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bacteria:t3e:xopq [2020/07/06 12:47] rkoebnik |
bacteria:t3e:xopq [2020/07/08 18:31] rkoebnik |
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=== How discovered? === | === How discovered? === | ||
- | XopQ was identified in a genetic screen, using a Tn// | + | XopQ was identified in a genetic screen, using a Tn// |
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
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* Mutations of two potential active site residues, D116 and Y279, resulted in // | * Mutations of two potential active site residues, D116 and Y279, resulted in // | ||
* Compatibility studies with //X. euvesicatoria// | * Compatibility studies with //X. euvesicatoria// | ||
- | * XopQ mediated cell death suppression in //N. benthamiana// | + | |
+ | * Transient co-expression of XopQ::GFP and XopS::GFP in //N. benthamiana// | ||
+ | * XopQ suppressed cell death reactions in //N. benthamiana// | ||
+ | | ||
* A Δ// | * A Δ// | ||
* A reverse genetics screen identified Recognition of XopQ 1 (Roq1), a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, which mediates XopQ recognition in //N. benthamiana// | * A reverse genetics screen identified Recognition of XopQ 1 (Roq1), a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, which mediates XopQ recognition in //N. benthamiana// | ||
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* Roq1 is also involved in the recognition of RipB, the homolog of XopQ in //Ralstonia solanacearum//: | * Roq1 is also involved in the recognition of RipB, the homolog of XopQ in //Ralstonia solanacearum//: | ||
* Effectors that interact with 14–3–3 proteins may provide plant-pathogenic bacteria with the ability to modulate PTI as well as ETI. Suppression of immune responses induced by a // | * Effectors that interact with 14–3–3 proteins may provide plant-pathogenic bacteria with the ability to modulate PTI as well as ETI. Suppression of immune responses induced by a // | ||
+ | * Roq1 was found to confer immunity to // | ||
+ | * Strong resistance to // | ||
=== Localization === | === Localization === | ||
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Using protein-protein interaction studies in yeast and in planta, XopQ< | Using protein-protein interaction studies in yeast and in planta, XopQ< | ||
+ | |||
+ | Bimolecular fluorescence complementation assays upon transient expression in //N. benthamiana// | ||
Roq1, a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, was found to co-immunoprecipitate with XopQ, suggesting a physical association between the two proteins (Schultink //et al.//, 2017). | Roq1, a nucleotide-binding leucine-rich repeat (NLR) protein with a Toll-like interleukin-1 receptor (TIR) domain, was found to co-immunoprecipitate with XopQ, suggesting a physical association between the two proteins (Schultink //et al.//, 2017). | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | XopQ is a widely conserved across // | + | XopQ is a widely conserved across // |
=== In other plant pathogens/ | === In other plant pathogens/ | ||
- | XopQ shares homology with the //Ralstonia solanacearum// | + | XopQ shares homology with the //Ralstonia solanacearum// |
===== References ===== | ===== References ===== | ||
- | Adlung N (2016). Charakterisierung der Avirulenzaktivität von XopQ und Identifizierung möglicher Interaktoren von XopL aus // | + | Adlung N (2016). Charakterisierung der Avirulenzaktivität von XopQ und Identifizierung möglicher Interaktoren von XopL aus // |
Adlung N, Bonas U (2017). Dissecting virulence function from recognition: | Adlung N, Bonas U (2017). Dissecting virulence function from recognition: | ||
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Teper D, SalomonD, Sunitha S, Kim JG, Mudgett MB, Sessa G. (2014). // | Teper D, SalomonD, Sunitha S, Kim JG, Mudgett MB, Sessa G. (2014). // | ||
- | Thomas NC, Hendrich CG, Gill US, Allen C, Hutton SF, Schultink A (2020). The immune receptor Roq1 confers resistance to the bacterial pathogens // | + | Thomas NC, Hendrich CG, Gill US, Allen C, Hutton SF, Schultink A (2020). The immune receptor Roq1 confers resistance to the bacterial pathogens // |
Yu S, Hwang I, Rhee S (2013). Crystal structure of the effector protein XOO4466 from // | Yu S, Hwang I, Rhee S (2013). Crystal structure of the effector protein XOO4466 from // |