ArticleParasites & vectors2015
Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone.
Article in Parasites & vectors, 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, 14 citations in OpenAlex.
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- A type II protein arginine methyltransferase regulates merozoite invasion in Plasmodium falciparum.Communications biology · 2023Article
- Advances in Protozoan Epigenetic Targets and Their Inhibitors for the Development of New Potential Drugs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Are Metabolites From the Gut Microbiota Capable of Regulating Epigenetic Mechanisms in the Human ParasiteFrontiers in cell and developmental biology · 2022Review
- Telomeric Repeat-Binding Factor Homologs inFrontiers in cellular and infection microbiology · 2018Article
- Identification and Characterization of Protein Arginine Methyltransferase 1 inThe Korean journal of parasitology · 2017Article
- The Tudor Staphylococcal Nuclease Protein ofFrontiers in cellular and infection microbiology · 2017Article
- Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba.The Korean journal of parasitology · 2016Article
- Identification of repressive and active epigenetic marks and nuclear bodies in Entamoeba histolytica.Parasites & vectors · 2016Article
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4 authors at 2 institutions in 1 country.
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Abstract
backgroundIn eukaryotes, histone arginine methylation associates with both active and repressed chromatin states depending on the residues involved and the status of methylation. Even when the amino-terminus of Entamoeba histolytica histones diverge from metazoan sequences, these regions contain arginine residues that are potential targets for methylation. However, histone arginine methylation as well as the activity of arginine methyltransferases (PRMTs) has not been studied in this parasite. The aim of this work was to examine the dimethylation of arginine 3 of H4 histone (H4R3me2) and to identify the parasite PRMT that could be responsible for this modification (EhPRMT1).
methodsTo examine the presence of H4R3me2 in E histolytica, we performed Western blot and immunofluorescence assays on trophozoites using an antibody against this epigenetic mark. To recognize the PRMT1 enzyme of this parasite that possibly perform that modification, we first performed a phylogenetic analysis of E. histolytica and human PRMTs. RT-PCR assays were carried out to analyze the expression of the putative PRMT1 genes. One of these genes was cloned and expressed in Escherichia coli. The recombinant protein was tested by its recognition by an antibody against human PRMT1 and in its ability to form homodimers and to methylate commercial histones.
resultsThe arginine 3 of human H4, which is subjected to post translational methylation, was aligned with the arginine 8 of E. histolytica H4, suggesting that this residue could be methylated. The recognition of an 18 kDa nuclear protein of E. histolytica by an antibody against H4R3me2 confirmed this assumption. We found that this parasite expresses three phylogenetic and structural proteins related to PRMT1. Antibodies against the human PRMT1 detected E. histolytica proteins in cytoplasm and nuclei and recognized a recombinant PRMT1 of this parasite. The recombinant protein was able to form homodimers and homotetramers and displayed methyltransferase activity on arginine 3 of chicken H4.
conclusionAll these results suggest that E. histolytica contains as a minimum one structural and functional protein ortholog to PRMT1, enzyme that potentially dimethylates H4R8. This modification may play an important role in the gene expression regulation of this microorganism.
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