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bacteria:t3e:xopq [2020/07/06 12:54] rkoebnik [Biological function] |
bacteria:t3e:xopq [2021/01/05 17:25] (current) rkoebnik [References] |
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Class: XopQ\\ | Class: XopQ\\ | ||
Family: XopQ\\ | Family: XopQ\\ | ||
- | Prototype: XCV4438: Xanthomonas outer protein Q from // | + | Prototype: XCV4438 |
RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
3D structure: [[https:// | 3D structure: [[https:// | ||
+ | |||
===== Biological function ===== | ===== Biological function ===== | ||
=== 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 // | ||
- | * The NLR protein Recognition of XopQ 1 (Roq1) was recently identified from the plant Nicotiana benthamiana and mediates perception of the effector proteins XopQ and HopQ1 from Xanthomonas and P. syringae respectively. Unlike most recognized effectors, alleles of XopQ/HopQ1 are highly conserved and present in most plant pathogenic strains of Xanthomonas and P. syringae. A homolog of XopQ/HopQ1, named RipB, is present in most Ralstonia strains. We found that Roq1 was found to confer immunity to Xanthomonas (containing XopQ), P. syringae (containing the XopQ homolog HopQ1), and Ralstonia (containing the XopQ homolog RipB) when expressed in tomato (Thomas et al., 2020). | + | * Roq1 was found to confer immunity to //Xanthomonas// |
* Strong resistance to // | * Strong resistance to // | ||
+ | * Agrobacterium-mediated transient expression of both XopQ and XopX in rice cells resulted in induction of rice immune responses. These immune responses were not observed when either protein was individually expressed in rice cells. XopQ-XopX induced rice immune responses were not observed with a XopX mutant that is defective in 14-3-3 binding (Deb //et al.//, 2020). | ||
+ | * A screen for // | ||
=== 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). | ||
- | XopQ< | + | XopQ< |
+ | |||
+ | Yeast two-hybrid, bimolecular fluorescence complementation (BiFC) and co-IP assays indicated that XopQ and XopX interact with each other (Deb et al., 2020). | ||
===== Conservation ===== | ===== Conservation ===== | ||
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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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Büttner D, Bonas U (2010). Regulation and secretion of // | Büttner D, Bonas U (2010). Regulation and secretion of // | ||
+ | |||
+ | Deb S, Ghosh P, Patel HK, Sonti RV (2020). Interaction of the // | ||
Deb S, Gupta MK, Patel HK, Sonti RV (2019). // | Deb S, Gupta MK, Patel HK, Sonti RV (2019). // |