The TIR–NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response

Gao, Jun; Sasaki, Nobumitsu; Kitano, Hiromi; Konagaya, Ken Ichi; Takizawa, Kaori; Hayashi, Naomi; Okano, Yosuke; Kasahara, Masahiro; Matsushita, Yasuhiko; Nyunoya, Hiroshi

doi:10.1016/j.pmpp.2007.11.002

Cited by 18 publications

(8 citation statements)

References 24 publications

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“…Finally, it should be noted that a functional combination of N‐ and C‐terminal LRRs also needs a fitting ARC2 domain for optimal function: PM3B‐D NB‐ARC and PM3D‐B NB‐ARC are still functioning race‐specifically, but they lose full resistance activity. This is reminiscent of findings from the tobacco N‐like proteins (Gao et al. , 2007).…”

Section: Discussionsupporting

confidence: 55%

Intragenic allele pyramiding combines different specificities of wheat Pm3 resistance alleles

et al. 2010

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SUMMARYSome plant resistance genes occur as allelic series, with each member conferring specific resistance against a subset of pathogen races. In wheat, there are 17 alleles of the Pm3 gene. They encode nucleotide-binding (NB-ARC) and leucine-rich-repeat (LRR) domain proteins, which mediate resistance to distinct race spectra of powdery mildew. It is not known if specificities from different alleles can be combined to create resistance genes with broader specificity. Here, we used an approach based on avirulence analysis of pathogen populations to characterize the molecular basis of Pm3 recognition spectra. A large survey of mildew races for avirulence on the Pm3 alleles revealed that Pm3a has a resistance spectrum that completely contains that of Pm3f, but also extends towards additional races. The same is true for the Pm3b and Pm3c gene pair. The molecular analysis of these allelic pairs revealed a role of the NB-ARC protein domain in the efficiency of effector-dependent resistance. Analysis of the wild-type and chimeric Pm3 alleles identified single residues in the C-terminal LRR motifs as the main determinant of allele specificity. Variable residues of the N-terminal LRRs are necessary, but not sufficient, to confer resistance specificity. Based on these data, we constructed a chimeric Pm3 gene by intragenic allele pyramiding of Pm3d and Pm3e that showed the combined resistance specificity and, thus, a broader recognition spectrum compared with the parental alleles. Our findings support a model of stepwise evolution of Pm3 recognition specificities.

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Section: Discussionsupporting

confidence: 55%

Intragenic allele pyramiding combines different specificities of wheat Pm3 resistance alleles

et al. 2010

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“…Experiments on the potential signaling functions of domains in NB-LRR-class R proteins indicate that the LRR domain or the combined action of the LRR domain and N-terminal domain has been implicated in pathogen recognition (Banerjee et al 2001;Burch-Smith et al 2007;Ellis et al 1999Ellis et al , 2007Gao et al 2007;Luck et al 2000;Rairdan and Moffett 2006;Rairdan et al 2008;Tomita et al 2011). The LRR domain is a structural motif characterized by a conserved pattern of hydrophobic leucine residues and displays a broad surface for protein-protein interactions (Kobe and Kajara 2001;Padmanabhan et al 2009).…”

Section: Function Of Lrr Domain In Rcy1-conferred Resistance To Cmv(y)mentioning

confidence: 99%

RCY1-Mediated Resistance to Cucumber mosaic virus Is Regulated by LRR Domain-Mediated Interaction with CMV(Y) Following Degradation of RCY1

Takahashi¹,

Shoji²,

Ando³

et al. 2012

MPMI

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RCY1, which encodes a coiled coil nucleotide-binding site leucine-rich repeat (LRR) class R protein, confers the hypersensitive response (HR) to a yellow strain of Cucumber mosaic virus (CMV[Y]) in Arabidopsis thaliana. Nicotiana benthamiana transformed with hemagglutinin (HA) epitope-tagged RCY1 (RCY1-HA) also exhibited a defense response accompanied by HR cell death and induction of defense-related gene expression in response to CMV(Y). Following transient expression of RCY1-HA by agroinfiltration, the defense reaction was induced in N. benthamiana leaves infected with CMV(Y) but not in virulent CMV(B2)-infected N. benthamiana leaves transiently expressing RCY1-HA or CMV(Y)-infected N. benthamiana leaves transiently expressing HA-tagged RPP8 (RPP8-HA), which is allelic to RCY1. This result suggests that Arabidopsis RCY1-conferred resistance to CMV(Y) could be reproduced in N. benthamiana leaves in a gene-for-gene manner. Expression of a series of chimeric constructs between RCY1-HA and RPP8-HA in CMV(Y)-infected N. benthamiana indicated that induction of defense responses to CMV(Y) is regulated by the LRR domain of RCY1. Interestingly, in CMV(Y)-infected N. benthamiana manifesting the defense response, the levels of both RCY1 and chimeric proteins harboring the RCY1 LRR domain were significantly reduced. Taken together, these data indicate that the RCY1-conferred resistance response to CMV(Y) is regulated by an LRR domain-mediated interaction with CMV(Y) and seems to be tightly associated with the degradation of RCY1 in response to CMV(Y).

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“…Individual LRR units contain xxLxLxx motifs generating β-strand/β-turn structures in which the variable non-leucine residues form the concave, solvent-exposed surface of the horseshoe and are available for participation in protein-protein interactions [29], [30]. This region of plant R proteins is often highly variable, as a result of diversifying selection, and a number of studies have demonstrated changes in specificity mediated by polymorphisms in the LRR domain [18], [30], [31], [32], [33], [34], [35], [36], [37], [38].…”

Section: Introductionmentioning

confidence: 99%

Intramolecular Interaction Influences Binding of the Flax L5 and L6 Resistance Proteins to their AvrL567 Ligands

et al. 2012

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L locus resistance (R) proteins are nucleotide binding (NB-ARC) leucine-rich repeat (LRR) proteins from flax (Linum usitatissimum) that provide race-specific resistance to the causal agent of flax rust disease, Melampsora lini. L5 and L6 are two alleles of the L locus that directly recognize variants of the fungal effector AvrL567. In this study, we have investigated the molecular details of this recognition by site-directed mutagenesis of AvrL567 and construction of chimeric L proteins. Single, double and triple mutations of polymorphic residues in a variety of AvrL567 variants showed additive effects on recognition strength, suggesting that multiple contact points are involved in recognition. Domain-swap experiments between L5 and L6 show that specificity differences are determined by their corresponding LRR regions. Most positively selected amino acid sites occur in the N- and C-terminal LRR units, and polymorphisms in the first seven and last four LRR units contribute to recognition specificity of L5 and L6 respectively. This further confirms that multiple, additive contact points occur between AvrL567 variants and either L5 or L6. However, we also observed that recognition of AvrL567 is affected by co-operative polymorphisms between both adjacent and distant domains of the R protein, including the TIR, ARC and LRR domains, implying that these residues are involved in intramolecular interactions to optimize detection of the pathogen and defense signal activation. We suggest a model where Avr ligand interaction directly competes with intramolecular interactions to cause activation of the R protein.

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The TIR–NBS but not LRR domains of two novel N-like proteins are functionally competent to induce the elicitor p50-dependent hypersensitive response

Cited by 18 publications

References 24 publications

Intragenic allele pyramiding combines different specificities of wheat Pm3 resistance alleles

Intragenic allele pyramiding combines different specificities of wheat Pm3 resistance alleles

RCY1-Mediated Resistance to Cucumber mosaic virus Is Regulated by LRR Domain-Mediated Interaction with CMV(Y) Following Degradation of RCY1

Intramolecular Interaction Influences Binding of the Flax L5 and L6 Resistance Proteins to their AvrL567 Ligands

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