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bacteria:t3e:xopaj [2020/07/15 12:05] rkoebnik |
bacteria:t3e:xopaj [2020/09/29 22:21] lindsay.triplett_ct.gov |
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Authors: [[https:// | Authors: [[https:// | ||
- | Internal reviewer: | + | Internal reviewer: |
- | Expert reviewer: | + | Expert reviewer: |
Class: XopAJ\\ | Class: XopAJ\\ | ||
Family: XopAJ\\ | Family: XopAJ\\ | ||
Prototype: XopAJ (// | Prototype: XopAJ (// | ||
- | RefSeq ID: [[https:// | + | RefSeq ID: [[https:// |
Synonym: AvrRxo1\\ | Synonym: AvrRxo1\\ | ||
- | 3D structure: [[https:// | + | 3D structure: [[https:// |
===== Biological function ===== | ===== Biological function ===== | ||
=== How discovered? === | === How discovered? === | ||
- | Maize lines that contain the single dominant gene //Rxo1// exhibit a rapid hypersensitive response (HR) after infiltration with the rice bacterial streak pathogen // | + | Maize lines that contain the single dominant gene //Rxo1// exhibit a rapid hypersensitive response (HR) after infiltration with the nonhost |
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
When expressed in an //Xoo// //hrpC// mutant that is deficient in the type III secretion system, //avrRxo1// did not elicit the HR, indicating that the // | When expressed in an //Xoo// //hrpC// mutant that is deficient in the type III secretion system, //avrRxo1// did not elicit the HR, indicating that the // | ||
=== Regulation === | === Regulation === | ||
+ | |||
+ | No data available. | ||
=== Phenotypes === | === Phenotypes === | ||
Line 25: | Line 27: | ||
* When introduced into //Xoo//, clones containing // | * When introduced into //Xoo//, clones containing // | ||
* // | * // | ||
- | * AvrRxo1 | + | * AvrRxo1 |
* Variants of AvrRxo1 were found to suppress the HR caused by the non-host resistance recognition of // | * Variants of AvrRxo1 were found to suppress the HR caused by the non-host resistance recognition of // | ||
- | * Among four // | + | * Among four // |
* The ATP/GTP binding site motif A and the NLS are required for both the avirulence activity and the suppression of non-host resistance (Liu //et al.//, 2014). | * The ATP/GTP binding site motif A and the NLS are required for both the avirulence activity and the suppression of non-host resistance (Liu //et al.//, 2014). | ||
- | * AvrRxo1 has a T4 polynucleotide kinase domain, and expression of AvrRxo1-ORF1 suppresses bacterial growth in a manner dependent on the kinase motif (Han //et al.//, 2015). | + | * AvrRxo1 has a T4 polynucleotide kinase domain |
- | * The gene product of the adjacent gene, AvrRxo1-ORF2 aka Arc1, functions to suppress | + | * The gene product of the adjacent gene, AvrRxo1-ORF2 aka Arc1, suppresses |
- | * AvrRxo1 and its binding partner Arc1 function as a toxin-antitoxin system when expressed in // | + | * AvrRxo1 and its binding partner Arc1 function as a toxin-antitoxin system when expressed in // |
+ | * XopAJ< | ||
+ | * AvrRxo1 is a kinase that converts NAD to 3' | ||
+ | * AvrRxo1 targets the cysteine protease RD21A, which is required for drought-induced immunity (Liu //et al.//, 2020). | ||
=== Localization === | === Localization === | ||
- | Transient expression of // | + | Transient expression of // |
=== Enzymatic function === | === Enzymatic function === | ||
- | AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015). | + | AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015; Wu //et al//., 2015). |
+ | |||
+ | AvrRxo1 is a phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/ | ||
+ | |||
+ | AvrRxo1 phosphorylates NAD //in planta//, and its kinase catalytic sites are necessary for toxicity, suppression of PAMP-triggered immunity, and activation of Rxo1-mediated resistance (Shidore //et al.//, 2017). In a metabolomic profile, 3' | ||
=== Interaction partners === | === Interaction partners === | ||
Line 45: | Line 54: | ||
Molecular modeling was used to decipher structural mechanisms of AvrRxo1-Rxo1 interaction (Bahadur & Basak, 2014). | Molecular modeling was used to decipher structural mechanisms of AvrRxo1-Rxo1 interaction (Bahadur & Basak, 2014). | ||
- | The gene product of the adjacent gene, //avrRxo1-ORF2//, binds AvrRxo1, but binding is structurally different from typical effector-binding chaperones, in that it has a distinct fold containing a novel kinase-binding domain (Han //et al.//, 2015). | + | The gene product of the adjacent gene, AvrRxo1-ORF2 aka Arc1, binds AvrRxo1, but binding is structurally different from typical effector-binding chaperones, in that it has a distinct fold containing a novel kinase-binding domain (Han //et al.//, 2015). |
+ | |||
+ | AvrRxo1 interacts with the // | ||
===== Conservation ===== | ===== Conservation ===== | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | Yes (e.g. //X. alfalfae//, //X. axonopodis//, | + | Yes (e.g. //X. alfalfae//, //X. axonopodis//, |
+ | |||
+ | AvrRxo1 appears to be widely conserved in Asian strains of // | ||
+ | |||
+ | AvrRxo1 is conserved in nearly all strains of //X. euvesicatoria//, | ||
=== In other plant pathogens/ | === In other plant pathogens/ | ||
- | Yes (// | + | Yes (// |
+ | |||
+ | Homologs of the // | ||
===== References ===== | ===== References ===== | ||
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Liu H, Chang Q, Feng W, Zhang B, Wu T, Li N, Yao F, Ding X, Chu Z (2014). Domain dissection of AvrRxo1 for suppressor, avirulence and cytotoxicity functions. PLoS One 9: e113875. DOI: [[https:// | Liu H, Chang Q, Feng W, Zhang B, Wu T, Li N, Yao F, Ding X, Chu Z (2014). Domain dissection of AvrRxo1 for suppressor, avirulence and cytotoxicity functions. PLoS One 9: e113875. DOI: [[https:// | ||
+ | |||
+ | Liu Y, Wang K, Cheng Q, Kong D, Zhang X, Wang Z, Wang Q, Qi X, Yan J, Chu J, Ling H, Li Q, Miao J, Zhao B (2020). Cysteine protease RD21A regulated by E3 ligase SINAT4 is required for drought-induced resistance to // | ||
Popov G, Fraiture M, Brunner F, Sessa G (2016). Multiple // | Popov G, Fraiture M, Brunner F, Sessa G (2016). Multiple // | ||
- | Salomon D, Dar D, Sreeramulu S, Sessa G (2011). Expression of // | + | Salomon D, Dar D, Sreeramulu S, Sessa G (2011). Expression of // |
Schuebel F, Rocker A, Edelmann D, Schessner J, Brieke C, Meinhart A (2016). 3' | Schuebel F, Rocker A, Edelmann D, Schessner J, Brieke C, Meinhart A (2016). 3' | ||
- | Shidore T, Broeckling CD, Kirkwood JS, Long JJ, Miao J, Zhao B, Leach JE, Triplett LR (2017). The effector AvrRxo1 phosphorylates NAD in planta. PLoS Pathog. 13: e1006442. DOI: [[https:// | + | Shidore T, Broeckling CD, Kirkwood JS, Long JJ, Miao J, Zhao B, Leach JE, Triplett LR (2017). The effector AvrRxo1 phosphorylates NAD //in planta//. PLoS Pathog. 13: e1006442. DOI: [[https:// |
Triplett LR, Shidore T, Long J, Miao J, Wu S, Han Q, Zhou C, Ishihara H, Li J, Zhao B, Leach JE (2016). AvrRxo1 Is a bifunctional type III secreted effector and toxin-antitoxin system component with homologs in diverse environmental contexts. PLoS One 11: e0158856. DOI: [[https:// | Triplett LR, Shidore T, Long J, Miao J, Wu S, Han Q, Zhou C, Ishihara H, Li J, Zhao B, Leach JE (2016). AvrRxo1 Is a bifunctional type III secreted effector and toxin-antitoxin system component with homologs in diverse environmental contexts. PLoS One 11: e0158856. DOI: [[https:// | ||
Line 77: | Line 96: | ||
Wonni I, Cottyn B, Detemmerman L, Dao S, Ouedraogo L, Sarra S, Tekete C, Poussier S, Corral R, Triplett L, Koita O, Koebnik R, Leach J, Szurek B, Maes M, Verdier V (2014). Analysis of // | Wonni I, Cottyn B, Detemmerman L, Dao S, Ouedraogo L, Sarra S, Tekete C, Poussier S, Corral R, Triplett L, Koita O, Koebnik R, Leach J, Szurek B, Maes M, Verdier V (2014). Analysis of // | ||
- | Xie XW, Yu J, Xu JL, Zhou YL, Li ZK (2007). Introduction of a non-host gene // | + | Wu S (2015). Structural and functional characterization of a // |
+ | |||
+ | Xie XW, Yu J, Xu JL, Zhou YL, Li ZK (2007). Introduction of a non-host gene // | ||
Zhao B, Ardales EY, Raymundo A, Bai J, Trick HN, Leach JE, Hulbert SH (2004). The // | Zhao B, Ardales EY, Raymundo A, Bai J, Trick HN, Leach JE, Hulbert SH (2004). The // |