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- | ====== XopAJ ====== | ||
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- | Authors: [[https:// | ||
- | Internal reviewer: FIXME \\ | ||
- | Expert reviewer: FIXME | ||
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- | Class: XopAJ\\ | ||
- | Family: XopAJ\\ | ||
- | Prototype: XopAJ (// | ||
- | RefSeq ID: [[https:// | ||
- | Synonym: AvrRxo1\\ | ||
- | 3D structure: [[https:// | ||
- | ===== Biological function ===== | ||
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- | === How discovered? === | ||
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- | Maize lines that contain the single dominant gene //Rxo1// exhibit a rapid hypersensitive response (HR) after infiltration with the rice bacterial streak pathogen // | ||
- | === (Experimental) evidence for being a T3E === | ||
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- | 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 === | ||
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- | === Phenotypes === | ||
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- | * When introduced into //Xoo//, clones containing // | ||
- | * // | ||
- | * AvrRxo1 was found to be cytotoxic when expressed in yeast and caused chlorosis and patches of cell death in the infiltrated leaf areas upon transient expression in tomato and //Nicotiana benthamiana// | ||
- | * Variants of AvrRxo1 were found to suppress the HR caused by the non-host resistance recognition of // | ||
- | * 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). | ||
- | * AvrRxo1 has a T4 polynucleotide kinase domain, and expression of AvrRxo1 suppresses bacterial growth in a manner dependent on the kinase motif (Han //et al.//, 2015). | ||
- | * The gene product of the adjacent gene, AvrRxo1-ORF2 aka Arc1, functions to suppress the bacteriostatic activity of AvrRxo1 in bacterial cells (Han //et al.//, 2015). | ||
- | * AvrRxo1 and its binding partner Arc1 function as a toxin-antitoxin system when expressed in // | ||
- | * XopAJ< | ||
- | * Mutation of the catalytic aspartic acid residue D193 abolished AvrRxo1 kinase activity and several phenotypes of AvrRxo1, including toxicity in yeast, bacteria, and plants, suppression of the flg22-triggered ROS burst, and ability to trigger an //R// gene-mediated hypersensitive response. A mutation in the Walker A ATP-binding motif abolished the toxicity of AvrRxo1, but did not abolish the 3' | ||
- | * AvrRxo1 targets the cysteine protease RD21A, which is required for drought-induced immunity (Liu //et al.//, 2020). | ||
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- | === Localization === | ||
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- | Transient expression of // | ||
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- | === Enzymatic function === | ||
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- | AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015). | ||
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- | AvrRxo1 is an authentic phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/ | ||
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- | AvrRxo1 was also found to phosphorylate NAD i//n planta//, and that its kinase catalytic sites are necessary for its toxic and resistance-triggering phenotypes (Shidore //et al.//, 2017). 3' | ||
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- | === Interaction partners === | ||
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- | Molecular modeling was used to decipher structural mechanisms of AvrRxo1-Rxo1 interaction (Bahadur & Basak, 2014). | ||
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- | 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). | ||
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- | AvrRxo1 interacts with both the ubiquitin E3 ligase SINAT4 and the cysteine protease RD21A, enhancing SINAT4 activity, thus promoting the degradation of RD21A in vivo (Liu //et al.//, 2020). | ||
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- | ===== Conservation ===== | ||
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- | === In xanthomonads === | ||
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- | Yes (e.g. //X. alfalfae//, //X. axonopodis//, | ||
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- | AvrRxo1 appears to be widely conserved in Asian strains of // | ||
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- | === In other plant pathogens/ | ||
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- | Yes (// | ||
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- | ===== References ===== | ||
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- | Bahadur RP, Basak J (2014). Molecular modeling of protein-protein interaction to decipher the structural mechanism of nonhost resistance in rice. J. Biomol. Struct. Dyn. 32: 669-681. DOI: [[https:// | ||
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- | Han Q, Zhou C, Wu S, Liu Y, Triplett L, Miao J, Tokuhisa J, Deblais L, Robinson H, Leach JE, Li J, Zhao B (2015). Crystal structure of // | ||
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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:// | ||
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- | 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 // | ||
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- | Popov G, Fraiture M, Brunner F, Sessa G (2016). Multiple // | ||
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- | Salomon D, Dar D, Sreeramulu S, Sessa G (2011). Expression of // | ||
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- | Schuebel F, Rocker A, Edelmann D, Schessner J, Brieke C, Meinhart A (2016). 3' | ||
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- | 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:// | ||
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- | 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:// | ||
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- | 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 // | ||
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- | Xie XW, Yu J, Xu JL, Zhou YL, Li ZK (2007). Introduction of a non-host gene // | ||
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- | Zhao B, Ardales EY, Raymundo A, Bai J, Trick HN, Leach JE, Hulbert SH (2004). The // | ||
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- | Zhao B, Lin X, Poland J, Trick H, Leach J, Hulbert S (2005). A maize resistance gene functions against bacterial streak disease in rice. Proc. Natl. Acad. Sci. USA 102: 15383-15388. DOI: [[https:// | ||