Tobacco Transgenic for the Flax Rust Resistance Gene <i>L</i> Expresses Allele-Specific Activation of Defense Responses

Frost, Donna; Way, Heather M.; Howles, Paul A.; Luck, Jo; Manners, John M.; Hardham, Adrienne R.; Finnegan, Jean; Ellis, Jeff

doi:10.1094/mpmi.2004.17.2.224

Cited by 79 publications

(62 citation statements)

References 30 publications

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“…Transfer of R genes across plant families typically fail, either because they simply do not function or because they induce constitutive defense responses (37,38). On the basis of our work and that of Day et al (38), it appears that the solution to both of these problems is to identify the target of the pathogen effector molecule in the species from which the R gene is originating and then to coexpress the target with the cognate NBS-LRR protein in the recipient.…”

Section: Discussionmentioning

confidence: 72%

Indirect activation of a plant nucleotide binding site–leucine-rich repeat protein by a bacterial protease

Ade

DeYoung

Golstein

et al. 2007

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

368

404

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Nucleotide binding site-leucine-rich repeat (NBS-LRR) proteins mediate pathogen recognition in both mammals and plants. The molecular mechanisms by which pathogen molecules activate NBS-LRR proteins are poorly understood. Here we show that RPS5, a NBS-LRR protein from Arabidopsis, is activated by AvrPphB, a bacterial protease, via an indirect mechanism. When transiently expressed in Nicotiana benthamiana leaves, full-length RPS5 protein triggered programmed cell death, but only when coexpressed with AvrPphB and a second Arabidopsis protein, PBS1, which is a specific substrate of AvrPphB. Using coimmunoprecipitation analysis, we found that PBS1 is in a complex with the N-terminal coiled coil (CC) domain of RPS5 before exposure to AvrPphB. Deletion of the RPS5 LRR domain caused RPS5 to constitutively activate programmed cell death, even in the absence of AvrPphB and PBS1, and this activation depended on both the CC and NBS domains. The LRR and CC domains both coimmunoprecipitate with the NBS domain but not with each other. Thus, the LRR domain appears to function in part to inhibit RPS5 signaling, and cleavage of PBS1 by AvrPphB appears to release RPS5 from this inhibition. An amino acid substitution in the NBS site of RPS5 that is known to inhibit ATP binding in other NBS-LRR proteins blocked activation of RPS5, whereas a substitution thought to inhibit ATP hydrolysis constitutively activated RPS5. Combined, these data suggest that ATP versus ADP binding functions as a molecular switch that is flipped by cleavage of PBS1.B oth plants and animals employ nucleotide binding siteleucine-rich repeat (NBS-LRR) proteins to mediate detection of pathogen molecules (1). There appear to be at least two distinct mechanisms by which NBS-LRR proteins detect pathogens: either by binding pathogen-derived molecules directly or by sensing the modification of host proteins by pathogen-derived molecules (2). It is presently unclear how either mechanism causes activation of signaling by NBS-LRR proteins. We have been investigating these processes by using the plant NBS-LRR protein RPS5, which mediates detection of the protease AvrPphB from the bacterial pathogen Pseudomonas syringae (3-6).In plants, NBS-LRR proteins were first identified as the products of classically defined disease-resistance genes (R genes) (7-9), which are genes that confer resistance to infection by specific pathogen strains. R gene-mediated resistance is typically manifested by activation of a programmed cell death response referred to as the hypersensitive response (HR) that is localized to the site of pathogen ingress (10). In the last decade, R genes have been cloned from a large range of plant species, with the majority being found to encode NBS-LRR proteins (11). Plant NBS-LRR proteins can be subdivided into two broad categories defined by the presence of a Toll-interleukin receptor (TIR) domain or a non-TIR domain, most often a coiled-coil (CC) domain, at the amino terminus. The function of the CC and TIR domains in pathogen perception and signaling is un...

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Section: Discussionmentioning

confidence: 72%

Indirect activation of a plant nucleotide binding site–leucine-rich repeat protein by a bacterial protease

Ade

DeYoung

Golstein

et al. 2007

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

368

404

View full text Add to dashboard Cite

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“…NATURE COMMUNICATIONS | DOI: 10.1038/ncomms7338 ARTICLE as some of them can trigger immune responses when overexpressed alone in planta [32][33][34][35][36] . We showed overexpression of RPS4 TIR (1-235 a.a.)-triggered cell death in N. tabacum, whereas RRS1 TIR (1-175 a.a.) did not (Fig.…”

Section: Resultsmentioning

confidence: 99%

Two linked pairs of Arabidopsis TNL resistance genes independently confer recognition of bacterial effector AvrRps4

et al. 2015

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Plant immunity requires recognition of pathogen effectors by intracellular NB-LRR immune receptors encoded by Resistance (R) genes. Most R proteins recognize a specific effector, but some function in pairs that recognize multiple effectors. Arabidopsis thaliana TIR-NB-LRR proteins RRS1-R and RPS4 together recognize two bacterial effectors, AvrRps4 from Pseudomonas syringae and PopP2 from Ralstonia solanacearum. However, AvrRps4, but not PopP2, is recognized in rrs1/rps4 mutants. We reveal an R gene pair that resembles and is linked to RRS1/RPS4, designated as RRS1B/RPS4B, which confers recognition of AvrRps4 but not PopP2. Like RRS1/RPS4, RRS1B/RPS4B proteins associate and activate defence genes upon AvrRps4 recognition. Inappropriate combinations (RRS1/RPS4B or RRS1B/RPS4) are non-functional and this specificity is not TIR domain dependent. Distinct putative orthologues of both pairs are maintained in the genomes of Arabidopsis thaliana relatives and are likely derived from a common ancestor pair. Our results provide novel insights into paired R gene function and evolution.

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“…In similar experiments, maize Rp1 genes, which are also NBS-LRR genes, did not function in wheat and barley (14). Other NBS-LRR R genes also have a restricted taxonomic functionality (40), although some aspects of their function can sometimes be detected after transfer between distantly related species (41). If other R genes function in heterologous cereal backgrounds, it will have a significant impact on strategies to improve disease resistance in our most important crops.…”

Section: Discussionmentioning

confidence: 97%

A maize resistance gene functions against bacterial streak disease in rice

Zhao

Lin

Poland

et al. 2005

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

225

146

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Although cereal crops all belong to the grass family (Poacea), most of their diseases are specific to a particular species. Thus, a given cereal species is typically resistant to diseases of other grasses, and this nonhost resistance is generally stable. To determine the feasibility of transferring nonhost resistance genes (R genes) between distantly related grasses to control specific diseases, we identified a maize R gene that recognizes a rice pathogen, Xanthomonas oryzae pv. oryzicola, which causes bacterial streak disease. Bacterial streak is an important disease of rice in Asia, and no simply inherited sources of resistance have been identified in rice. Although X. o. pv. oryzicola does not cause disease on maize, we identified a maize gene, Rxo1, that conditions a resistance reaction to a diverse collection of pathogen strains. Surprisingly, Rxo1 also controls resistance to the unrelated pathogen Burkholderia andropogonis, which causes bacterial stripe of sorghum and maize. The same gene thus controls resistance reactions to both pathogens and nonpathogens of maize. Rxo1 has a nucleotide-binding siteleucine-rich repeat structure, similar to many previously identified R genes. Most importantly, Rxo1 functions after transfer as a transgene to rice, demonstrating the feasibility of nonhost R gene transfer between cereals and providing a valuable tool for controlling bacterial streak disease.disease resistance ͉ nonhost resistance ͉ Xanthomonas

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Tobacco Transgenic for the Flax Rust Resistance Gene L Expresses Allele-Specific Activation of Defense Responses

Cited by 79 publications

References 30 publications

Indirect activation of a plant nucleotide binding site–leucine-rich repeat protein by a bacterial protease

Indirect activation of a plant nucleotide binding site–leucine-rich repeat protein by a bacterial protease

Two linked pairs of Arabidopsis TNL resistance genes independently confer recognition of bacterial effector AvrRps4

A maize resistance gene functions against bacterial streak disease in rice

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