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bacteria:t3e:xopj1 [2020/06/25 17:33] joana_costa [XopJ1] |
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- | ===== Biological function ===== | ||
- | |||
- | === How discovered? === | ||
- | |||
- | XopJ was initially discovered as a HrpG-induced gene in a cDNA-AFLP screen in // | ||
- | === (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 the interaction of XopJ with the effector chaperone HpaB or HrcQ from the bacterial type III secretion system (Scheibner //et al//., 2018). | ||
- | === Regulation === | ||
- | |||
- | //xopJ// is expressed in a //hrpG-// and // | ||
- | === 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, | ||
- | === Localization === | ||
- | |||
- | Following type III translocation, | ||
- | === Enzymatic function === | ||
- | |||
- | XopJ belongs to the group of YopJ-family effectors. These are characterized as C55 cysteine proteases, ubiquitin-like proteases (deSUMOylation), | ||
- | === 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. | ||
- | |||
- | ===== Conservation ===== | ||
- | |||
- | XopJ belongs to the broadly occurring YopJ-effector family of cysteine proteases/ | ||
- | |||
- | === In xanthomonads === | ||
- | |||
- | Yes (//e.g.//, //X. campestris// | ||
- | === In other plant pathogens/ | ||
- | |||
- | Yes (//e.g.//, many // | ||
- | ===== References ===== | ||
- | |||
- | Bartetzko V, Sonnewald S, Vogel F, Hartner K, Stadler R, Hammes UZ, Börnke F (2009). The // | ||
- | |||
- | Noël L, Thieme F, Nennstiel D, Bonas U (2001). cDNA-AFLP analysis unravels a genome-wide // | ||
- | |||
- | Noël L, Thieme F, Gäbler J, Büttner D, Bonas U (2003). XopC and XopJ, two novel type III effector proteins from // | ||
- | |||
- | 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 // | ||
- | |||
- | Thieme F, Szczesny R, Urban A, Kirchner O, Hause G, Bonas U (2007). New type III effectors from // | ||
- | |||
- | Üstün S, Bartetzko V, Börnke F (2013). The // | ||
- | |||
- | Üstün S, Börnke F (2014). Interactions of // | ||
- | |||
- | Üstün S, Börnke F (2015). The // | ||
- | |||
- | Üstün S, Bartetzko V, Börnke F (2015). The // | ||
- | |||
- | White F, Potnis N, Jones JB, Koebnik R (2009) The type III effectors of // | ||
- | |||
- | ===== Biological function ===== | ||
- | |||
- | === 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). | ||
- | |||
- | === (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). | ||
- | |||
- | === Regulation === | ||
- | //xopJ// is expressed in a //hrpG-// and // | ||
- | |||
- | === 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, | ||
- | |||
- | === Localization === | ||
- | Following type III translocation, | ||
- | |||
- | === Enzymatic function === | ||
- | XopJ belongs to the group of YopJ-family effectors. These are characterized as C55 cysteine proteases, ubiquitin-like proteases (deSUMOylation), | ||
- | |||
- | === 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. | ||
- | |||
- | ===== Conservation ===== | ||
- | XopJ belongs to the broadly occuring YopJ-effector family of cysteine proteases/ | ||
- | |||
- | === In xanthomonads === | ||
- | Yes (//e.g.//, //X. campestris// | ||
- | |||
- | === In other plant pathogens/ | ||
- | Yes (//e.g.//, many // | ||
- | |||
- | ===== References ===== | ||
- | |||
- | Bartetzko V, Sonnewald S, Vogel F, Hartner K, Stadler R, Hammes UZ, Börnke F (2009). The // | ||
- | |||
- | Noël L, Thieme F, Nennstiel D, Bonas U (2001). cDNA-AFLP analysis unravels a genome-wide // | ||
- | |||
- | Noël L, Thieme F, Gäbler J, Büttner D, Bonas U (2003). XopC and XopJ, two novel type III effector proteins from // | ||
- | |||
- | 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 // | ||
- | |||
- | Thieme F, Szczesny R, Urban A, Kirchner O, Hause G, Bonas U (2007). New type III effectors from // | ||
- | |||
- | Üstün S, Bartetzko V, Börnke F (2013). The // | ||
- | |||
- | Üstün S, Börnke F (2014). Interactions of // | ||
- | |||
- | Üstün S, Börnke F (2015). The // | ||
- | |||
- | Üstün S, Bartetzko V, Börnke F (2015). The // | ||
- | |||
- | White F, Potnis N, Jones JB, Koebnik R (2009) The type III effectors of // | ||