistance protein RPV1 from the wild grapevine Muscadinia rotundifolia. The RPV1 TIR domain, without additional flanking sequence present, is autoactive when transiently expressed in tobacco, demonstrating that the TIR domain alone is capable of cell-death signaling. We determined the crystal structure of the RPV1 TIR domain at 2.3 Å resolution. In the crystals, the RPV1 TIR domain forms a dimer, mediated predominantly through residues in the αA and αE helices (“AE” interface). This interface is shared with the interface discovered in the dimeric complex of the TIR domains from the Arabidopsis RPS4/RRS1 resistance protein pair. We show that surface-exposed residues in the AE interface that mediate the dimer interaction in the crystals are highly conserved among plant TIR domain-containing proteins. While we were unable to demonstrate self-association of the RPV1 TIR domain in solution or using yeast 2-hybrid, mutations of surface-exposed residues in the AE interface prevent the cell-death autoactive phenotype. In addition, mutation of residues known to be important in the cell-death signaling function of the flax L6 TIR domain were also shown to be required for RPV1 TIR domain mediated cell-death. Our data demonstrate that multiple TIR domain surfaces control the cell-death function of the RPV1 TIR domain and we suggest that the conserved AE interface may have a general function in TIR-NLR signaling.
Keyword Nucleotide-binding oligomerisation domain (NOD)-like receptor (NLR)
Toll/interleukin-1 receptor (TIR)
Muscadinia rotundifolia
Plasmopara viticola
Grapevine downy mildew
Plant disease resistance
X-ray crystallography
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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