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bacteria:t3e:xopah

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bacteria:t3e:xopah [2025/01/29 23:11] – [Biological function] jfpothierbacteria:t3e:xopah [2025/02/21 11:35] (current) – [Conservation] rkoebnik
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 AvrXccC was described during a genome comparison analysis between //Xanthomonas citri// pv. citri and //X. campestris// pv. campestris Xcc strain ATCC 33913 = NCPPB 528 (Da Silva et al., 2002) and in a search of annotated genome (Castenada //et al//., 2005). AvrXccC was described during a genome comparison analysis between //Xanthomonas citri// pv. citri and //X. campestris// pv. campestris Xcc strain ATCC 33913 = NCPPB 528 (Da Silva et al., 2002) and in a search of annotated genome (Castenada //et al//., 2005).
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 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
 Secreted XopAH (AvrXccC) proteins were detected in culture fluid from //Xcc// 8004 and //hrcV// mutant complemented strains but not from the //hrcV// mutant (Wang //et al//., 2007). Insertion and deletion mutants affecting the locus (Xcc2109) in the type strain (Xcc 528) resulted in loss of virulence on the host Florida Broad Leaf Mustard (Castañeda //et al//., 2005). Secreted XopAH (AvrXccC) proteins were detected in culture fluid from //Xcc// 8004 and //hrcV// mutant complemented strains but not from the //hrcV// mutant (Wang //et al//., 2007). Insertion and deletion mutants affecting the locus (Xcc2109) in the type strain (Xcc 528) resulted in loss of virulence on the host Florida Broad Leaf Mustard (Castañeda //et al//., 2005).
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 === Regulation === === Regulation ===
  
 Promoter activity assays showed that the expression of XopAH (//avrXccC//) is //hrpG/hrpX//-dependent (Wang //et al//., 2007). Promoter activity assays showed that the expression of XopAH (//avrXccC//) is //hrpG/hrpX//-dependent (Wang //et al//., 2007).
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 === Phenotypes === === Phenotypes ===
  
-This effector is required for full virulence in the susceptible host cabbage (//Brassica oleracea//) (Wang //et al//., 2007) and results in avirulence in the resistant host mustard (//Brassica napiformis//) (Castaneda //et al//., 2005; He //et al//., 2007; Wang //et al//., 2007). The intact AvrB-AvrC domain of //AvrXccC<sub>8004</sub>// is essential and sufficient to elicit defense responses in an //Arabidopsis// resistant ecotype (Col-0) (Ho //et al//., 2013). +This effector is required for full virulence in the susceptible host cabbage (//Brassica oleracea//) (Wang //et al//., 2007) and results in avirulence in the resistant host mustard (//Brassica napiformis//) (Castaneda //et al//., 2005; He //et al//., 2007; Wang //et al//., 2007). The intact AvrB-AvrC domain of //AvrXccC<sub>8004</sub> // is essential and sufficient to elicit defense responses in an //Arabidopsis// resistant ecotype (Col-0) (Ho //et al//., 2013).
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-In the interaction //Arabidopsis// / //Xcc// strain 8004, //AvrXccC<sub>8004</sub> // not only presented its avirulence activity to trigger plant defense response but also possessed its virulence activity to manipulate the component involved in the ABA signalling pathway leading to an increase of ABA concentrations (Ho //et al//., 2013).+
  
 +In the interaction //Arabidopsis// / //Xcc// strain 8004, AvrXccC<sub>8004</sub> not only presented its avirulence activity to trigger plant defense response but also possessed its virulence activity to manipulate the component involved in the ABA signalling pathway leading to an increase of ABA concentrations (Ho //et al.//, 2013).
 === Localization === === Localization ===
  
-XopAH (AvrXccC) is anchored to the plant plasma membrane, and the N‐terminal myristoylation site (amino acids 2–7: GLcaSK) is essential for its localization (Wang //et al//., 2007). +XopAH (AvrXccC) is anchored to the plant plasma membrane, and the N‐terminal myristoylation site (amino acids 2–7: GLcaSK) is essential for its localization (Wang //et al.//, 2007).
 === Enzymatic function === === Enzymatic function ===
  
-XopAH has a Fido/AvrB domain derived from the fic (cyclic adenosine monophosphate (cAMP)-induced filamentation and doc (death on curing) domains (Kinch //et al//., 2009). Structural comparisons resulted in the inclusion of similar segments of the T3 effector AvrB from //Pseudomonas syringae// species (Kinch //et al//., 2009; White //et al//., 2009). T3 effectors in the XopAH group could trans-AMPylate plant host proteins. AMPylation represents a posttranslational modification used to stably modify proteins with AMP (Kinch //et al//., 2009). +XopAH has a Fido/AvrB domain derived from the fic (cyclic adenosine monophosphate (cAMP)-induced filamentation and doc (death on curing) domains (Kinch //et al//., 2009). Structural comparisons resulted in the inclusion of similar segments of the T3 effector AvrB from //Pseudomonas syringae// species (Kinch //et al//., 2009; White //et al//., 2009). T3 effectors in the XopAH group could trans-AMPylate plant host proteins. AMPylation represents a posttranslational modification used to stably modify proteins with AMP (Kinch //et al.//, 2009).
 === Interaction partners === === Interaction partners ===
  
-Not known ?+Not known.
  
 ===== Conservation ===== ===== Conservation =====
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 === In xanthomonads === === In xanthomonads ===
  
-In //Xanthomonas campestris// pv. campestris. XopAH is also present in //X. arboricola// pv. juglandis within strains causing Walnut Blight but is absent from the strains causing vertical oozing canker (Cesbron et al., 2015).+In //Xanthomonas campestris// pv. campestris. XopAH is also present in //X. arboricola// pv. juglandis within strains causing Walnut Blight but is absent from the strains causing vertical oozing canker (Cesbron //et al.//, 2015).
 === In other plant pathogens/symbionts === === In other plant pathogens/symbionts ===
  
 Yes (AvrB //Pseudomonas savastanoi//, //Pseudomonas syringae//) (Lee //et al.//, 2004; Desveaux //et al.//, 2007) Yes (AvrB //Pseudomonas savastanoi//, //Pseudomonas syringae//) (Lee //et al.//, 2004; Desveaux //et al.//, 2007)
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 ===== References ===== ===== References =====
  
bacteria/t3e/xopah.1738192301.txt.gz · Last modified: 2025/01/29 23:11 by jfpothier