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bacteria:t3e:xopq

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bacteria:t3e:xopq [2020/07/07 18:34]
rkoebnik 		bacteria:t3e:xopq [2020/07/09 11:12]
rkoebnik [XopQ]
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 Class: XopQ\\ Class: XopQ\\
 Family: XopQ\\ Family: XopQ\\
-Prototype: XCV4438: Xanthomonas outer protein Q from //Xanthomonas euvesicatoria// pv. //euvesicatoria// strain 85-10 (aka //X. campestris// pv. //vesicatoria//, //Xcv//)\\+Prototype: XCV4438 (//Xanthomonas euvesicatoria// pv. //euvesicatoria//, ex //Xanthomonas campestris// pv. //vesicatoria//; strain 85-10)\\
 RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_011349176.1|WP_011349176.1]] (464 aa)\\ RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_011349176.1|WP_011349176.1]] (464 aa)\\
 3D structure: [[https://www.rcsb.org/structure/4kl0|4KL0]] (Yu //et al.//, 2013); [[https://www.rcsb.org/structure/4P5F|4P5F]] (Yu //et al.//, 2014) 3D structure: [[https://www.rcsb.org/structure/4kl0|4KL0]] (Yu //et al.//, 2013); [[https://www.rcsb.org/structure/4P5F|4P5F]] (Yu //et al.//, 2014)
 +
 ===== Biological function ===== ===== Biological function =====
  
 === How discovered? === === How discovered? ===
  
-XopQ was identified in a genetic screen, using a Tn//5//-based transposon construct harboring the coding sequence for the HR-inducing domain of AvrBs2, but devoid of the effectors' T3SS signal, that was randomly inserted into the genome of //Xcv //strain 85-10. The XopQ::AvrBs2 fusion protein triggered a //Bs2//-dependent hypersensitive response (HR) in pepper leaves (Roden //et al//., 2004). XopQ was also identified in //X. campestris// pv. //campestris// (//Xcc//) strain 8004 as a candidate T3E due to the presence of a plant-inducible promoter (PIP) box in its gene, XC_3177 (Jiang //et al.//, 2009).+XopQ was identified in a genetic screen, using a Tn//5//-based transposon construct harboring the coding sequence for the HR-inducing domain of AvrBs2, but devoid of the effectors' T3SS signal, that was randomly inserted into the genome of //X. campestris// pv. //vesicatoria// (//Xcv//)// //strain 85-10. The XopQ::AvrBs2 fusion protein triggered a //Bs2//-dependent hypersensitive response (HR) in pepper leaves (Roden //et al//., 2004). XopQ was also identified in //X. campestris// pv. //campestris// (//Xcc//) strain 8004 as a candidate T3E due to the presence of a plant-inducible promoter (PIP) box in its gene, XC_3177 (Jiang //et al.//, 2009).
 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
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   * Compatibility studies with //X. euvesicatoria//  pv. //perforans//  revealed that a double deletion of //avrBsT//  and //xopQ//  allows a host range expansion for //Nicotiana benthamiana//  (Schwartz //et al.//, 2015).   * Compatibility studies with //X. euvesicatoria//  pv. //perforans//  revealed that a double deletion of //avrBsT//  and //xopQ//  allows a host range expansion for //Nicotiana benthamiana//  (Schwartz //et al.//, 2015).
   * The avirulence activity of XopQ derivatives did not correlate with macroscopically visible plant reactions upon transient expression in //N. benthamiana//. It was therefore speculated that //N. benthamiana//  might encode two resistance proteins for the recognition of XopQ (Adlung, 2016).   * The avirulence activity of XopQ derivatives did not correlate with macroscopically visible plant reactions upon transient expression in //N. benthamiana//. It was therefore speculated that //N. benthamiana//  might encode two resistance proteins for the recognition of XopQ (Adlung, 2016).
-  * +  * Transient co-expression of XopQ::GFP and XopS::GFP in //N. benthamiana//  triggered cell death reactions, which were not observed when each effector was expressed alone. Bimolecular fluorescence complementation using split-YFP derivatives revealed that XopQ and XopS co-localize in the nucleus. These results suggested that both effectors may form a protein-protein complex i//n planta //  (Adlung, 2016).
- +
-Transient co-expression of XopQ::GFP and XopS::GFP in //N. benthamiana//  triggered cell death reactions, which were not observed when each effector was expressed alone. Bimolecular fluorescence complementation using split-YFP derivatives revealed that XopQ and XopS co-localize in the nucleus. These results suggested that both effectors may form a protein-protein complex i//n planta // (Adlung, 2016). +
   * XopQ suppressed cell death reactions in //N. benthamiana//  that were triggered by three //Xcv//  type III effectors (XopB, XopJ, XopL), whereas cell death reactions triggered by AvrBsT were not suppressed by XopQ (Adlung, 2016).   * XopQ suppressed cell death reactions in //N. benthamiana//  that were triggered by three //Xcv//  type III effectors (XopB, XopJ, XopL), whereas cell death reactions triggered by AvrBsT were not suppressed by XopQ (Adlung, 2016).
   * XopQ-mediated cell death suppression in //N. benthamiana//  during transient expression assays was later shown to result from an attenuation of //Agrobacterium//  ‐mediated protein expression rather than reflecting a genuine XopQ virulence activity (Adlung & Bonas, 2017).   * XopQ-mediated cell death suppression in //N. benthamiana//  during transient expression assays was later shown to result from an attenuation of //Agrobacterium//  ‐mediated protein expression rather than reflecting a genuine XopQ virulence activity (Adlung & Bonas, 2017).
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 Using protein-protein interaction studies in yeast and in planta, XopQ<sub>Xcv</sub>  was shown to physically interacts with the 14–3–3 protein TFT4 from tomato (//Solanum lycopersicum//) (Teper //et al.//, 2014). A mutation in the putative 14–3–3 binding site of XopQ (S65A) impaired interaction of the effector with TFT4 from pepper and tomato (//Capsicum annuum//) and its virulence function //in planta//  (Teper //et al.//, 2014). Yeast 2-hybrid assays revealed that XopQ<sub>Xcv</sub>  interacts with multiple, but perhaps not all 14–3–3 protein isoforms (Teper //et al.//, 2014; Dubrov //et al.//, 2018). Using protein-protein interaction studies in yeast and in planta, XopQ<sub>Xcv</sub>  was shown to physically interacts with the 14–3–3 protein TFT4 from tomato (//Solanum lycopersicum//) (Teper //et al.//, 2014). A mutation in the putative 14–3–3 binding site of XopQ (S65A) impaired interaction of the effector with TFT4 from pepper and tomato (//Capsicum annuum//) and its virulence function //in planta//  (Teper //et al.//, 2014). Yeast 2-hybrid assays revealed that XopQ<sub>Xcv</sub>  interacts with multiple, but perhaps not all 14–3–3 protein isoforms (Teper //et al.//, 2014; Dubrov //et al.//, 2018).
 +
 +Bimolecular fluorescence complementation assays upon transient expression in //N. benthamiana//  using split-YFP derivatives revealed that XopQ may interact with itself and also with XopS, maybe forming a large protein complex i//n planta //  (Adlung, 2016).
  
 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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