scholarly journals The NLR helper protein NRC3 but not NRC1 is required for Pto-mediated cell death in Nicotiana benthamiana

2015 ◽  
Author(s):  
Chih-Hang Wu ◽  
Khaoula Belhaj ◽  
Tolga O. Bozkurt ◽  
Sophien Kamoun
Keyword(s):  
Cell Death ◽  
Nicotiana Benthamiana ◽  
Rna Silencing ◽  
Genetic Complementation ◽  
Hypersensitive Cell Death ◽  
Immune Receptors ◽  
Disease Resistance Protein ◽  
Resistance Protein ◽  
Solanaceous Plants ◽  
Lrr Protein

Intracellular immune receptors of the nucleotide-binding leucine-rich repeat (NB-LRR or NLR) proteins often function in pairs, with "helper" proteins required for the activity of "sensors" that mediate pathogen recognition. The NLR helper NRC1 (NB-LRR protein required for HR-associated cell death 1) has been described as a signalling hub required for the cell death mediated by both cell surface and intracellular immune receptors in the model plant Nicotiana benthamiana. However, this work predates the availability of the N. benthamiana genome and whether NRC1 is indeed required for the reported phenotypes has not been confirmed. Here, we investigated the NRC family of solanaceous plants using a combination of genome annotation, phylogenetics, gene silencing and genetic complementation experiments. We discovered that a paralog of NRC1, we termed NRC3, is required for the hypersensitive cell death triggered by the disease resistance protein Pto but not Rx and Mi-1.2. NRC3 may also contribute to the hypersensitive cell death triggered by the receptor-like protein Cf-4. Our results highlight the importance of applying genetic complementation to validate gene function in RNA silencing experiments.

scholarly journals Characterization of blast resistance related protein domains in wheat for molecular marker development

2019 ◽  
Vol 17 (2) ◽  
pp. 161-171
Author(s):  
M. Thoihidul Islam ◽  
Mohammad Rashid Arif ◽  
Arif Hasan Khan Robin
Keyword(s):  
Disease Resistance ◽  
Blast Resistance ◽  
Protein Domains ◽  
Protein Domain ◽  
Leucine Rich Repeat ◽  
Related Protein ◽  
Disease Resistance Protein ◽  
Protein Encoding ◽  
Resistance Protein ◽  
Lrr Protein

Wheat blast is a devastating disease which is baffling scientists from its inception. This study characterized the blast resistance related protein domains with a view to develop molecular markers to identify resistant wheat genotypes against Blast fungus Magnaporthe oryzae. A genome browse analysis detected that the candidate resistance gene against blast could be located in several different chromosomes. An in silico analysis was collected with fifty nucleotide-binding site leucine-rich repeat (NBS-LRR), leucine-rich repeat (LRR), pathogenesis and resistance protein-encoding accessions on the basis of the previous resistance report. The phylogenetic tree of those putative resistance accessions, bearing resistance related protein-encoding domains, showed that an NBS-LRR accession JP957107.1 has 67% similarity with the disease resistance protein domain encoding accession of Brazilian resistant cultivar Thatcher. By contrast, the rice blast resistance Pita gene has 72% similarity with 18 pathogenesis protein domain encoding accessions. Among putative protein domains, disease resistance protein of Thatcher has 78% similarity with two NBS-LRR protein domains AAZ99757.1 and AAZ99757.1. Eighteen microsatellite markers were designed from eighteen putative NBS-LRR protein encoding accessions along with Piz3 marker. The 19 markers were unable to separate resistant and susceptible genotypes. Diffused versus conspicuous bands indicated either presence of insertion/deletion (InDel) or single nucleotide polymorphism (SNP) among wheat genotypes. Detection of InDel or SNP markers is a subject of further investigation. Additional markers are needed to be designed using new NBS-LRR, pathogenesis, coiled-coil (CC), translocated intimin receptor (TIR) resistance protein encoding accessions to find out markers specific for blast resistance. J. Bangladesh Agril. Univ. 17(2): 161–171, June 2019

scholarly journals The Chloroplastic Protein THF1 Interacts with the Coiled-Coil Domain of the Disease Resistance Protein N′ and Regulates Light-Dependent Cell Death

2016 ◽  
Vol 171 (1) ◽  
pp. 658-674 ◽  
Author(s):  
Louis-Philippe Hamel ◽  
Ken-Taro Sekine ◽  
Thérèse Wallon ◽  
Yuji Sugiwaka ◽  
Kappei Kobayashi ◽  
...  
Keyword(s):  
Cell Death ◽  
Disease Resistance ◽  
Coiled Coil ◽  
Coiled Coil Domain ◽  
Disease Resistance Protein ◽  
Dependent Cell ◽  
Resistance Protein

scholarly journals XopQ induced stromule formation in Nicotiana benthamiana is causally linked to ETI signaling and depends on ADR1 and NRG1

2021 ◽  
Author(s):  
Jennifer Prautsch ◽  
Jessica L. Erickson ◽  
Sedef Özyürek ◽  
Rahel Gormannns ◽  
Lars Franke ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Nicotiana Benthamiana ◽  
Double Mutant ◽  
Plant Immunity ◽  
Signaling Cascade ◽  
Nuclear Dynamics ◽  
Hypersensitive Cell Death ◽  
Host Cell Death ◽  
Dependent Cell

In Nicotiana benthamiana, expression of the Xanthomonas effector XopQ triggers ROQ1-dependent ETI responses and in parallel accumulation of plastids around the nucleus and the formation of stromules. Both processes were proposed to contribute to ETI-related hypersensitive cell death and thereby to plant immunity. Whether these reactions are directly connected to ETI signaling events has not been tested. Here we utilized transient expression experiments to determine whether XopQ-mediated plastid reactions are a result of XopQ perception by ROQ1 or a consequence of XopQ virulence activity. We find that N. benthamiana mutants lacking ROQ1, both RNLs (NRG1 and ADR1) or EDS1, fail to elicit XopQ-dependent host cell death and stromule formation. Mutants lacking only NRG1 lost XopQ-dependent cell death but retained some stromule induction that was abolished in the RNL double mutant. This analysis aligns XopQ-induced stromules with the ETI signaling cascade but not to host programmed cell death. Furthermore, data reveal that XopQ-triggered plastid clustering is not strictly linked to stromule formation during ETI. Our data suggest that stromule formation, in contrast to chloroplast peri-nuclear dynamics, is an integral part of the N. benthamiana ETI response and that both RNL sub-types play a role in this ETI response.

scholarly journals A Sec-Dependent Secretory Protein of the Huanglongbing-Associated Pathogen Suppresses Hypersensitive Cell Death in Nicotiana benthamiana

2020 ◽  
Vol 11 ◽  
Author(s):  
Chao Zhang ◽  
Peixiu Du ◽  
Hailin Yan ◽  
Zongcai Zhu ◽  
Xuefeng Wang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cell Death ◽  
Pseudomonas Syringae ◽  
Nicotiana Benthamiana ◽  
Transcriptome Profiling ◽  
Secretory Protein ◽  
Hypersensitive Cell Death ◽  
Challenge Inoculation ◽  
Transient Overexpression ◽  
Shock Proteins

“Candidatus Liberibacter asiaticus” (CLas) is a phloem-restricted Gram-negative bacterium that is the causal agent of citrus huanglongbing (HLB). In this study, we identified a CLas-encoded Sec-dependent secretory protein CLIBASIA_04405 that could contribute to the pathogenicity of this bacterium. The gene expression level of CLIBASIA_04405 was significantly higher in citrus than in psyllids. Transient overexpression of the mature CLIBASIA_04405 protein (m4405) in Nicotiana benthamiana leaves could suppress hypersensitive response (HR)-based cell death and H2O2 accumulation triggered by the mouse BAX and the Phytophthora infestans INF1. An alanine-substitution mutagenesis assay revealed the essential of amino acid clusters EKR45–47 and DE64–65 in cell death suppression. Challenge inoculation of the transgenic N. benthamiana-expressing m4405 with Pseudomonas syringae DC3000ΔhopQ1-1 demonstrated the greatly reduced bacterial proliferation. Remarkably, transcriptome profiling and RT-qPCR analysis disclosed that the gene expression of six small heat shock proteins (sHSPs), a set of plant defense regulators, were significantly elevated in the transgenic m4405 lines compared with those in wild-type N. benthamiana. In addition, the transgenic m4405 lines displayed phenotypes of dwarfism and leaf deformation. Altogether, these data indicated that m4405 was a virulence factor of CLas.

scholarly journals Multiple functional self-association interfaces in plant TIR domains

2017 ◽  
Vol 114 (10) ◽  
pp. E2046-E2052 ◽  
Author(s):  
Xiaoxiao Zhang ◽  
Maud Bernoux ◽  
Adam R. Bentham ◽  
Toby E. Newman ◽  
Thomas Ve ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cell Death ◽  
Interleukin 1 ◽  
Tir Domain ◽  
Disease Resistance Protein ◽  
Resistance Protein ◽  
Cell Death Signaling ◽  
Self Association ◽  
Tir Domains ◽  
Diverse Plant

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 fromArabidopsis. Here we show that the crystal structure of the TIR domain from theArabidopsisNLR 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 theArabidopsisNLR recognition ofPeronospora parasitica1 (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.

scholarly journals Tomato Prf requires NLR helpers NRC2 and NRC3 to confer resistance against the bacterial speck pathogen Pseudomonas syringae pv. tomato

2019 ◽  
Author(s):  
Chih-Hang Wu ◽  
Sophien Kamoun
Keyword(s):  
Cell Death ◽  
Pseudomonas Syringae ◽  
Effector Proteins ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Hypersensitive Cell Death ◽  
Tomato Production ◽  
Bacterial Speck ◽  
Solanaceous Plants ◽  
Pto Kinase

AbstractBacterial speck, caused by the pathogen Pseudomonas syringae pv. tomato, is one of the most common diseases in tomato production. Together with Pto kinase, the NLR (nucleotide-binding domain leucine-rich repeat containing) protein Prf confers resistance against the bacterial speck pathogen by recognizing AvrPto and AvrPtoB, two Type III effector proteins secreted by P. syringae pv. tomato. This Prf/Pto pathway is part of a complex NLR network in solanaceous plants that mediates resistance to diverse pathogens through the helper NLR proteins NRCs (NLR required for cell death). We previously showed that, in Nicotiana benthamiana, the hypersensitive cell death elicited by expression of AvrPto and Pto, which activate immunity through the endogenous Prf ortholog NbPrf, requires functionally redundant NRC2 and NRC3. However, whether tomato (Solanum lycopersicum) Prf (SlPrf) confers resistance to the bacterial speck pathogen through NRC2 and NRC3 has not been determined. In this study, we show that SlPrf requires NRC2 and NRC3 to trigger hypersensitive cell death and disease resistance in both N. benthamiana and tomato. We found that the hypersensitive cell death induced by AvrPtoB/Pto/SlPrf in N. benthamiana is compromised when NRC2 and NRC3 are silenced, indicating that SlPrf is an NRC2/3-dependent NLR. We validated this finding by showing that silencing NRC2 and NRC3 in the bacterial speck resistant tomato ‘Rio Grande 76R’ compromised Prf-mediated resistance. These results indicate that the NRC network extends beyond N. benthamiana to solanaceous crops.

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