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bacteria:t3e:xopj1 [2020/04/22 21:58] – external edit 127.0.0.1 | bacteria:t3e:xopj1 [2025/02/13 11:38] (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 cell death reactions during //Xcv// infection of its susceptible host plant pepper. The activity of the proteasome is required for this cell death. XopJ further suppresses defence-related callose deposition and secretion of extracellular proteins (secGFP) from the plant cell (Bartetzko //et al//., 2009). The XopJ protein interacts with RPT6 from the 26S proteasome in yeast and in planta and recruits RPT6 to the plant plasma membrane which leads to inhibition of the proteasome activity. For this activity, the myristoylation sequence and the catalytic triad are required (Üstun //et al//., 2013). Furthermore, | ||
+ | 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 tissue necrosis during //Xcv// infection of its susceptible host plant pepper. XopJ further suppresses defence-related callose deposition and secretion of extracellular proteins (secGFP) from the plant cell (Bartetzko //et al//., 2009). The XopJ protein interacts with the proteasomal subunit Regulatory Particle AAA-ATPase6 (RPT6) from the 26S proteasome in yeast and in planta and recruits RPT6 to the plant plasma membrane which leads to inhibition of the proteasome activity. For this activity, the myristoylation sequence and the catalytic triad are required (Üstün //et al//., 2013). The ability of XopJ to inhibit the proteasome is directly related to its function in cell death suppression. The interaction of XopJ with RPT6 leads to degradation of the latter, which depends on the XopJ catalytic Cys residue indicating that XopJ acts as protease (Üstun & Börnke, 2015). The inhibition of proteasome activity results in the inhibition of NPR1 turnover and subsequent salicylic acid-related immune responses (Üstün //et al//., 2013; Üstün & Börnke, 2015). The degradation of RPT6 is dependent on the Walker B motif (ATP hydrolysis) of RPT6 (Üstün & Börnke, 2015). Furthermore, | ||
=== Localization === | === Localization === | ||
- | Following type III translocation, | ||
+ | XopJ carries a predicted N-myristoylation motif on a glycine residue at position two of the polypeptide. Following type III translocation, | ||
=== 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 and is a member of the YopJ/AvrRxv family of SUMO peptidases and acetyltransferases. These are characterized as C55 cysteine proteases, ubiquitin-like proteases (deSUMOylation), | ||
=== Interaction partners === | === Interaction partners === | ||
- | 19S RP subunit RPT6 (RP ATPase 6) of the 26S proteasome (Üstun & Börnke, 2015). The interaction is dependent on the Walker A motif (ATP binding) of RPT6. | ||
+ | 19S RP subunit RPT6 (RP ATPase 6) of the 26S proteasome (Üstün & Börnke, 2015). The interaction is dependent on the Walker A motif (ATP binding) of RPT6. The interaction between the two proteins has been shown by yeast two-hybrid assays, //in vivo// and //in vitro// pull-down, as well as by bimolecular fluorescence assays //in planta// (Üstün et al., 2013). | ||
===== 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). |