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| bacteria:t3e:xopag [2025/07/24 22:24] – jfpothier | bacteria:t3e:xopag [2026/10/29 12:46] (current) – [Biological function] rkoebnik | ||
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| === How discovered? === | === How discovered? === | ||
| - | // | + | // |
| === (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
| An active TTSS is necessary for HR produced by AvrGf1 in grapefruit leaves, as it was proven by transconjugation experiments (Rybak //et al.//, 2009). | An active TTSS is necessary for HR produced by AvrGf1 in grapefruit leaves, as it was proven by transconjugation experiments (Rybak //et al.//, 2009). | ||
| - | |||
| === Regulation === | === Regulation === | ||
| - | No data available. The effector gene //xopAG// was however shown to be induced in XVM2 medium compared to NB medium in //X//. //citri// subsp. //citri// A< | + | No data available. The effector gene //xopAG// was however shown to be induced in XVM2 medium compared to NB medium in //X//. //citri// subsp. //citri// A< |
| === Phenotypes === | === Phenotypes === | ||
| - | All // | + | All // |
| + | Deletion of XopAG in //X. phaseoli// pv. // | ||
| === Localization === | === Localization === | ||
| AvrGf1 (Figueiredo //et al.//, 2011) and AvrGf2 (Gochez //et al.//, 2017) possess a N-terminal chloroplast localization signal. The signal is not shared by all members of the XopAG effector family (Gochez //et al.//, 2017). Transient expression of the protein with the first 116 amino acids deleted in grapefruit leaves resulted in the elimination of the HR and a lack of accumulation of the protein in the chloroplast. | AvrGf1 (Figueiredo //et al.//, 2011) and AvrGf2 (Gochez //et al.//, 2017) possess a N-terminal chloroplast localization signal. The signal is not shared by all members of the XopAG effector family (Gochez //et al.//, 2017). Transient expression of the protein with the first 116 amino acids deleted in grapefruit leaves resulted in the elimination of the HR and a lack of accumulation of the protein in the chloroplast. | ||
| - | |||
| === Enzymatic function === | === Enzymatic function === | ||
| AvrGf2 elicited rapid cell death in grapfruit leaves (Gonchez //et al.//, 2015), detailed enzymatic function has not been determined yet. | AvrGf2 elicited rapid cell death in grapfruit leaves (Gonchez //et al.//, 2015), detailed enzymatic function has not been determined yet. | ||
| - | |||
| === Interaction partners === | === Interaction partners === | ||
| The XopAG AvrGf2 effector contains a Cyp-binding site that is essential for the elicitation of HR in citrus (Gochez //et al.//, 2017). Yeast two-hybrid experiments showed strong interaction of AvrGf2 with grapefruit cyclophilin (GfCyp), whereas mutation of the GPLL motif in the cyclophilin-binding domain abolished the interaction. | The XopAG AvrGf2 effector contains a Cyp-binding site that is essential for the elicitation of HR in citrus (Gochez //et al.//, 2017). Yeast two-hybrid experiments showed strong interaction of AvrGf2 with grapefruit cyclophilin (GfCyp), whereas mutation of the GPLL motif in the cyclophilin-binding domain abolished the interaction. | ||
| + | |||
| + | The cassava small heat shock protein MeHSP26 was identified as a host target of XopAG, and both proteins were found to interact in both the cytoplasm and nucleus in //Nicotiana benthamiana// | ||
| ===== Conservation ===== | ===== Conservation ===== | ||
| Line 68: | Line 66: | ||
| Rybak M, Minsavage GV, Stall RE, Jones JB (2009). Identification of // | Rybak M, Minsavage GV, Stall RE, Jones JB (2009). Identification of // | ||
| + | |||
| + | Yang L, Wang Y, Yang D, Chen Y, Xiang L, Zhu S, Niu X, Garcia JMP, Morales Rodríguez A, Ou W, Chen Y (2026). // | ||
| ===== Acknowledgements ===== | ===== Acknowledgements ===== | ||