Korean J Parasitol.  2016 Apr;54(2):133-138. 10.3347/kjp.2016.54.2.133.

Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba

Affiliations
  • 1Department of Medical Zoology, Kyung Hee University School of Medicine, Seoul 02447, Korea.
  • 2Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine, Daegu 41944, Korea.
  • 3Department of Parasitology, Dong-A University College of Medicine, Busan 49201, Korea. hhkong@dau.ac.kr

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.

Keyword

Acanthamoeba; encystation; cellulose synthase; endocyst

MeSH Terms

Acanthamoeba castellanii
Acanthamoeba*
Epigenesis, Genetic
Epigenomics
Gene Expression Regulation
Methyltransferases
Parasites
Protein-Arginine N-Methyltransferases*
RNA, Small Interfering
Trophozoites
Methyltransferases
Protein-Arginine N-Methyltransferases
RNA, Small Interfering
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