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 The Coiled-Coil and Nucleotide Binding Domains of the Potato Rx Disease Resistance Protein Function in Pathogen Recognition and Signaling

2008 ◽  
Vol 20 (3) ◽  
pp. 739-751 ◽  
Author(s):  
Gregory J. Rairdan ◽  
Sarah M. Collier ◽  
Melanie A. Sacco ◽  
Thomas T. Baldwin ◽  
Teresa Boettrich ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Protein Function ◽  
Coiled Coil ◽  
Nucleotide Binding ◽  
Pathogen Recognition ◽  
Binding Domains ◽  
Disease Resistance Protein ◽  
Resistance Protein

scholarly journals Uncoupling Salicylic Acid-Dependent Cell Death and Defense-Related Responses From Disease Resistance in the Arabidopsis Mutant acd5

Genetics ◽  
2000 ◽  
Vol 156 (1) ◽  
pp. 341-350
Author(s):  
Jean T Greenberg ◽  
F Paul Silverman ◽  
Hua Liang
Keyword(s):  
Cell Death ◽  
Salicylic Acid ◽  
Disease Resistance ◽  
Pseudomonas Syringae ◽  
Higher Plants ◽  
Ethylene Signaling ◽  
Symptom Development ◽  
Wild Type ◽  
Dependent Cell ◽  
Arabidopsis Mutant

Abstract Salicylic acid (SA) is required for resistance to many diseases in higher plants. SA-dependent cell death and defense-related responses have been correlated with disease resistance. The accelerated cell death 5 mutant of Arabidopsis provides additional genetic evidence that SA regulates cell death and defense-related responses. However, in acd5, these events are uncoupled from disease resistance. acd5 plants are more susceptible to Pseudomonas syringae early in development and show spontaneous SA accumulation, cell death, and defense-related markers later in development. In acd5 plants, cell death and defense-related responses are SA dependent but they do not confer disease resistance. Double mutants with acd5 and nonexpressor of PR1, in which SA signaling is partially blocked, show greatly attenuated cell death, indicating a role for NPR1 in controlling cell death. The hormone ethylene potentiates the effects of SA and is important for disease symptom development in Arabidopsis. Double mutants of acd5 and ethylene insensitive 2, in which ethylene signaling is blocked, show decreased cell death, supporting a role for ethylene in cell death control. We propose that acd5 plants mimic P. syringae-infected wild-type plants and that both SA and ethylene are normally involved in regulating cell death during some susceptible pathogen infections.

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 Subfamily-Specific Specialization of RGH1/MLA Immune Receptors in Wild Barley

2019 ◽  
Vol 32 (1) ◽  
pp. 107-119 ◽  
Author(s):  
Takaki Maekawa ◽  
Barbara Kracher ◽  
Isabel M. L. Saur ◽  
Makoto Yoshikawa-Maekawa ◽  
Ronny Kellner ◽  
...  
Keyword(s):  
Cell Death ◽  
Disease Resistance ◽  
Geographic Origin ◽  
Coiled Coil ◽  
Hordeum Spontaneum ◽  
R Gene ◽  
Powdery Mildew Fungus ◽  
Signaling Domain ◽  
Pathogen Populations ◽  
Signaling Domains

The barley disease resistance (R) gene locus mildew locus A (Mla) provides isolate-specific resistance against the powdery mildew fungus Blumeria graminis hordei and has been introgressed into modern cultivars from diverse germplasms, including the wild relative Hordeum spontaneum. Known Mla disease resistance specificities to B. graminis hordei appear to encode allelic variants of the R gene homolog 1 (RGH1) family of nucleotide-binding domain and leucine-rich repeat (NLR) proteins. Here, we sequenced and assembled the transcriptomes of 50 H. spontaneum accessions representing nine populations distributed throughout the Fertile Crescent. The assembled Mla transcripts exhibited rich sequence diversity, linked neither to geographic origin nor population structure, and could be grouped into two similar-sized subfamilies based on two major N-terminal coiled-coil (CC) signaling domains that are both capable of eliciting cell death. The presence of positively selected sites located mainly in the C-terminal leucine-rich repeats of both MLA subfamilies, together with the fact that both CC signaling domains mediate cell death, implies that the two subfamilies are actively maintained in the population. Unexpectedly, known MLA receptor variants that confer B. graminis hordei resistance belong exclusively to one subfamily. Thus, signaling domain divergence, potentially as adaptation to distinct pathogen populations, is an evolutionary signature of functional diversification of an immune receptor. [Formula: see text] Copyright © 2018 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license .

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