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bacteria:t3e:xopag [2025/02/12 23:22] – jfpothier | bacteria:t3e:xopag [2025/07/24 22:24] (current) – jfpothier | ||
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Author: [[https:// | Author: [[https:// | ||
Internal reviewer: [[https:// | Internal reviewer: [[https:// | ||
- | Expert reviewer: [[https:// | + | Expert reviewer: [[https:// |
Class: XopAG\\ | Class: XopAG\\ | ||
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// | // | ||
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=== (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). | ||
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=== 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< | ||
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=== Phenotypes === | === Phenotypes === | ||
- | All // | + | All // |
=== 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. | ||
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=== 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. | ||
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=== 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. | ||
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===== Conservation ===== | ===== Conservation ===== | ||
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Yes (//e.g.//, //X. campestris//, | Yes (//e.g.//, //X. campestris//, | ||
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=== In other plant pathogens/ | === In other plant pathogens/ | ||
Yes (//e.g.//, //P. syringae.// pv. // | Yes (//e.g.//, //P. syringae.// pv. // | ||
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===== References ===== | ===== References ===== | ||