The soybean-Phytophthora resistance locus Rps1-k encompasses coiled coil-nucleotide binding-leucine rich repeat-like genes and repetitive sequences

A series of single genes protect soybean from the root and stem disease caused by the oomycete pathogen Phytophthora sojae. In the last two decades, Rps1-k has been the most stable and widely used Phytophthora resistance gene for the major soybean-producing regions of the United States. Four highly similar genes encoding coiled coil-nucleotide binding-leucine rich repeat (CC-NB-LRR)-type proteins were isolated from the Rps1-k locus. These genes were grouped into two classes based on their sequence identity. Class I contains three genes with identical open reading frames (ORF) and 5′ end regions. Two of these genes were also identical at the 3′ untranslated regions; the third gene showed a recombination breakpoint in the 3′ untranslated region resulting in the combination of 3′ end sequences of members from both classes. Reverse transcription-polymerase chain reaction analyses suggested that members of both classes of genes are transcribed at low levels. Representative members from each gene class were expressed in transgenic soybean plants. Analyses of independent R0, R1, R2, and R3 progeny populations suggested that both gene classes confer Phytophthora resistance in soybean. A possible evolutionary mechanism for the Class I gene family is proposed.

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Molecular characterization and functional analysis of CzR1, a coiled-coil-nucleotide-binding-site-leucine-rich repeat R-gene from Curcuma zedoaria Loeb. that confers resistance to Pythium aphanidermatum

Physiological and Molecular Plant Pathology ◽

10.1016/j.pmpp.2013.05.003 ◽

2013 ◽

Vol 83 ◽

pp. 59-68 ◽

Cited By ~ 13

Author(s):

Basudeba Kar ◽

Satyabrata Nanda ◽

Pradeep Kumar Nayak ◽

Sanghamitra Nayak ◽

Raj Kumar Joshi

Keyword(s):

Functional Analysis ◽

Binding Site ◽

Molecular Characterization ◽

Coiled Coil ◽

Nucleotide Binding ◽

Pythium Aphanidermatum ◽

Nucleotide Binding Site ◽

R Gene ◽

Leucine Rich Repeat ◽

Curcuma Zedoaria

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The in Silico Map-Based Cloning of Pi36, a Rice Coiled-Coil–Nucleotide-Binding Site–Leucine-Rich Repeat Gene That Confers Race-Specific Resistance to the Blast Fungus

Genetics ◽

10.1534/genetics.107.075465 ◽

2007 ◽

Vol 176 (4) ◽

pp. 2541-2549 ◽

Cited By ~ 139

Author(s):

Xinqiong Liu ◽

Fei Lin ◽

Ling Wang ◽

Qinghua Pan

Keyword(s):

Binding Site ◽

In Silico ◽

Specific Resistance ◽

Coiled Coil ◽

Nucleotide Binding ◽

Nucleotide Binding Site ◽

Leucine Rich Repeat ◽

Blast Fungus

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Dissection of Cell Death Induction by Wheat Stem Rust Resistance Protein Sr35 and Its Matching Effector AvrSr35

Molecular Plant-Microbe Interactions ◽

10.1094/mpmi-08-19-0216-r ◽

2020 ◽

Vol 33 (2) ◽

pp. 308-319 ◽

Cited By ~ 2

Author(s):

Stephen Bolus ◽

Eduard Akhunov ◽

Gitta Coaker ◽

Jorge Dubcovsky

Keyword(s):

Cell Death ◽

Transient Expression ◽

Stem Rust ◽

Fluorescent Protein ◽

Coiled Coil ◽

Nucleotide Binding ◽

Leucine Rich Repeat ◽

Wheat Stem Rust ◽

Pathogen Effector ◽

Lrr Domain

Nucleotide-binding leucine-rich repeat receptors (NLRs) are the most abundant type of immune receptors in plants and can trigger a rapid cell-death (hypersensitive) response upon sensing pathogens. We previously cloned the wheat NLR Sr35, which encodes a coiled-coil (CC) NLR that confers resistance to the virulent wheat stem rust race Ug99. Here, we investigated Sr35 signaling after Agrobacterium-mediated transient expression in Nicotiana benthamiana. Expression of Sr35 in N. benthamiana leaves triggered a mild cell-death response, which is enhanced in the autoactive mutant Sr35 D503V. The N-terminal tagging of Sr35 with green fluorescent protein (GFP) blocked the induction of cell death, whereas a C-terminal GFP tag did not. No domain truncations of Sr35 generated cell-death responses as strong as the wild type, but a truncation including the NB-ARC (nucleotide binding adaptor) shared by APAF-1, R proteins, and CED-4 domains in combination with the D503V autoactive mutation triggered cell death. In addition, coexpression of Sr35 with the matching pathogen effector protein AvrSr35 resulted in robust cell death and electrolyte leakage levels that were similar to autoactive Sr35 and significantly higher than Sr35 alone. Coexpression of Sr35-CC-NB-ARC and AvrSr35 did not induce cell death, confirming the importance of the leucine-rich repeat (LRR) domain for AvrSr35 recognition. These findings were confirmed through Agrobacterium-mediated transient expression in barley. Taken together, these results implicate the CC-NB-ARC domains of Sr35 in inducing cell death and the LRR domain in AvrSr35 recognition. [Formula: see text] Copyright © 2020 The Author(s). This is an open access article distributed under the CC BY 4.0 International license .

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RicePi5-Mediated Resistance toMagnaporthe oryzaeRequires the Presence of Two Coiled-Coil–Nucleotide-Binding–Leucine-Rich Repeat Genes

Genetics ◽

10.1534/genetics.108.099226 ◽

2009 ◽

Vol 181 (4) ◽

pp. 1627-1638 ◽

Cited By ~ 176

Author(s):

Sang-Kyu Lee ◽

Min-Young Song ◽

Young-Su Seo ◽

Hye-Kyung Kim ◽

Seho Ko ◽

...

Keyword(s):

Coiled Coil ◽

Nucleotide Binding ◽

Leucine Rich Repeat

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TIR-only protein RBA1 recognizes a pathogen effector to regulate cell death inArabidopsis

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1620973114 ◽

2017 ◽

Vol 114 (10) ◽

pp. E2053-E2062 ◽

Cited By ~ 55

Author(s):

Marc T. Nishimura ◽

Ryan G. Anderson ◽

Karen A. Cherkis ◽

Terry F. Law ◽

Qingli L. Liu ◽

...

Keyword(s):

Cell Death ◽

Immune System ◽

Pasteurella Multocida ◽

Coiled Coil ◽

Nucleotide Binding ◽

Leucine Rich Repeat ◽

Multidomain Structure ◽

Pathogen Effector ◽

Self Association ◽

And Function

Detection of pathogens by plants is mediated by intracellular nucleotide-binding site leucine-rich repeat (NLR) receptor proteins. NLR proteins are defined by their stereotypical multidomain structure: an N-terminal Toll–interleukin receptor (TIR) or coiled-coil (CC) domain, a central nucleotide-binding (NB) domain, and a C-terminal leucine-rich repeat (LRR). The plant innate immune system contains a limited NLR repertoire that functions to recognize all potential pathogens. We isolated Response to the bacterial type III effector protein HopBA1 (RBA1), a gene that encodes a TIR-only protein lacking all other canonical NLR domains. RBA1 is sufficient to trigger cell death in response to HopBA1. We generated a crystal structure for HopBA1 and found that it has similarity to a class of proteins that includes esterases, the heme-binding protein ChaN, and an uncharacterized domain ofPasteurella multocidatoxin. Self-association, coimmunoprecipitation with HopBA1, and function of RBA1 require two previously identified TIR–TIR dimerization interfaces. Although previously described as distinct in other TIR proteins, in RBA1 neither of these interfaces is sufficient when the other is disrupted. These data suggest that oligomerization of RBA1 is required for function. Our identification of RBA1 demonstrates that “truncated” NLRs can function as pathogen sensors, expanding our understanding of both receptor architecture and the mechanism of activation in the plant immune system.

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