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bacteria:t3e:xopah [2020/06/22 10:18] jfpothier |
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- | ====== XopAH ====== | ||
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- | Author: Steven J. Roberts\\ | ||
- | Internal reviewer: Christian Vernière \\ | ||
- | Expert reviewer: FIXME | ||
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- | Class: XopAH\\ | ||
- | Family: XopAH\\ | ||
- | Prototype: XopAH (AvrXccC) (// | ||
- | RefSeq ID: [[https:// | ||
- | 3D structure: Unknown | ||
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- | ===== Biological function ===== | ||
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- | === How discovered? === | ||
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- | === (Experimental) evidence for being a T3E === | ||
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- | 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 (Castenada //et al//., 2005). | ||
- | === Regulation === | ||
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- | Promoter activity assays showed that the expression of XopAH (// | ||
- | === Phenotypes === | ||
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- | 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// | ||
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- | In the interaction | ||
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- | === Localization === | ||
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- | 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). | ||
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- | === Enzymatic function === | ||
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- | 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 // | ||
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- | === Interaction partners === | ||
- | Not known ? | ||
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- | ===== Conservation ===== | ||
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- | === In xanthomonads === | ||
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- | In // | ||
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- | === In other plant pathogens/ | ||
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- | Yes (AvrB // | ||
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- | ===== References ===== | ||
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- | Castenada A, Reddy JD, El-Yacoubi B, Gabriel DW (2005). Mutagenesis of all eight avr genes in // | ||
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- | Cesbron, S., Briand, M., Essakhi, S., Gironde, S., Boureau, T., Manceau, C., Fischer-Le Saux, M., and Jacques, M. A. 2015.</ | ||
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- | Da Silva, A. C., Ferro, J. A., Reinach, F. C., Farah, C. S., Furlan, L. R., Quaggio, R. B., Monteiro-Vitorello, | ||
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- | <font 10.5pt/ | ||
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- | Ho, Y. P., Tan, C. M., Li, M. Y., Lin, H., Deng, W. L., and Yang, J. Y. 2013. The AvrB_AvrC Domain of AvrXccC of // | ||
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- | Kinch, L. N., Yarbrough, M. L., Orth, K., and Grishin, N. V. 2009. Fido, a Novel AMPylation Domain Common to Fic, Doc, and AvrB. Plos One 4: e5818. | ||
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- | Qian W, Jia Y, Ren SX, He Y Q, Feng JX, Lu LF, Sun Q, Ying G, Tang DJ, Tang H, Wu W, Hao P, Wang L, Jiang BL, Zeng S, Gu WY, Lu G, Rong L, Tian Y, Yao Z, Fu G, Chen B, Fang R, Qiang B, Chen Z, Zhao GP, Tang JL and He C (2005). Comparative and functional genomic analyses of the pathogenicity of phytopathogen // | ||
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- | Wang L, Tang X, He C (2007). The bifunctional effector AvrXccC of // | ||
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- | <font 10.5pt/ | ||