<i>Xanthomonas</i> type III effector XopD targets SUMO‐conjugated proteins <i>in planta</i>

Hotson, Andrew; Chosed, Renée J.; Shu, Hongjun; Orth, Kim; Mudgett, Mary Beth

doi:10.1046/j.1365-2958.2003.03730.x

Cited by 236 publications

(261 citation statements)

References 63 publications

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“…The targets of HopPtoD have not yet been identified. The XopD protein of Xanthomonas campestris has recently been shown to possess SUMO isopeptidase activity and to be nuclear localized, suggesting that it may target nuclear proteins and remove SUMO groups, which are ubiquitin-like peptides that modify the localization and/or stability of proteins (Hotson et al, 2003). As with HopPtoD, the specific targets of XopD, and how it contributes to virulence, are not known.…”

Section: The Biological Functions Of Bacterial Avirulence Proteinsmentioning

confidence: 99%

Guarding the Goods. New Insights into the Central Alarm System of Plants

Innes

2004

Plant Physiology

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Section: The Biological Functions Of Bacterial Avirulence Proteinsmentioning

confidence: 99%

Guarding the Goods. New Insights into the Central Alarm System of Plants

Innes

2004

Plant Physiology

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“…vesicatoria (15). This pathogen is the causative agent of bacterial spot disease in tomato and pepper plants (16).…”

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confidence: 99%

“…The effector proteins are transported through this syringe-like channel in an unfolded state to reach the host cell interior (18), where they interact with specific targets to cause plant cell death (17). In planta, XopD exhibits an isopeptidase activity that reduces the amount of SUMO protein conjugates (15). In vitro, XopD exhibits peptidase and isopeptidase activities (15).…”

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confidence: 99%

“…In planta, XopD exhibits an isopeptidase activity that reduces the amount of SUMO protein conjugates (15). In vitro, XopD exhibits peptidase and isopeptidase activities (15). XopD appears to be plant-specific as evidenced by the fact that, in vitro, it is able to cleave and activate tomato SUMO (T-SUMO), but not mammalian SUMO (M-SUMO).…”

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confidence: 99%

“…XopD appears to be plant-specific as evidenced by the fact that, in vitro, it is able to cleave and activate tomato SUMO (T-SUMO), but not mammalian SUMO (M-SUMO). Likewise, XopD can process plant sumoylated proteins, but not mammalian sumoylated proteins (15). The activity of XopD is inhibited by mutation of the catalytic cysteine to alanine or serine or by treatment with the chemical inhibitors N-ethylmaleimide and iodoacetamide (15).…”

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Structural Analysis of Xanthomonas XopD Provides Insights into Substrate Specificity of Ubiquitin-like Protein Proteases

Chosed

Tomchick

Brautigam

et al. 2007

Journal of Biological Chemistry

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XopD (Xanthomonas outer protein D), a type III secreted effector from Xanthomonas campestris pv. vesicatoria, is a desumoylating enzyme with strict specificity for its plant small ubiquitin-like modifier (SUMO) substrates. Based on SUMO sequence alignments and peptidase assays with various plant, yeast, and mammalian SUMOs, we identified residues in SUMO that contribute to XopD/SUMO recognition. Further predictions regarding the enzyme/substrate specificity were made by solving the XopD crystal structure. By incorporating structural information with sequence alignments and enzyme assays, we were able to elucidate determinants of the rigid SUMO specificity exhibited by the Xanthomonas virulence factor XopD.The small ubiquitin-like modifier (SUMO) 2 is a member of a large family of reversible post-translational modifiers. SUMO is structurally similar to ubiquitin. Like ubiquitin, SUMO utilizes a conjugation machinery (ubiquitin-activating enzyme, ubiquitin carrier protein, and ubiquitin-protein isopeptide ligase) to modify target proteins, but sumoylated proteins are not targeted for degradation by the proteasome (1). The conjugation machinery catalyzes the formation of a covalent isopeptide bond between the C-terminal glycine residue of SUMO and the ⑀-amino group of a lysine residue in the target protein. The removal of SUMO moieties from conjugated proteins by isopeptidases regenerates pools of processed SUMOs and unmodified target proteins.

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Human promyelocytic leukemia protein is targeted to distinct subnuclear domains in plant nuclei and colocalizes with nucleolar constituents in a SUMO‐dependent manner

et al. 2016

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Eukaryotic nuclei are subdivided into subnuclear structures. Among the most prominent of these structures are the nucleolus and the PML nuclear bodies (PML‐NBs). PML‐NBs are spherical multiprotein aggregates of varying size localized in the interchromosomal area. PML‐NB formation is dependent on the presence of the promyelocytic leukemia protein (PML) as well as on post‐translational modification of core components by covalent attachment of the small ubiquitin‐like modifier (SUMO). So far, PML‐NBs as well as PML have been described in mammalian cells only, whereas no orthologs are known in the plant kingdom. In order to investigate conserved mechanisms in PML targeting, we expressed human PML (hPML) fused to the GFP in Nicotiana benthamiana. Using confocal laser scanning microscopy and coimmunoprecipitation followed by mass spectrometric analysis, we found the fusion protein in association with nucleolar constituents. Importantly, mutants of hPML, which are no longer SUMOylated, showed altered localizations, implying SUMO‐dependent targeting of hPML in plants as has previously been shown for mammalian cells. Interestingly, in the presence of proteasome inhibitors, hPML could also be found in the nucleolus of mammalian cells suggesting conserved targeting mechanisms of PML across kingdoms. Finally, Solanum tuberosum COP1, a proposed PML‐like protein from plants, was fused to the red fluorescent protein (RFP) and coexpressed with hPML::eGFP. Microscopic analysis confirmed the localization of COP1::RFP in nuclear speckles. However, hPML::eGFP did not colocalize with COP1::RFP. Hence, we conclude that plants do not possess specialized PML‐NBs, but that their functions may be covered by other subnuclear structures like the nucleolus. Database Proteomics data have been deposited to the ProteomeXchange Consortium with the identifier PXD004254.

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Xanthomonas type III effector XopD targets SUMO‐conjugated proteins in planta

Cited by 236 publications

References 63 publications

Guarding the Goods. New Insights into the Central Alarm System of Plants

Guarding the Goods. New Insights into the Central Alarm System of Plants

Structural Analysis of Xanthomonas XopD Provides Insights into Substrate Specificity of Ubiquitin-like Protein Proteases

Human promyelocytic leukemia protein is targeted to distinct subnuclear domains in plant nuclei and colocalizes with nucleolar constituents in a SUMO‐dependent manner

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