ArticleThe Korean journal of parasitology2016
Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba.
Article in The Korean journal of parasitology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 12 citations in OpenAlex.
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- Encystment and Excystment Processes inPathogens (Basel, Switzerland) · 2025Review
- Biological characteristics and pathogenicity ofFrontiers in microbiology · 2023Review
- Stimulation ofFrontiers in cell and developmental biology · 2022Article
- Identification and Characterization of Protein Arginine Methyltransferase 1 inThe Korean journal of parasitology · 2017Article
- DNA Methylation of Gene Expression inThe Korean journal of parasitology · 2017Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
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Abstract
Encystation is an essential process for Acanthamoeba survival under nutrient-limiting conditions and exposure to drugs. The expression of several genes has been observed to increase or decrease during encystation. Epigenetic processes involved in regulation of gene expression have been shown to play a role in several pathogenic parasites. In the present study, we identified the protein arginine methyltransferase 5 (PRMT5), a known epigenetic regulator, in Acanthamoeba castellanii. PRMT5 of A. castellanii (AcPRMT5) contained domains found in S-adenosylmethionine-dependent methyltransferases and in PRMT5 arginine-N-methyltransferase. Expression levels of AcPRMT5 were increased during encystation of A. castellanii. The EGFP-PRMT5 fusion protein was mainly localized in the nucleus of trophozoites. A. castellanii transfected with siRNA designed against AcPRMT5 failed to form mature cysts. The findings of this study lead to a better understanding of epigenetic mechanisms behind the regulation of encystation in cyst-forming pathogenic protozoa.
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