ArticleScientific reports2015
Identification of enzymes involved in SUMOylation in Trypanosoma brucei.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 17 citations in OpenAlex.
- Two Centrins and Their Posttranslational Modification Modulate the Cell Cycle of Giardia lamblia.MicrobiologyOpen · 2025Article
- Deubiquitinase USP39 and E3 ligase TRIM26 balance the level of ZEB1 ubiquitination and thereby determine the progression of hepatocellular carcinoma.Cell death and differentiation · 2021Article
- Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.Biomolecules · 2020Review
- Leishmania differentiation requires ubiquitin conjugation mediated by a UBC2-UEV1 E2 complex.PLoS pathogens · 2020Article
- Ubiquitination and the Proteasome as Drug Targets in Trypanosomatid Diseases.Frontiers in chemistry · 2020Review
- NEK7 interacts with NLRP3 to modulate the pyroptosis in inflammatory bowel disease via NF-κB signaling.Cell death & disease · 2019Article
- Farnesoid X receptor interacts with cAMP response element binding protein to modulate glucagon-like peptide-1 (7-36) amide secretion by intestinal L cell.Journal of cellular physiology · 2019Article
- Article
- High-throughput Methods for Dissection of Trypanosome Gene Regulatory Networks.Current genomics · 2018Review
- Biosynthesis of SUMOylated Proteins in Bacteria Using the Trypanosoma brucei Enzymatic System.PloS one · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small ubiquitin-like modifier (SUMO), a reversible post-translational protein modifier, plays important roles in diverse cellular mechanisms. Three enzymes, E1 (activating enzyme), E2 (conjugating enzyme) and E3 (ligase), are involved in SUMO modification. SUMOylation system and process in higher eukaryotes have been well studied. However, in protozoa, such as Trypanosoma brucei (T. brucei), these remain poorly understood. Herein, we identified the E1 (TbAos1/TbUba2) and E2 (TbUbc9) enzymes of SUMOylation pathway in T. brucei by sequence analysis and GST pull-down assay. Furthermore, we successfully reconstructed the SUMOylation system in vitro with recombinant enzymes. Using this system, the active site of TbUba2 and TbUbc9 was revealed to be located at Cys343 and Cys132, respectively, and a centrin homologue (TbCentrin3) was identified to be a target of SUMOylation in T. brucei. Altogether, our results demonstrate that TbAos1/TbUba2 and TbUbc9 are the bona fide E1 and E2 enzymes of the SUMOylation system in T. brucei.
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