ArticleThe Journal of biological chemistry2016
Characterization and Structural Insights into Selective E1-E2 Interactions in the Human and Plasmodium falciparum SUMO Conjugation Systems.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Implications of critical node-dependent unidirectional cross-talk of Plasmodium SUMO pathway proteins.Biophysical journal · 2022Article
- (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants.Life (Basel, Switzerland) · 2022Review
- Mild Hypothermia Promotes Ischemic Tolerance and Survival of Neural Stem Cell Grafts by Enhancing Global SUMOylation.Oxidative medicine and cellular longevity · 2022Article
- Histone Modification Landscapes as a Roadmap for Malaria Parasite Development.Frontiers in cell and developmental biology · 2022Review
- Targeting SUMOylation inFrontiers in cellular and infection microbiology · 2021Review
- SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance.Frontiers in cell and developmental biology · 2021Review
- Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.Biomolecules · 2020Review
- Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction.Scientific reports · 2017Article
- Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein modification by small ubiquitin-related modifiers (SUMOs) is essential and conserved in the malaria parasite, Plasmodium falciparum. We have previously shown that interactions between the SUMO E1-activating and E2-conjugating enzyme in P. falciparum are distinct compared with human, suggesting a potential target for development of parasite-specific inhibitors of SUMOylation. The parasite asexual trophozoite stage is susceptible to iron-induced oxidative stress and is subsequently a target for many of the current anti-malarial drugs. Here, we provide evidence that SUMOylation plays a role in the parasite response to oxidative stress during red blood cell stages, indicative of a protective role seen in other organisms. Using x-ray crystallography, we solved the structure of the human SUMO E1 ubiquitin fold domain in complex with the E2, Ubc9. The interface defined in this structure guided in silico modeling, mutagenesis, and in vitro biochemical studies of the P. falciparum SUMO E1 and E2 enzymes, resulting in the identification of surface residues that explain species-specific interactions. Our findings suggest that parasite-specific inhibitors of SUMOylation could be developed and used in combination therapies with drugs that induce oxidative stress.
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