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bacteria:t3e:xopj1 [2020/04/22 21:58] – external edit 127.0.0.1 | bacteria:t3e:xopj1 [2025/07/04 23:36] (current) – jfpothier | ||
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- | ====== XopJ1 ====== | + | ====== |
- | Author: Jens Boch\\ | + | Author: |
- | Internal reviewer: | + | Internal reviewer: |
- | Expert reviewer: | + | Expert reviewer: |
Class: XopJ\\ | Class: XopJ\\ | ||
Family: XopJ1\\ | Family: XopJ1\\ | ||
- | Prototype: | + | Prototype: |
- | RefSeq | + | GenBank |
+ | RefSeq ID: [[https:// | ||
3D structure: Unknown | 3D structure: Unknown | ||
Line 14: | Line 15: | ||
=== How discovered? === | === How discovered? === | ||
- | XopJ was initially discovered as a HrpG-induced gene in a cDNA-AFLP screen in //Xcv// and identified as a homolog to YopJ from //Yersinia pestis// (Noël //et al//., 2001). XopJ later studied in more detail (Noël //et al//., 2003). | + | |
+ | XopJ was initially discovered as a HrpG-induced gene in a cDNA-AFLP screen in // | ||
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
- | A chimeric protein consisting of the 155 N-terminal amino acids of XopJ fused to an N-terminally truncated AvrBs3 is secreted out of the bacterial cell and elicits a hypersensitive response in a //Bs3// pepper plant. Secretion and translocation are dependent on components of the //Xcv// type III secretion system (//hrcV//) and translocon (//hrpF//) (Noël //et al//., 2003). The first 50 amino acids of XopJ are sufficient and the amino acids 2-8 required for secretion (Scheibner //et al//., 2018). This minimal secretion signal is not required for interaction of XopJ with the effector chaperone HpaB or HrcQ from the bacterial type III secretion system (Scheibner //et al//., 2018). | + | |
+ | A chimeric protein consisting of the 155 N-terminal amino acids of XopJ fused to an N-terminally truncated AvrBs3 is secreted out of the bacterial cell and elicits a hypersensitive response in a //Bs3// pepper plant. Secretion and translocation are dependent on components of the //Xcv// type III secretion system (//hrcV//) and translocon (//hrpF//) (Noël //et al//., 2003). The first 50 amino acids of XopJ are sufficient and the amino acids 2-8 required for secretion (Scheibner //et al//., 2018). This minimal secretion signal is not required for the interaction of XopJ with the effector chaperone HpaB or HrcQ from the bacterial type III secretion system (Scheibner //et al//., 2018). | ||
=== Regulation === | === Regulation === | ||
+ | |||
//xopJ// is expressed in a //hrpG-// and // | //xopJ// is expressed in a //hrpG-// and // | ||
=== Phenotypes === | === Phenotypes === | ||
- | Although a frameshift mutation of //xopJ// did not affect pathogenicity or bacterial growth in plants in early experiments (Noël //et al//., 2003), later studies showed that a //xopJ// mutant is slightly impaired in growth in pepper in late stages of the infection (Üstun //et al//., 2013). XopJ also suppresses | + | |
+ | Although a frameshift mutation of //xopJ// did not affect pathogenicity or bacterial growth in plants in early experiments (Noël //et al//., 2003), later studies showed that a //xopJ// mutant is slightly impaired in growth in pepper in late stages of the infection (Üstun //et al//., 2013). XopJ also suppresses | ||
=== Localization === | === Localization === | ||
- | Following type III translocation, | + | |
+ | XopJ carries a predicted N-myristoylation motif on a glycine residue at position two of the polypeptide. | ||
=== Enzymatic function === | === Enzymatic function === | ||
- | XopJ belongs to the group of YopJ-family effectors. These are characterized as C55 cysteine proteases, ubiquitin-like proteases (deSUMOylation), | + | |
+ | XopJ belongs to the group of YopJ-family effectors | ||
=== Interaction partners === | === Interaction partners === | ||
- | 19S RP subunit RPT6 (RP ATPase 6) of the 26S proteasome (Üstun | + | |
+ | 19S RP subunit RPT6 (RP ATPase 6) of the 26S proteasome (Üstün | ||
===== Conservation ===== | ===== Conservation ===== | ||
- | XopJ belongs to the broadly | + | |
+ | XopJ belongs to the broadly | ||
=== In xanthomonads === | === In xanthomonads === | ||
+ | |||
Yes (//e.g.//, //X. campestris// | Yes (//e.g.//, //X. campestris// | ||
+ | === In other plant pathogens/ | ||
- | === In other plant pathogens/ | ||
Yes (//e.g.//, many // | Yes (//e.g.//, many // | ||
===== References ===== | ===== References ===== | ||
- | Bartetzko V, Sonnewald S, Vogel F, Hartner K, Stadler R, Hammes UZ, Börnke F (2009). The // | + | Bartetzko V, Sonnewald S, Vogel F, Hartner K, Stadler R, Hammes UZ, Börnke F (2009). The // |
+ | |||
+ | 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, Nennstiel D, Bonas U (2001). cDNA-AFLP analysis unravels a genome-wide // | ||
- | Noël L, Thieme | + | Scheibner |
- | Noël L, Thieme F, Gäbler J, Büttner D, Bonas U (2003). XopC and XopJ, two novel type III effector proteins | + | Thieme F, Szczesny R, Urban A, Kirchner O, Hause G, Bonas U (2007). New type III effectors |
- | Scheibner F, Hartmann N, Hausner J, Lorenz C, Hoffmeister A-K, Büttner D (2018). The type III secretion chaperone HpaB controls the translocation of effector and noneffector proteins from // | + | Üstün S, Bartetzko V, Börnke F (2013). The // |
- | Thieme F, Szczesny R, Urban A, Kirchner O, Hause G, Bonas U (2007). New type III effectors from // | + | Üstün S, Bartetzko V, Börnke F (2015). The // |
- | Üstün S, Bartetzko V, Börnke F (2013). The // | + | Üstün S, Börnke F (2014). Interactions of // |
- | Üstün S, Börnke F (2014). Interactions of // | + | Üstün S, Börnke F (2015). The // |
- | Üstün S, Börnke | + | White F, Potnis N, Jones JB, Koebnik R (2009). The type III effectors of // |
- | Üstün S, Bartetzko V, Börnke F (2015). The // | + | ===== Acknowledgements ===== |
- | White F, Potnis N, Jones JB, Koebnik R (2009) The type III effectors of // | + | This fact sheet is based upon work from COST Action CA16107 EuroXanth, supported by COST (European Cooperation in Science and Technology). |