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; Lu, Jiang; Bodén, Mikael; Dry, Ian B.; Kobe, Boštjan

doi:10.3389/fpls.2016.01850

Cited by 45 publications

(48 citation statements)

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“…Self-association of both TIR (8, 9, 11, 15) and CC (10,13,16,17) domains has been shown to be important for the signaling function. In animal NLRs, the formation of postactivation oligomeric complexes, such as the NLRC4/NAIP inflammasome or the APAF1 apoptosome, is important for bringing together N-terminal domains into a signaling platform (18)(19)(20), but there is yet little evidence for such signaling complexes in plants.Several crystal structures of plant TIR domains have been reported (9,11,(21)(22)(23)(24). These structures reveal a similar overall structure, which consists of a flavodoxin-like fold containing a central parallel β-sheet surrounded by α-helices.…”

mentioning

confidence: 78%

“…Several crystal structures of plant TIR domains have been reported (9,11,(21)(22)(23)(24). These structures reveal a similar overall structure, which consists of a flavodoxin-like fold containing a central parallel β-sheet surrounded by α-helices.…”

mentioning

confidence: 78%

“…Whereas in mammalian TIR domains no common trends have emerged among the available crystals structures in terms of protein-protein association (21), most plant TIR-domain crystal structures feature structurally analogous AE interfaces (Figs. 1B and 5B) (23). The exception is L6 TIR , the crystal structure of which features the DE but not the AE interface.…”

Section: Discussionmentioning

confidence: 99%

“…TIR from Mirabilis rotundifolia; no self-association of this protein could be detected in solution or yeast, but nevertheless, mutations within the predicted AE-and DE-interface regions suppressed its cell-death signaling function (23). All of the TIR:TIR domain interactions studied to date are weak and transient, with the exception of the heterodimer association between RRS1 TIR and RPS4 TIR , which appears to play an inhibitory rather than signaling role.…”

Section: Tirmentioning

confidence: 99%

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Multiple functional self-association interfaces in plant TIR domains

Zhang

Bernoux

Bentham

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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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 TIRdomain 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. Selfassociation 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.plant immunity | NLR | TIR domain | plant disease resistance | signaling by cooperative assembly formation P lants have evolved a sophisticated innate immune system to detect pathogens, in which plant resistance (R) proteins recognize pathogen proteins (effectors) in a highly specific manner. This recognition leads to the effector-triggered immunity (ETI) response that often induces a localized cell death known as the hypersensitive response (1). Most R proteins belong to the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family. NLRs are prevalent in the immune systems of plants and animals and provide resistance to a broad range of pathogens, including fungi, oomycetes, bacteria, viruses, and insects (2, 3). NLRs contain a central nucleotide-binding (NB) domain, often referred to as the nucleotide-binding adaptor shared by APAF-1, resistance proteins, and CED-4 (NB-ARC domain) (4) and a C-terminal leucine-rich repeat (LRR) domain. Plant NLRs can be further classified into two main subfamilies, depending on the presence of either a Toll/interleukin-1 receptor domain (TIR-NLR) or a coiled-coil domain (CC-NLR) at their N termini (5).The CC and TIR domains of many plant NLRs can autonomously signal cell-death responses when expressed ectopically in planta, and mutations in these domains within full-length proteins also compromise signaling, suggesting that these domains are responsible for propagating the resistance signal after activation of the receptor (6-14). Self-association of both TIR (8, 9, 11, 15) and CC (10,13,16,17) domains has been shown to be important for the signaling function. In animal NLRs, the formation of postactivation oligomeric complexes, such as the NLRC4/NAIP inflammasome or...

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mentioning

confidence: 78%

mentioning

confidence: 78%

Section: Discussionmentioning

confidence: 99%

Section: Tirmentioning

confidence: 99%

See 2 more Smart Citations

Multiple functional self-association interfaces in plant TIR domains

Zhang

Bernoux

Bentham

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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114

138

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“…In the aspect of structure, the main features of the LRR genes are their structural domain of 20-30 aa and their transmembrane domain containing 2-42 LRRs [14]. Previous studies showed that the LRR domain provides a versatile structural framework for protein-protein interactions and allows proteins to act as molecular switches in relation to pathogen recognition and defense activation [15,16].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and expression analysis of pitaya (Hylocereus polyrhizus) HpLRR genes in response to Neoscytalidium dimidiatum infection

Liu

et al. 2020

BMC Plant Biol

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Background: Canker disease caused by Neoscytalidium dimidiatum is a devastating disease resulting in a major loss to the pitaya industry. However, resistance proteins in plants play crucial roles to against pathogen infection. Among resistance proteins, the leucine-rich repeat (LRR) protein is a major family that plays crucial roles in plant growth, development, and biotic and abiotic stress responses, especially in disease defense. Results: In the present study, a transcriptomics analysis identified a total of 272 LRR genes, 233 of which had coding sequences (CDSs), in the plant pitaya (Hylocereus polyrhizus) in response to fungal Neoscytalidium dimidiatum infection. These genes were divided into various subgroups based on specific domains and phylogenetic analysis. Molecular characterization, functional annotation of proteins, and an expression analysis of the LRR genes were conducted. Additionally, four LRR genes (CL445.Contig4_All, Unigene28_All, CL28.Contig2_All, and Unigene2712_All, which were selected because they had the four longest CDSs were further assessed using quantitative reverse transcription PCR (qRT-PCR) at different fungal infection stages in different pitaya species (Hylocereus polyrhizus and Hylocereus undatus), in different pitaya tissues, and after treatment with salicylic acid (SA), methyl jasmonate (MeJA), and abscisic acid (ABA) hormones. The associated protein functions and roles in signaling pathways were identified. Conclusions: This study provides a comprehensive overview of the HpLRR family genes at transcriptional level in pitaya in response to N. dimidiatum infection, it will be helpful to understand the molecular mechanism of pitaya canker disease, and lay a strong foundation for further research.

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Death, TIR, and RHIM: Self-assembling domains involved in innate immunity and cell-death signaling

Nanson

Kobe

2018

Journal of Leukocyte Biology

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The innate immune system consists of pattern recognition receptors (PRRs) that detect pathogenand endogenous danger-associated molecular patterns (PAMPs and DAMPs), initiating signaling pathways that lead to the induction of cytokine expression, processing of pro-inflammatory cytokines, and induction of cell-death responses. An emerging concept in these pathways and associated processes is signaling by cooperative assembly formation (SCAF), which involves formation of higher order oligomeric complexes, and enables rapid and strongly amplified signaling responses to minute amounts of stimulus. Many of these signalosomes assemble through homotypic interactions of members of the death-fold (DF) superfamily, Toll/IL-1 receptor (TIR) domains, or the RIP homotypic interaction motifs (RHIM). We review the current understanding of the structure and function of these domains and their molecular interactions with a particular focus on higher order assemblies.

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Structure and Function of the TIR Domain from the Grape NLR Protein RPV1

Cited by 45 publications

References 44 publications

Multiple functional self-association interfaces in plant TIR domains

Multiple functional self-association interfaces in plant TIR domains

Molecular characterization and expression analysis of pitaya (Hylocereus polyrhizus) HpLRR genes in response to Neoscytalidium dimidiatum infection

Death, TIR, and RHIM: Self-assembling domains involved in innate immunity and cell-death signaling

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