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bacteria:t3e:xopae [2025/03/10 10:16] – [Biological function] rkoebnikbacteria:t3e:xopae [2025/07/07 12:42] (current) – [References] rkoebnik
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 Author: [[https://www.researchgate.net/profile/Guido_Sessa|Guido Sessa]]\\ Author: [[https://www.researchgate.net/profile/Guido_Sessa|Guido Sessa]]\\
-Internal reviewer: [[https://www.researchgate.net/profile/David_Studholme|David J. Studholme]]\\+Internal reviewers: [[https://www.researchgate.net/profile/David_Studholme|David J. Studholme]], [[https://www.researchgate.net/profile/Ralf-Koebnik|Ralf Koebnik]]\\
 Expert reviewer: [[https://www.researchgate.net/profile/Laurent_Noel|Laurent D. Noël]]\\ Expert reviewer: [[https://www.researchgate.net/profile/Laurent_Noel|Laurent D. Noël]]\\
  
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 GenBank ID: [[https://www.ncbi.nlm.nih.gov/protein/AAL78290.1|AAL78290.1]] (197 aa) / [[https://www.ncbi.nlm.nih.gov/protein/AAL78291.1|AAL78291.1]] (432 aa)\\ GenBank ID: [[https://www.ncbi.nlm.nih.gov/protein/AAL78290.1|AAL78290.1]] (197 aa) / [[https://www.ncbi.nlm.nih.gov/protein/AAL78291.1|AAL78291.1]] (432 aa)\\
 RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_011050288.1|WP_011050288.1]] (547 aa)\\ RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_011050288.1|WP_011050288.1]] (547 aa)\\
-Synonyms: XopAE was also referred to as HpaF (Kim //et al.//, 2003; Sugio //et al.//, 2005). In //Xcv// strain 85-10, the gene is bipartite and the two parts were first coined //hpaF// and //hpaG// (Noël //et al.//, 2002). Be careful: //hpaG// was also used in other Xanthomonas to designate the homolog of //hpa1// (//X. campestris//, //X. oryzae//) and //xopA// (//Xcv// 85-10) (Kim //et al.//, 2003).\\ +Synonyms: XopAE was also referred to as HpaF (Kim //et al.//, 2003; Sugio //et al.//, 2005). In //Xee// strain 85-10, the gene is bipartite and the two parts were first coined //hpaF// and //hpaG// (Noël //et al.//, 2002). Be careful: //hpaG// was also used in other //Xanthomonas// to designate the homolog of //hpa1// (//X. campestris//, //X. oryzae//) and //xopA// (//Xcv// 85-10) (Kim //et al.//, 2003).\\ 
-3D structure: Most XopAE possesses a N-terminal leucine-rich repeat (LRR) domain and a C-terminal XL box motif with an E3 ubiquitin ligase fold, based on homology modelling (Popov //et al//., 2018). Predicted fold of XopAE C terminus is similar to that of XopL (Popov //et al//., 2018).+3D structure: Most XopAE possesses a N-terminal leucine-rich repeat (LRR) domain and a C-terminal XL box motif with an E3 ubiquitin ligase fold, based on homology modelling (Popov //et al.//., 2018). Predicted fold of XopAE C terminus is similar to that of XopL (Popov //et al.//, 2018).
  
 ===== The locus ===== ===== The locus =====
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 XopAE was discovered by studying //hrpG//-regulated genes within the //hrp// gene cluster of //X. euvesicatoria// pv. //euvesicatoria// (//Xee//) strain 85-10 (Noël //et al.//, 2002). XopAE was discovered by studying //hrpG//-regulated genes within the //hrp// gene cluster of //X. euvesicatoria// pv. //euvesicatoria// (//Xee//) strain 85-10 (Noël //et al.//, 2002).
 +
 === (Experimental) evidence for being a T3E === === (Experimental) evidence for being a T3E ===
  
 XopAE<sub>//Xee//85-10</sub> was fused to the AvrBs2 reporter and shown to translocate into plant cells in an //hrpF//-dependent manner (Popov //et al.//, 2018). XopAE<sub>//Xee//85-10</sub> was fused to the AvrBs2 reporter and shown to translocate into plant cells in an //hrpF//-dependent manner (Popov //et al.//, 2018).
 +
 === Regulation === === Regulation ===
  
 In //Xee// strain 85-10, //xopAE// <sub>85-10</sub> transcription is driven by the promoter of the immediately upstream //hpaF// gene and regulated by the HrpX and HrpG master transcriptional regulators of the //Xanthomonas// T3SS (Popov //et al.//, 2016). An imperfect PIP box (TTCGC-N<sub>16</sub>-TTCGC) is located 82 bp upstream of the predicted translation start codon of //hpaF// (Noël //et al.//, 2002). In //Xee// strain 85-10, //xopAE// <sub>85-10</sub> transcription is driven by the promoter of the immediately upstream //hpaF// gene and regulated by the HrpX and HrpG master transcriptional regulators of the //Xanthomonas// T3SS (Popov //et al.//, 2016). An imperfect PIP box (TTCGC-N<sub>16</sub>-TTCGC) is located 82 bp upstream of the predicted translation start codon of //hpaF// (Noël //et al.//, 2002).
 +
 === Phenotypes === === Phenotypes ===
  
 XopAE<sub>//Xee//85-10</sub> is a suppressor of PTI that was shown to inhibit flg22-mediated signaling in //Arabidopsis// and tomato protoplasts, downstream or in parallel to the activation of the MPK3 and MPK6 MAP kinases. //Pseudomonas syringae//-mediated delivery of XopAE<sub>//Xee//85-10</sub> in plants inhibits PTI-associated callose deposition at the cell wall and enhances disease symptoms in tomato (Popov //et al.//, 2016). Later, XopAE<sub>//Xpm// </sub> was confirmed to suppress basal defenses such as callose deposition and the production of reactive oxygen species (Gomez De la Cruz //et al.//, 2025). XopAE<sub>//Xee//85-10</sub> is a suppressor of PTI that was shown to inhibit flg22-mediated signaling in //Arabidopsis// and tomato protoplasts, downstream or in parallel to the activation of the MPK3 and MPK6 MAP kinases. //Pseudomonas syringae//-mediated delivery of XopAE<sub>//Xee//85-10</sub> in plants inhibits PTI-associated callose deposition at the cell wall and enhances disease symptoms in tomato (Popov //et al.//, 2016). Later, XopAE<sub>//Xpm// </sub> was confirmed to suppress basal defenses such as callose deposition and the production of reactive oxygen species (Gomez De la Cruz //et al.//, 2025).
 +
 === Localization === === Localization ===
  
 XopAE<sub>//Xee//85-10</sub>-YFP fusion protein localizes to the cytoplasm and nucleus of //Nicotiana benthamiana// leaf epidermal cells (Popov //et al.//, 2016). XopAE<sub>//Xpm// </sub> localizes to the nucleus and in scattered points throughout the cell border, while Mep23-1 shows a nucleocytoplasmic localization. Upon interaction, XopAE//<sub>Xpm</sub> // hijacks Mep23-1 to the scattered points throughout the cell border and they also interact in nucleus (Gomez De la Cruz //et al.//, 2025). XopAE<sub>//Xee//85-10</sub>-YFP fusion protein localizes to the cytoplasm and nucleus of //Nicotiana benthamiana// leaf epidermal cells (Popov //et al.//, 2016). XopAE<sub>//Xpm// </sub> localizes to the nucleus and in scattered points throughout the cell border, while Mep23-1 shows a nucleocytoplasmic localization. Upon interaction, XopAE//<sub>Xpm</sub> // hijacks Mep23-1 to the scattered points throughout the cell border and they also interact in nucleus (Gomez De la Cruz //et al.//, 2025).
 +
 === Enzymatic function === === Enzymatic function ===
  
 XopAE<sub>85-10</sub> is an active E3 ubiquitin ligase //in vitro// (Popov //et al.//, 2018). XopAE<sub>85-10</sub> is an active E3 ubiquitin ligase //in vitro// (Popov //et al.//, 2018).
 +
 === Interaction partners === === Interaction partners ===
  
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 ===== References ===== ===== References =====
  
-Gomez De la Cruz D, Castillo DA, Trujillo B CA, Medina CA, Hurtado V, Gil J, Padmanabhan M, Restrepo S, Dinesh-Kumar SP, Germain H, Lopez C, Bernal A (2025). XopAE effector from Xanthomonas phaseoli pv. manihotis targets HSP20-like p23 cochaperone to suppress plant basal immunity. Mol. Plant Microbe Interact., in press. DOI: [[https://doi.org/10.1094/MPMI-08-24-0086-R|10.1094/MPMI-08-24-0086-R]]+Gomez De la Cruz D, Castillo DA, Trujillo B CA, Medina CA, Hurtado V, Gil J, Padmanabhan M, Restrepo S, Dinesh-Kumar SP, Germain H, Lopez C, Bernal A (2025). XopAE effector from //Xanthomonas phaseoli //pv. //manihotis// targets HSP20-like p23 cochaperone to suppress plant basal immunity. Mol. Plant Microbe Interact. 
 +38: 365-375 . DOI: [[https://doi.org/10.1094/MPMI-08-24-0086-R|10.1094/MPMI-08-24-0086-R]]
  
 Kim JG, Park BK, Yoo CH, Jeon E, Oh J, Hwang I (2003). Characterization of the //Xanthomonas axonopodis// pv. //glycines// Hrp pathogenicity island. J. Bacteriol. 185: 3155‐3166. DOI: [[https://doi.org/10.1128/jb.185.10.3155-3166.2003|jb.185.10.3155-3166.2003]] Kim JG, Park BK, Yoo CH, Jeon E, Oh J, Hwang I (2003). Characterization of the //Xanthomonas axonopodis// pv. //glycines// Hrp pathogenicity island. J. Bacteriol. 185: 3155‐3166. DOI: [[https://doi.org/10.1128/jb.185.10.3155-3166.2003|jb.185.10.3155-3166.2003]]
bacteria/t3e/xopae.1741601802.txt.gz · Last modified: 2025/03/10 10:16 by rkoebnik

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