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bacteria:t3e:xopr [2025/02/24 10:41] – [Biological function] rkoebnikbacteria:t3e:xopr [2025/07/24 22:51] (current) – jfpothier
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 Author: [[https://www.researchgate.net/profile/Fernando_Tavares|Fernando Tavares]]\\ Author: [[https://www.researchgate.net/profile/Fernando_Tavares|Fernando Tavares]]\\
-Reviewer: [[https://www.researchgate.net/profile/Amandine_Cunty|Amandine Cunty]]+Reviewer: [[https://www.researchgate.net/profile/Amandine_Cunty|Amandine Cunty]]\\
  
 Class: XopR\\ Class: XopR\\
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 //xopR// was firstly identified as a putative T3E ORF (XOO4134) shown to be under regulation of HrpX preceded by both a PIP box and a -10 box-like motif (Furutani //et al.//, 2006). Later, translocation of XOO4134::Cya fusion proteins into plant cells were shown to occur via a T3SS (Furutani //et al.//, 2009; White //et al.//, 2009). //xopR// was firstly identified as a putative T3E ORF (XOO4134) shown to be under regulation of HrpX preceded by both a PIP box and a -10 box-like motif (Furutani //et al.//, 2006). Later, translocation of XOO4134::Cya fusion proteins into plant cells were shown to occur via a T3SS (Furutani //et al.//, 2009; White //et al.//, 2009).
 +
 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
-Evidence for T3SS-dependent secretion and translocation of XopR into plant cells was mainly based on calmodulin-dependent adenylate cyclase (Cya) reporter assays of fusion proteins (Furutani //et al.//, 2009). XopR<sub>//Xoo// </sub> was confirmed to have a functional type III secretion signal using a reporter fusion with AvrBs1 (Zhao //et al.//, 2013).+Evidence for T3SS-dependent secretion and translocation of XopR into plant cells was mainly based on calmodulin-dependent adenylate cyclase (Cya) reporter assays of fusion proteins (Furutani //et al.//, 2009). XopR<sub>//Xoo//</sub> was confirmed to have a functional type III secretion signal using a reporter fusion with AvrBs1 (Zhao //et al.//, 2013). 
 === Regulation === === Regulation ===
  
-Functional studies using //hrp//-inducing and non-//hrp//-inducing media and reverse-transcriptase PCR in wild type and //X. oryzae// pv. //oryzae// (//Xoo//) ∆//hrpX// mutants showed that the expression of //xopR// is //hrpX// dependent (Verma //et al.//, 2019). These results are indirectly supported by previous findings showing that //Xoo// mutants deficient for //xrvB//, a gene coding for a repressor of //hrp// gene expression, leads to an increase of XopR into plant cells (Kametani-Ikawa //et al.//, 2011).+Functional studies using //hrp//-inducing and non-//hrp//-inducing media and reverse-transcriptase PCR in wild type and //X. oryzae// pv. //oryzae// (//Xoo//) ∆//hrpX// mutants showed that the expression of //xopR// is //hrpX// dependent (Verma //et al.//, 2019). These results are indirectly supported by previous findings showing that //Xoo// mutants deficient for //xrvB//, a gene coding for a repressor of //hrp// gene expression, leads to an increase of XopR secretion into plant cells (Kametani-Ikawa //et al.//, 2011). 
 + 
 +qRT-PCR revealed that transcript levels of 15 out of 18 tested non-TAL effector genes (as well as the regulatory genes //hrpG// and //hrpX//) were significantly reduced in the //Xoo// Δ//xrvC// mutant compared with those in the wild-type strain PXO99<sup>A</sup>, but this did not apply to //xopR// (Liu //et al.//, 2016).
  
-qRT-PCR revealed that transcript levels of 15 out of 18 tested non-TAL effector genes (as well as the regulatory genes //hrpG// and //hrpX//) were significantly reduced in the //Xoo// Δ//xrvC// mutant compared with those in the wild-type strain PXO99<sup>A</sup> , but this did not apply to //xopR// (Liu //et al.//, 2016). 
 === Phenotypes === === Phenotypes ===
  
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 Later studies suggested that XopR suppress PAMP-triggered stomatal closure in transgenic //Arabidopsis// expressing XopR (Wang //et al.//, 2016). More recently, when compared with a //Xoo// wild type strain, //xopR// deficient mutants (//Xoo// ∆//xopR//) infiltrated in rice leaves led to an increase of callose deposits, and a significant higher production of reactive oxygen species (ROS), namely of hydrogen peroxide (H<sub>2</sub> O<sub>2</sub>) and superoxide anion (O<sub>2<sup>-</sup></sub>), known as the main components of the plant oxidative burst (Verma //et al.//, 2018). Furthermore, reverse transcriptase expression analyses of eight rice genes linked to plant disease resistance (//BRI1//, //GST1//, //PR2//, //PR5//, //RAC1//, //SERK1//, //WRKY29// and //WRKY71//) were shown to be up-regulated in rice leaves inoculated with //Xoo// ∆//xopR// (Verma //et al.//, 2018; Verma //et al.//, 2019). To further support these findings, complementation of //Xoo// ∆//xopR// with //xopR// was able to restore the disease phenotype of the wild type Xoo strain (Verma //et al.//, 2018; Verma //et al.//, 2019). Later studies suggested that XopR suppress PAMP-triggered stomatal closure in transgenic //Arabidopsis// expressing XopR (Wang //et al.//, 2016). More recently, when compared with a //Xoo// wild type strain, //xopR// deficient mutants (//Xoo// ∆//xopR//) infiltrated in rice leaves led to an increase of callose deposits, and a significant higher production of reactive oxygen species (ROS), namely of hydrogen peroxide (H<sub>2</sub> O<sub>2</sub>) and superoxide anion (O<sub>2<sup>-</sup></sub>), known as the main components of the plant oxidative burst (Verma //et al.//, 2018). Furthermore, reverse transcriptase expression analyses of eight rice genes linked to plant disease resistance (//BRI1//, //GST1//, //PR2//, //PR5//, //RAC1//, //SERK1//, //WRKY29// and //WRKY71//) were shown to be up-regulated in rice leaves inoculated with //Xoo// ∆//xopR// (Verma //et al.//, 2018; Verma //et al.//, 2019). To further support these findings, complementation of //Xoo// ∆//xopR// with //xopR// was able to restore the disease phenotype of the wild type Xoo strain (Verma //et al.//, 2018; Verma //et al.//, 2019).
 +
 === Localization === === Localization ===
  
 Confocal microscopy studies of XopR::EYFP (enhanced yellow fluorescent protein) fusion protein transiently expressed in //Nicotiana benthaminiana//, suggested that XopR is localized to the plasma membrane of plant epidermal cells (Akimoto-Tomiyama //et al.//, 2012; Verma //et al.//, 2019). These results are further corroborate by findings assigning XopR localization to the plasma membrane of rice protoplasts, contrary to other effectors analysed, namely XopL XopV, XopC, and XopW, which were localized to the cytoplasm (Wang //et al.//, 2016). Confocal microscopy studies of XopR::EYFP (enhanced yellow fluorescent protein) fusion protein transiently expressed in //Nicotiana benthaminiana//, suggested that XopR is localized to the plasma membrane of plant epidermal cells (Akimoto-Tomiyama //et al.//, 2012; Verma //et al.//, 2019). These results are further corroborate by findings assigning XopR localization to the plasma membrane of rice protoplasts, contrary to other effectors analysed, namely XopL XopV, XopC, and XopW, which were localized to the cytoplasm (Wang //et al.//, 2016).
 +
 === Enzymatic function === === Enzymatic function ===
  
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 Yes (e.g. //X. arboricola, X. axonopodis//, //X. campestris//, //X. citri//, //X. gardneri//, //X. oryzae//, //X. phaseoli//, //X. populi//, //X. vasicola//, //X. bromi//, //X. cucurbitae// inferred from a BlastP search for a query coverage higher than 90% and a percent identity over 35%). Yes (e.g. //X. arboricola, X. axonopodis//, //X. campestris//, //X. citri//, //X. gardneri//, //X. oryzae//, //X. phaseoli//, //X. populi//, //X. vasicola//, //X. bromi//, //X. cucurbitae// inferred from a BlastP search for a query coverage higher than 90% and a percent identity over 35%).
 +
 === In other plant pathogens/symbionts === === In other plant pathogens/symbionts ===
  
bacteria/t3e/xopr.1740393665.txt.gz · Last modified: 2025/02/24 10:41 by rkoebnik

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