bacteria:t3e:xopag
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| bacteria:t3e:xopag [2020/05/18 14:07] – created jfpothier | bacteria:t3e:xopag [2025/02/12 23:22] (current) – jfpothier | ||
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| - | ====== XopAG ====== | + | ====== |
| - | Author: | + | Author: |
| - | Internal reviewer: | + | Internal reviewer: |
| - | Expert reviewer: | + | Expert reviewer: |
| - | Class: | + | Class: |
| - | Family: XopAG\\ | + | Families: XopAG1, XopAG2\\ |
| - | Prototype: | + | Prototype: |
| - | RefSeq ID: [[https:// | + | GenBank ID (AvrGf1): [[https:// |
| - | 3D structure: | + | GenBank ID (AvrGf2): [[https:// |
| + | RefSeq ID (XopAG1): [[https:// | ||
| + | RefSeq ID (XopAG2): [[https:// | ||
| + | Synonym: AvrGf1, AvrGf2\\ | ||
| + | 3D structure: | ||
| ===== Biological function ===== | ===== Biological function ===== | ||
| - | === How discovered? === | + | === How discovered? === |
| - | // | + | |
| - | Genes //avrGf1// and //avrGf2// were found to share low sequence similarity at the nucleotide level, except for a small region in the last 200 nucleotides of the genes, which showed a high level of identity (68%) (Gochez //et al//., 2017). The alignment of translated proteins AvrGf1 (533 amino acids) and AvrGf2 (509 amino acids) determined that AvrGf2 had a low degree of sequence identity (45% amino acid identity) with the previously identified AvrGf1. The highest sequence similarities were observed between AvrGf1 and AvrGf2 in the C-terminal portions of the effector proteins (74.5% identity at the amino acid level over 51 amino acids) (Gochez //et al//., 2017). | + | |
| + | // | ||
| === (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). | ||
| === 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< | ||
| === 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. | ||
| === Enzymatic function === | === Enzymatic function === | ||
| + | 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). | ||
| + | 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. | ||
| ===== Conservation ===== | ===== Conservation ===== | ||
| === In xanthomonads === | === In xanthomonads === | ||
| - | Yes (e.g. //X.c.// pv. // | ||
| + | Yes (//e.g.//, //X. campestris//, | ||
| === In other plant pathogens/ | === In other plant pathogens/ | ||
| - | Yes (e.g. //P.s.// pv. // | ||
| + | Yes (//e.g.//, //P. syringae.// pv. // | ||
| ===== References ===== | ===== References ===== | ||
| - | Escalon A, Javegny S, Vernière C, Noël LD, Vital K, Poussier S, Hajri A, Boureau T, Pruvost O, Arlat M, Gagnevin L 2013. Variations in type III effector repertoires, | ||
| - | Figueiredo JF, Romer P, Lahaye | + | Escalon A, Javegny S, Vernière C, Noël LD, Vital K, Poussier S, Hajri A, Boureau |
| - | Gochez AM, Shantharaj D, Potnis N, Zhou X, Minsavage GV, White FF, Wang N, Hurlbert JC, Jones JB 2017. Molecular characterization of XopAG effector AvrGf2 from //Xanthomonas fuscans// ssp. // | + | Figueiredo JF, Romer P, Lahaye T, Graham JH, White FF, Jones JB (2011). //Agrobacterium//-mediated transient expression |
| - | Rybak M, Minsavage GV, Stall RE, Jones JB 2009. Identification of // | + | Gochez AM, Minsavage GV, Potnis N, Canteros BI, Stall RE, Jones JB (2015). A functional XopAG homologue in // |
| + | Gochez AM, Shantharaj D, Potnis N, Zhou X, Minsavage GV, White FF, Wang N, Hurlbert JC, Jones JB (2017). Molecular characterization of XopAG effector AvrGf2 from // | ||
| + | Jalan N, Kumar D, Andrade MO, Yu F, Jones JB, Graham JH, White FF, Setubal JC, Wang N (2013). Comparative genomic and transcriptome analyses of pathotypes of // | ||
| + | |||
| + | Rybak M, Minsavage GV, Stall RE, Jones JB (2009). Identification of // | ||
| + | |||
| + | ===== Acknowledgements ===== | ||
| + | |||
| + | This fact sheet is based upon work from COST Action CA16107 EuroXanth, supported by COST (European Cooperation in Science and Technology). | ||
bacteria/t3e/xopag.1589807278.txt.gz · Last modified: 2023/01/09 10:20 (external edit)
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