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Updated: Sep 29, 2025
Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Protein arginine methyltransferases in protozoan parasites
1Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, Ciudad de México, México.
Abstract:
Arginine methylation is a post-translational modification involved in gene transcription, signalling pathways, DNA repair, RNA metabolism and splicing, among others, mechanisms that in protozoa parasites may be involved in pathogenicity-related events. This modification is performed by protein arginine methyltransferases (PRMTs), which according to their products are divided into three main types: type I yields monomethylarginine (MMA) and asymmetric dimethylarginine; type II produces MMA and symmetric dimethylarginine; whereas type III catalyses MMA only. Nine PRMTs (PRMT1 to PRMT9) have been characterized in humans, whereas in protozoa parasites, except for Giardia intestinalis, three to eight PRMTs have been identified, where in each group there are at least two enzymes belonging to type I, the majority with higher similarity to human PRMT1, and one of type II, related to human PRMT5. However, the information on the role of most of these enzymes in the parasites biology is limited so far. Here, current knowledge of PRMTs in protozoan parasites is reviewed; these enzymes participate in the cell growth, stress response, stage transitions and virulence of these microorganisms. Thus, PRMTs are attractive targets for developing new therapeutic strategies against these pathogens.
Insights
Protein arginine methyltransferases (PRMTs) are crucial in protozoan parasites, influencing pathogenicity. Understanding these enzymes offers potential for new anti-parasitic therapies.
Area of Science:
- Biochemistry
- Molecular Biology
- Parasitology
Background:
- Arginine methylation is a key post-translational modification regulating vital cellular processes.
- Protein arginine methyltransferases (PRMTs) catalyze arginine methylation, classified into types I, II, and III based on their products.
- While nine PRMTs are known in humans, protozoan parasites possess three to eight PRMTs, often with homologs to human type I and type II enzymes.
Purpose of the Study:
- To review the current knowledge of PRMTs in protozoan parasites.
- To highlight the roles of PRMTs in parasite biology and pathogenicity.
- To identify PRMTs as potential therapeutic targets.
Main Methods:
- Literature review of existing studies on PRMTs in protozoan parasites.
- Comparative analysis of PRMTs across different protozoan species and with human PRMTs.
- Synthesis of information on the functional roles of PRMTs in parasite life cycles.
Main Results:
- Protozoan parasites harbor diverse PRMTs, with type I and type II enzymes being common.
- PRMTs are implicated in essential parasite processes including cell growth, stress response, stage transitions, and virulence.
- Despite limited information on most parasite PRMTs, their involvement in pathogenicity is evident.
Conclusions:
- PRMTs play significant roles in the biology and pathogenicity of protozoan parasites.
- The identified PRMTs represent promising targets for the development of novel therapeutic strategies against parasitic infections.
- Further research into the specific functions of PRMTs in various parasites is warranted.
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