bacteria:t3e:xopm
Differences
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| bacteria:t3e:xopm [2024/12/17 11:10] – fboernke | bacteria:t3e:xopm [2025/02/13 12:37] (current) – jfpothier | ||
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| Author: [[https:// | Author: [[https:// | ||
| - | Expert reviewer: | + | Expert reviewer: |
| Class: XopM\\ | Class: XopM\\ | ||
| Line 14: | Line 14: | ||
| === How discovered? === | === How discovered? === | ||
| - | //xopM// < | + | //xopM// < |
| - | < | + | |
| - | < | + | |
| - | < | + | |
| === (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
| Line 23: | Line 21: | ||
| To test for T3SS-dependent translocation into plant cells, //Xee// < | To test for T3SS-dependent translocation into plant cells, //Xee// < | ||
| + | |||
| === Regulation === | === Regulation === | ||
| Expression of //xopM// < | Expression of //xopM// < | ||
| + | |||
| === Phenotypes === | === Phenotypes === | ||
| - | The //Xee// < | + | The // |
| + | |||
| + | To identify defense reactions, mediated by //xopM//, leaves of pepper ECW, //Nicotiana benthamiana// | ||
| + | When ectopically expressed in plants, XopM supports growth of a non-pathogenic bacterial strain and dampens the production of reactive oxygen species, indicating its ability to suppress plant immunity (Brinkmann et al., 2024). The abilty to repress a flg22 induced ROS burst is independent of XopM binding to VAP but requires localization at the host cell plasma membrane (see below, Brinkmann et al., 2024). | ||
| - | To identify defense reactions, mediated by //xopM//, leaves of pepper ECW, //Nicotiana benthamiana// | ||
| === Localization === | === Localization === | ||
| - | XopM-GFP fusions have been shown to localize to the plant plasma membrane (PM) in //N. benthamiana //leaf epidermal cells. Possibly concentrated in ER-PM contact sites (Brinkmann et al., 2024) | + | XopM-GFP fusions have been shown to localize to the plant plasma membrane (PM) in //N. benthamiana// |
| === Enzymatic function === | === Enzymatic function === | ||
| Line 40: | Line 42: | ||
| === Interaction partners === | === Interaction partners === | ||
| - | XopM interacts with vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) in an isoform specific manner. XopM displays two FFAT [two phenylalanines (FF) in an acidic tract (AT)] motifs that cooperatively mediate the interaction with VAP. Binding to VAP is not required for XopM's ability to suppress PTI, indicating that it has other virulence targets. In planta pull-down assays using XopM-GFP as a bait, suggest that it interacts with additional membrane components (Brinkmann et al., 2024). | + | XopM interacts with vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) in an isoform specific manner. XopM displays two FFAT [two phenylalanines (FF) in an acidic tract (AT)] motifs that cooperatively mediate the interaction with VAP. Binding to VAP is not required for XopM's ability to suppress PTI, indicating that it has other virulence targets. |
| ===== Conservation ===== | ===== Conservation ===== | ||
bacteria/t3e/xopm.1734433814.txt.gz · Last modified: 2024/12/17 11:10 by fboernke
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