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bacteria:t3e:xopk [2020/07/08 19:24] rkoebnik [References] |
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- | ===== Biological function ===== | ||
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- | === How discovered? === | ||
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- | XopK was discovered using a machine-learning approach (Furutani //et al//., 2006). | ||
- | === (Experimental) evidence for being a T3E === | ||
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- | Mutation of a putative ubiquitin-conjugation enzyme (E2) binding site abolished XopK-induced degradation of rice somatic receptor kinase 2 (OsSERK2) and compromised XopK-dependent virulence (Qin //et al//., 2018). | ||
- | === Regulation === | ||
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- | Preceded by both a PIP box and a -10 box-like motif (Schulze //et al//., 2012; Furutani //et al//., 2006). | ||
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- | qRT-PCR revealed that transcript levels of 15 out of 18 tested non-TAL effector genes (as well as the regulatory genes //hrpG// and //hrpX//), including //xopK//, were significantly reduced in the // | ||
- | === Phenotypes === | ||
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- | * Deletion of XopK has been shown not to affect the virulence of //X. oryzae// | ||
- | * A ∆// | ||
- | * XopK inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades (Qin //et al.//, 2018) | ||
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- | === Localization === | ||
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- | The XopK sequence contains 54% hydrophobic residues and several predicted transmembrane domains. Thus, it is possible this protein is associated with host cell membranes following secretion (Mutka //et al//., 2016) | ||
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- | === Enzymatic function === | ||
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- | The protein has E3 ubiquinol ligase activity. The putative E2-binding site is highly conserved in the majority of members from different // | ||
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- | === Interaction partners === | ||
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- | XopK interacted with and directly ubiquitinated rice somatic embryogenic receptor kinase 2 (OsSERK2), resulting in its degradation (Qin //et al//., 2018) | ||
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- | ===== Conservation ===== | ||
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- | === In xanthomonads === | ||
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- | Yes (based on EDGAR; e.g., //X. oryzae// | ||
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- | === In other plant pathogens/ | ||
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- | Yes (e.g., // | ||
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- | ===== References ===== | ||
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- | Furutani A, Nakayama T, Ochiai H, Kaku H, Kubo Y, Tsuge S (2006). Identification of novel HrpXo regulons preceded by two // | ||
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- | Furutani A, Takaoka M, Sanada H, Noguchi Y, Oku T, Tsuno K, Ochiai H, Tsuge S (2009). Identification of novel type III secretion effectors in // | ||
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- | Liu Y, Long J, Shen D, Song C (2016). // | ||
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- | Mutka AM, Fentress SJ, Sher SW, Berry JC, Pretz C, Nusinow DA, Bart R (2016). Quantitative, | ||
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- | Qin J, Zhou X, Sun L, Wang K, Yang F, Liao H, Rong W, Yin J, Chen H, Chen X, Zhang J (2018). The // | ||
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- | Schulze S, Kay S, Büttner D, Egler M, Eschen-Lippold L, Hause G, Krüger A, Lee J, Müller O, Scheel D, Szczesny R, Thieme F, Bonas U (2012). Analysis of new type III effectors from // | ||
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- | Song C, Yang B (2010). Mutagenesis of 18 type III effectors reveals virulence function of XopZ< | ||