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bacteria:t3e:xopd [2020/07/01 10:19] rkoebnik [References] |
bacteria:t3e:xopd [2020/07/08 18:27] (current) rkoebnik [Biological function] |
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====== XopD ====== | ====== XopD ====== | ||
- | Author: Monika | + | Author: |
- | Internal reviewer: Alice Boulanger\\ | + | Internal reviewer: |
Expert reviewer: FIXME | Expert reviewer: FIXME | ||
Class: XopD (Xanthomonas outer protein D)\\ | Class: XopD (Xanthomonas outer protein D)\\ | ||
- | Family: | + | Family: |
- | Prototype: XopD (// | + | Prototype: XopD (// |
RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
- | 3D structure : [[https:// | + | 3D structure: [[https:// |
===== Biological function ===== | ===== Biological function ===== | ||
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XopD was discovered in a cDNA-AFLP screen and reverse transcription-PCR analyses (Noël //et al//., 2002). | XopD was discovered in a cDNA-AFLP screen and reverse transcription-PCR analyses (Noël //et al//., 2002). | ||
- | |||
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
- | 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, | + | 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 |
- | + | ||
- | 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/ | + | |
+ | Besides C-terminal SUMO protease domain (Hotson //et al//., 2003; Chosed //et al//., 2007), 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 === | === Regulation === | ||
- | The //xopD// gene expression is induced in a //hrpG//- and // | + | The //xopD// gene expression is induced in a //hrpG//- and // |
=== Phenotypes === | === Phenotypes === | ||
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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. | 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. | ||
- | Transgenic expression of XopD< | + | Transgenic expression of XopD< |
=== Localization === | === Localization === | ||
- | 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)). | + | 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 === | === Enzymatic function === | ||
- | Peptidase, isopeptidase or desumoylating enzyme (Hotson//et al//., 2003). | + | Peptidase, isopeptidase or desumoylating enzyme (Hotson// et al//., 2003). |
=== Interaction partners === | === Interaction partners === | ||
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Yes (e.g. // | Yes (e.g. // | ||
- | |||
=== In other plant pathogens/ | === In other plant pathogens/ | ||
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===== References ===== | ===== References ===== | ||
- | Canonne J, Marino D, Jauneau A, Pouzet C, Brière C, Roby D, Rivas S (2011). The // | + | Canonne J, Marino D, Jauneau A, Pouzet C, Brière C, Roby D, Rivas S (2011). The // |
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 // | 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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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:// | 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:// | ||
- | 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:// | + | 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:// |
Rawlings ND, Morton FR, Barrett AJ (2006). MEROPS: the peptidase database. Nucl. Acids Res. 34: D270-D272. DOI: [[https:// | Rawlings ND, Morton FR, Barrett AJ (2006). MEROPS: the peptidase database. Nucl. Acids Res. 34: D270-D272. DOI: [[https:// | ||
Tan CM, Li MY, Yang PY, Chang SH, Ho YP, Lin H, Deng WL, Yang JY (2015). // | Tan CM, Li MY, Yang PY, Chang SH, Ho YP, Lin H, Deng WL, Yang JY (2015). // | ||
+ | |||
+ | ===== Further reading ===== | ||
+ | |||
+ | 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 // | ||
+ | |||
+ | 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:// | ||
+ | |||
+ | Tan L, Rong W, Luo H, Chen Y, He C (2014). The // | ||