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bacteria:t3e:xopc [2020/07/03 17:38] rkoebnik |
bacteria:t3e:xopc [2022/08/12 18:04] rkoebnik [References] |
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Class: XopC\\ | Class: XopC\\ | ||
Family: XopC\\ | Family: XopC\\ | ||
- | Prototype: | + | Prototype: |
RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
- | 3D structure: Unknown | + | 3D structure: Unknown. XopC2 is predicted to be a 661 amino-acids protein with 5 alpha helices and 17 beta strands. It has 21 protein binding and one helical transmembrane region of 18 amino acids (Mondal et al., 2020). |
===== Biological function ===== | ===== Biological function ===== | ||
Line 15: | Line 15: | ||
=== How discovered? === | === How discovered? === | ||
- | XopC was discovered in //Xcv// in a cDNA-AFLP screen (Noël //et al//., 2001). XopC was also identified in a genetic screen, using a Tn// | + | XopC was discovered in //X. campestris// |
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
- | A chimeric protein consisting of XopC fused to a c-myc epitope (first 466 amino acids plus 5 kDa epitope) was secreted into culture supernatants of a strain with a constitutively active form of HrpG in a type III secretion-dependent manner (Noël //et al//., 2003). Another chimeric protein consisting of XopC fused to an N-terminally deleted derivative of the effector protein AvrBs3 (XopC< | + | A chimeric protein consisting of XopC fused to a c-myc epitope (first 466 amino acids plus 5 kDa epitope) was secreted into culture supernatants of a strain with a constitutively active form of HrpG in a type III secretion-dependent manner (Noël //et al//., 2003). Another chimeric protein consisting of XopC fused to an N-terminally deleted derivative of the effector protein AvrBs3 (XopC< |
+ | |||
+ | Type III-dependent secretion was also confirmed using a calmodulin-dependent adenylate cyclase reporter assay, with a Δ//hrpF// mutant strain serving as negative control (Roden //et al//., 2004). | ||
+ | |||
+ | Translocation of the XopC:: | ||
=== Regulation === | === Regulation === | ||
Line 27: | Line 31: | ||
* A deletion of // | * A deletion of // | ||
- | * Roden et al. did not find significant growth defects of a // | + | * Roden et al. did not find significant growth defects of a // |
* Later, 86 // | * Later, 86 // | ||
* The absence of // | * The absence of // | ||
* Virus-induced gene silencing (VIGS) of OAS-TL in planta abolished the acceleration of AvrBs1-mediated HR formation induced by the absence of // | * Virus-induced gene silencing (VIGS) of OAS-TL in planta abolished the acceleration of AvrBs1-mediated HR formation induced by the absence of // | ||
+ | * XopC2 of //X. citri //pv. // | ||
+ | * Ectopic expression of XopC2 was found to promote jasmonate signaling and stomatal opening in transgenic rice plants, which were more susceptible to //X. oryzae// pv. // | ||
=== Localization === | === Localization === | ||
- | XopC localises to the plant cell cytoplasm and the nucleus (Herzfeld, 2013). | + | XopC localises to the plant cell cytoplasm |
=== Enzymatic function === | === Enzymatic function === | ||
- | XopC contains a predicted phosphoribosyl transferase domain and a putative haloacid dehalogenase (HAD)-like hydrolase domain in its C-terminal end. Phenotype of point mutation in catalytic domain have shown that HAD-like hydrolase activity is required for the XopC deleterious effect in yeast (Salomon //et al//., 2011). | + | XopC contains a predicted phosphoribosyl transferase domain and a putative haloacid dehalogenase (HAD)-like hydrolase domain in its C-terminal end. Phenotype of point mutation in catalytic domain have shown that HAD-like hydrolase activity is required for the XopC deleterious effect in yeast (Salomon //et al//., 2011). XopC2 represents a family of atypical kinases that specifically phosphorylate OSK1, a universal adaptor protein of the Skp1-Cullin-F-box ubiquitin ligase complexes (Wang //et al.//, 2021). |
=== Interaction partners === | === Interaction partners === | ||
Line 48: | Line 54: | ||
=== In xanthomonads === | === In xanthomonads === | ||
- | Close, full-length homologs (>90% sequence identity) of XopC1 have only been found in several strains of clade-2 xanthomonads, | + | Close, full-length homologs (>90% sequence identity) of XopC1 have only been found in several strains of clade-2 xanthomonads, |
- | + | ||
- | The distantly related XopC2 has homologs in //X. citri//, //X. euvesicatoria//, | + | |
+ | The distantly related XopC2 has homologs in //X. citri//, //X. axonopodis//, | ||
=== In other plant pathogens/ | === In other plant pathogens/ | ||
- | XopC1: //Ralstonia solanacearum// | + | XopC1: //Ralstonia solanacearum// |
- | XopC2: // | + | XopC2: // |
+ | ===== Conservation ===== | ||
+ | |||
+ | === In xanthomonads === | ||
+ | |||
+ | Close, full-length homologs (>90% sequence identity) of XopC1 have only been found in several strains of clade-2 xanthomonads, | ||
+ | |||
+ | The distantly related XopC2 has homologs in //X. citri//, //X. axonopodis//, | ||
+ | === In other plant pathogens/ | ||
+ | |||
+ | XopC1: //Ralstonia solanacearum// | ||
+ | |||
+ | XopC2: // | ||
===== References ===== | ===== References ===== | ||
- | Adlung N, Prochaska H, Thieme S, Banik A, Blüher D, John P, Nagel O, Schulze S, Gantner J, Delker C, Stuttmann J, Bonas U (2006). Non-host resistance induced by the // | + | Adlung N, Prochaska H, Thieme S, Banik A, Blüher D, John P, Nagel O, Schulze S, Gantner J, Delker C, Stuttmann J, Bonas U (2006). Non-host resistance induced by the // |
- | Büttner D, Lorenz C, Weber E, Bonas U (2006). Targeting of two effector protein classes to the type III secretion system by a HpaC- and HpaB-dependent protein complex from // | + | Büttner D, Lorenz C, Weber E, Bonas U (2006). Targeting of two effector protein classes to the type III secretion system by a HpaC- and HpaB-dependent protein complex from // |
Herzfeld EM (2013). Identifizierung und Charakterisierung von dem pflanzlichen Interaktionspartner OAS-TL des Typ-III-Effektors XopC. Doctoral Thesis, Martin-Luther-Universität Halle-Wittenberg, | Herzfeld EM (2013). Identifizierung und Charakterisierung von dem pflanzlichen Interaktionspartner OAS-TL des Typ-III-Effektors XopC. Doctoral Thesis, Martin-Luther-Universität Halle-Wittenberg, | ||
- | Liu Y, Long J, Shen D, Song C (2016). // | + | Liu Y, Long J, Shen D, Song C (2016). // |
+ | < | ||
+ | |||
+ | Noël L, Thieme F, Gäbler J, Büttner D, Bonas U (2003). XopC and XopJ, two novel type III effector proteins from // | ||
- | Noël L, Thieme F, Gäbler J, Büttner | + | Noël L, Thieme F, Nennstiel |
- | Noël L, Thieme F, Nennstiel D, Bonas U (2001). cDNA-AFLP analysis unravels a genome-wide // | + | Roden JA, Belt B, Ross JB, Tachibana T, Vargas J, Mudgett MB (2004). A genetic screen to isolate type III effectors translocated into pepper cells during |
- | Roden JA, Belt B, Ross JB, Tachibana T, Vargas J, Mudgett MB (2004). A genetic screen to isolate type III effectors translocated into pepper cells during | + | Salomon D, Dar D, Sreeramulu S, Sessa G (2011). Expression of // |
- | Salomon D, Dar D, Sreeramulu S, Sessa G (2011). Expression | + | Szurek B, Rossier O, Hause G, Bonas U (2002). Type III-dependent translocation |
- | Szurek B, Rossier O, Hause G, Bonas U (2002). Type III-dependent translocation of the // | + | Wang S, Li S, Wang J, Li Q, Xin XF, Zhou S, Wang Y, Li D, Xu J, Luo ZQ, He SY, Sun W (2021). A bacterial kinase phosphorylates OSK1 to suppress stomatal immunity in rice. Nat. Commun.12: 5479. doi: [[https:// |