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- | ====== XopD ====== | ||
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- | Author: [[https:// | ||
- | Internal reviewer: [[https:// | ||
- | Expert reviewer: FIXME | ||
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- | Class: XopD (Xanthomonas outer protein D)\\ | ||
- | Family: family C48 (Rawlings //et al//., 2006)\\ | ||
- | Prototype: XopD (// | ||
- | RefSeq ID: [[https:// | ||
- | 3D structure: [[https:// | ||
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- | ===== Biological function ===== | ||
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- | === How discovered? === | ||
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- | XopD was discovered in a cDNA-AFLP screen and reverse transcription-PCR analyses (Noël //et al//., 2002). | ||
- | === (Experimental) evidence for being a T3E === | ||
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- | XopD is a desumoylating enzyme with strict specificity for its plant small ubiquitin-like modifier (SUMO) substrates (Chosed //et al//., 2007). C-terminus of XopD (amino acids 322–520) shares primary sequence similarity with the C48 family of cysteine peptidases. In the XopD polypeptide, | ||
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- | Besides C-terminal SUMO protease domain (Chosed //et al//., 2007; Hotson //et al//., 2003), XopD has a unique N-terminal region with a host range determining non-specific DNA-binding domain (DBD) (Kim //et al//., 2011) and a central domain with two internal ERF-associated amphiphilic repression (EAR) motifs (L/ | ||
- | === Regulation === | ||
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- | The //xopD// gene expression is induced in a //hrpG//- and // | ||
- | === Phenotypes === | ||
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- | XopD is a unique virulence factor that promotes tolerance to //Xcv// 85-10 in infected host leaves and affects bacteria miltiplication (Kim //et al//., 2008). It was found that delays the onset leaf chlorosis and necrosis, two phenotypes associated with pathogen-triggered immunity (PTI) activation (Kim //et al//., 2008). Delaying in tissue damages and lower chlorophyll loss corelate with reduced host defense transcription and reduced salicylic acid (SA) levels-plant defense hormone that limits the spread of pathogens in infected host plant. Moreover, expression of XopD //in planta// is sufficient to repress not only SA- but also jasmonic acid–induced gene transcription (Hotson //et al//., 2003; Kim //et al//., 2008; Kim //et al//., 2011). It was also shown that XopD highly induces the tomato transcription factor, bHLH132 (Kim //et al//., 2019). This induction is dependant of XopD SUMO protease activity. This sutdy has shown that is involved in both plant development and plant defense regulation and that silencing bHLH132 mRNA expression results in stuned tomato with enhanced susceptibility to //Xcv// infection. | ||
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- | For instance, XcvΔ// | ||
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- | Comparative analysis of the XopD effector family in other phytopathogenic bacteria revealed that so called XopD-like proteins presents differences in sequence and length of their N-terminal domains. This suggests that the N-terminal domain of XopD and XopD-like effectors might impart substrate and/or host specificity. | ||
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- | Transgenic expression of XopD< | ||
- | === Localization === | ||
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- | XopD localizes to subnuclear foci. The N terminus of XopD is required for targeting the effector to the plant nucleus; C-terminal domain encodes a Cys protease that cleaves SUMO-conjugated proteins (Hotson //et al//., 2003; Kim //et al//., 2008)). | ||
- | === Enzymatic function === | ||
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- | Peptidase, isopeptidase or desumoylating enzyme (Hotson//et al//., 2003). | ||
- | === Interaction partners === | ||
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- | Unknown. | ||
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- | ===== Conservation ===== | ||
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- | === In xanthomonads === | ||
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- | Yes (e.g. // | ||
- | === In other plant pathogens/ | ||
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- | Yes (// | ||
- | ===== References ===== | ||
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- | Canonne J, Marino D, Jauneau A, Pouzet C, Brière C, Roby D, Rivas S (2011). The // | ||
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- | Canonne J, Pichereaux C, Mario D, Roby D, Rossignol M, Rivas S (2012). Identification of the protein sequence of the type III effector XopD from the B100 strain of // | ||
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- | Castaneda A, Reddy JD, El-Yacoubi B, Gabriel DW (2005). Mutagenesis of all eight //avr// genes in // | ||
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- | Chosed R, Tomchick DR, Brautigam CA, Mukherjee S, Negi VS, Machius M, Orth K (2007). Structural analysis of // | ||
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- | Hotson A, Chosed R, Shu H, Orth K, Mudgett MB (2003). // | ||
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- | Innes RW, Bent AF, Kunkel BN, Bisgrove SR, Staskawicz BJ (1993). Molecular analysis of avirulence gene //avrRpt2// and identification of a putative regulatory sequence common to all known // | ||
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- | Kim JG, Taylor KW, Hotson A, Keegan M, Schmelz EA, Mudgett MB (2008). XopD SUMO protease affects host transcription, | ||
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- | Kim JG, Stork W, Mudgett MB (2013). // | ||
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- | Kim JG, Taylor KW, Mudgett MB (2011). Comparative analysis of the XopD type III secretion (T3S) effector family in plant pathogenic bacteria. Mol. Plant Pathol. 12: 715-730. DOI: [[https:// | ||
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- | Li SJ, Hochstrasser M (1999). A new protease required for cell-cycle progression in yeast. Nature 398: 246-251. DOI: [[https:// | ||
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- | Noël L, Thieme F, Nennstiel D, Bonas U (2002). Two novel type III-secreted proteins of // | ||
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- | Ohta M, Matsui K, Hiratsu K, Shinshi H, Ohme-Takagi M (2001). Repression domains of class II ERF transcriptional repressors share an essential motif for active repression. Plant Cell 13: 1959-1968. DOI: [[https:// | ||
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- | Pruneda JN, Durkin CH, Geurink PP, Ovaa H, Santhanam B, Holden DW, Komander D (2016). The molecular basis for ubiquitin and ubiquitin-like specificities in bacterial effector proteases. Mol. Cell 63: 261-276. DOI: [[https:// | ||
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- | Rawlings ND, Morton FR, Barrett AJ (2006). MEROPS: the peptidase database. Nucl. Acids Res. 34: D270-D272. DOI: [[https:// | ||
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- | Tan CM, Li MY, Yang PY, Chang SH, Ho YP, Lin H, Deng WL, Yang JY (2015). // | ||
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- | ===== Further reading ===== | ||
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- | Canonne J, Marino D, Noël LD, Arechaga I, Pichereaux C, Rossignol M, Roby D, Rivas S (2010). Detection and functional characterization of a 215 amino acid N-terminal extension in the // | ||
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- | Raffaele S, Rivas S (2013). Regulate and be regulated: integration of defense and other signals by the AtMYB30 transcription factor. Front. Plant Sci. 4: 98. DOI: [[https:// | ||
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- | Tan L, Rong W, Luo H, Chen Y, He C (2014). The // | ||