The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein

Fenyk, Stepan; Townsend, Philip D.; Dixon, Christopher H.; Spies, Gerhard B.; Campillo, Alba de San Eustaquio; Slootweg, E.J.; Westerhof, Lotte B.; Gawehns, Fleur; Knight, Marc R.; Sharples, Gary J.; Goverse, A.; Pålsson, Lars‐Olof; Takken, Frank L. W.; Cann, Martin J.

doi:10.1074/jbc.m115.672121

Cited by 38 publications

(52 citation statements)

References 95 publications

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“…In addition, the NB domains of several disease resistance proteins exhibit nucleotide phosphatase activity consistent with the switch model described above (Fenyk et al, 2012). Interestingly, Rx1 was recently found to bend and locally melt double-stranded DNA in a process mediated by its NB domain (Fenyk et al, 2015(Fenyk et al, , 2016. The functional activity of this NLR protein may thus be linked to a conserved direct interaction with DNA.…”

Section: Introductionmentioning

confidence: 53%

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

et al. 2017

Plant Cell

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BROWN PLANTHOPPER RESISTANCE14 (BPH14), the first planthopper resistance gene isolated via map-based cloning in rice (Oryza sativa), encodes a coiled-coil, nucleotide binding site, leucine-rich repeat (CC-NB-LRR) protein. Several planthopper and aphid resistance genes encoding proteins with similar structures have recently been identified. Here, we analyzed the functions of the domains of BPH14 to identify molecular mechanisms underpinning BPH14-mediated planthopper resistance. The CC or NB domains alone or in combination (CC-NB [CN]) conferred a similar level of brown planthopper resistance to that of full-length (FL) BPH14. Both domains activated the salicylic acid signaling pathway and defense gene expression. In rice protoplasts and Nicotiana benthamiana leaves, these domains increased reactive oxygen species levels without triggering cell death. Additionally, the resistance domains and FL BPH14 protein formed homocomplexes that interacted with transcription factors WRKY46 and WRKY72. In rice protoplasts, the expression of FL BPH14 or its CC, NB, and CN domains increased the accumulation of WRKY46 and WRKY72 as well as WRKY46-and WRKY72-dependent transactivation activity. WRKY46 and WRKY72 bind to the promoters of the receptor-like cytoplasmic kinase gene RLCK281 and the callose synthase gene LOC_Os01g67364.1, whose transactivation activity is dependent on WRKY46 or WRKY72. These findings shed light on this important insect resistance mechanism.

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Section: Introductionmentioning

confidence: 53%

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

et al. 2017

Plant Cell

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“…3e). A more direct nuclear signaling function of NLRs was recently proposed since the potato CNL Rx appears to bind and distort DNA via its central domain (Fenyk et al, 2015) (Fig. 3f).…”

Section: Tansley Insightmentioning

confidence: 95%

Multiple strategies for pathogen perception by plant immune receptors

2017

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Contents Summary17I.Introduction17II.Pathogen perception by NLRs: from direct recognition to integrated decoys18III.Multiple activation and signaling pathways for NLRs18IV.How to engineer NLR‐mediated disease resistance?21V.Conclusion23Acknowledgements23References23 Summary Plants have evolved a complex immune system to protect themselves against phytopathogens. A major class of plant immune receptors called nucleotide‐binding domain and leucine‐rich repeat‐containing proteins (NLRs) is ubiquitous in plants and is widely used for crop disease protection, making these proteins critical contributors to global food security. Until recently, NLRs were thought to be conserved in their modular architecture and functional features. Investigation of their biochemical, functional and structural properties has revealed fascinating mechanisms that enable these proteins to perceive a wide range of pathogens. Here, I review recent insights demonstrating that NLRs are more mechanistically and structurally diverse than previously thought. I also discuss how these findings provide exciting future prospects to improve plant disease resistance.

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“…It remains to be seen whether the DNA-binding properties of certain NLRs prove to play a role in plant NLR signalling (Fenyk et al, 2016(Fenyk et al, , 2015.…”

Section: Progress Towards a Mechanistic Understanding Of Plant Nlr Fumentioning

confidence: 99%

Animal NLRs provide structural insights into plant NLR function

Bentham

Burdett

Anderson

et al. 2016

Ann Bot

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Background The plant immune system employs intracellular NLRs (nucleotide binding [NB], leucine-rich repeat [LRR]/nucleotide-binding oligomerization domain [NOD]-like receptors) to detect effector proteins secreted into the plant cell by potential pathogens. Activated plant NLRs trigger a range of immune responses, collectively known as the hypersensitive response (HR), which culminates in death of the infected cell. Plant NLRs show structural and functional resemblance to animal NLRs involved in inflammatory and innate immune responses. Therefore, knowledge of the activation and regulation of animal NLRs can help us understand the mechanism of action of plant NLRs, and vice versa.Scope This review provides an overview of the innate immune pathways in plants and animals, focusing on the available structural and biochemical information available for both plant and animal NLRs. We highlight the gap in knowledge between the animal and plant systems, in particular the lack of structural information for plant NLRs, with crystal structures only available for the N-terminal domains of plant NLRs and an integrated decoy domain, in contrast to the more complete structures available for animal NLRs. We assess the similarities and differences between plant and animal NLRs, and use the structural information on the animal NLR pair NAIP/NLRC4 to derive a plausible model for plant NLR activation.Conclusions Signalling by cooperative assembly formation (SCAF) appears to operate in most innate immunity pathways, including plant and animal NLRs. Our proposed model of plant NLR activation includes three key steps: (1) initially, the NLR exists in an inactive auto-inhibited state; (2) a combination of binding by activating elicitor and ATP leads to a structural rearrangement of the NLR; and (3) signalling occurs through cooperative assembly of the resistosome. Further studies, structural and biochemical in particular, will be required to provide additional evidence for the different features of this model and shed light on the many existing variations, e.g. helper NLRs and NLRs containing integrated decoys.

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The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein

Cited by 38 publications

References 95 publications

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

Multiple strategies for pathogen perception by plant immune receptors

Animal NLRs provide structural insights into plant NLR function

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