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bacteria:t3e:xopaj [2020/08/14 00:44] jfpothier [Biological function] |
bacteria:t3e:xopaj [2022/06/22 14:01] rkoebnik [Biological function] |
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Authors: [[https:// | Authors: [[https:// | ||
Internal reviewer: [[https:// | Internal reviewer: [[https:// | ||
- | Expert reviewer: | + | Expert reviewer: |
+ | |||
+ | Class: XopAJ\\ | ||
+ | Family: XopAJ\\ | ||
+ | Prototype: XopAJ (// | ||
+ | RefSeq ID: [[https:// | ||
+ | Synonym: AvrRxo1\\ | ||
+ | 3D structure: [[https:// | ||
+ | ====== XopAJ ====== | ||
+ | |||
+ | Authors: [[https:// | ||
+ | Internal reviewer: [[https:// | ||
+ | Expert reviewer: [[https:// | ||
Class: XopAJ\\ | Class: XopAJ\\ | ||
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=== 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 === | ||
Line 21: | Line 33: | ||
=== Regulation === | === Regulation === | ||
- | No data available? :FIXME : | + | No data available. |
=== Phenotypes === | === Phenotypes === | ||
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* 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 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< | * XopAJ< | ||
- | * Mutation of the catalytic aspartic acid residue D< | + | * 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). | * AvrRxo1 targets the cysteine protease RD21A, which is required for drought-induced immunity (Liu //et al.//, 2020). | ||
+ | * AvrRxo1 enhances // | ||
=== Localization === | === Localization === | ||
- | Transient expression of // | + | Transient expression of // |
=== Enzymatic function === | === Enzymatic function === | ||
- | AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015; Wu //et al//., 2015). | + | AvrRxo1 has a T4 polynucleotide kinase domain (Han //et al.//, 2015; Wu //et al//., 2015). AvrRxo1 is an ATP-dependent protease (Liu //et al.//, 2022). |
- | AvrRxo1 is an authentic | + | AvrRxo1 is a phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/ |
- | AvrRxo1 | + | AvrRxo1 |
=== Interaction partners === | === Interaction partners === | ||
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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). | 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 both the ubiquitin E3 ligase SINAT4 and the cysteine protease RD21A, enhancing | + | AvrRxo1 interacts with the // |
+ | |||
+ | AvrRxo1 interacts with OsPDX1.2 in a yeast two-hybrid assay and in planta, as assessed by split YFP and coIP assays (Liu //et al.//, 2022). | ||
===== Conservation ===== | ===== Conservation ===== | ||
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AvrRxo1 appears to be widely conserved in Asian strains of // | 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 // | ||
+ | |||
+ | ===== Conservation ===== | ||
+ | |||
+ | === In xanthomonads === | ||
+ | |||
+ | 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/ | ||
+ | |||
+ | 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 // | + | Liu H, Lu C, Li Y, Wu T, Zhang B, Liu B, Feng W, Xu Q, Dong H, He S, Chu Z, Ding X (2022). The bacterial effector AvrRxo1 inhibits vitamin B6 biosynthesis to promote infection in rice. Plant Commun. 3: 100324. 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 // |