Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba.
10.3347/kjp.2016.54.2.133
- Author:
Eun Kyung MOON
1
;
Yeonchul HONG
;
Dong Il CHUNG
;
Youn Kyoung GOO
;
Hyun Hee KONG
Author Information
1. Department of Medical Zoology, Kyung Hee University School of Medicine, Seoul 02447, Korea.
- Publication Type:Original Article
- Keywords:
Acanthamoeba;
encystation;
cellulose synthase;
endocyst
- MeSH:
Acanthamoeba castellanii;
Acanthamoeba*;
Epigenesis, Genetic;
Epigenomics;
Gene Expression Regulation;
Methyltransferases;
Parasites;
Protein-Arginine N-Methyltransferases*;
RNA, Small Interfering;
Trophozoites
- From:The Korean Journal of Parasitology
2016;54(2):133-138
- CountryRepublic of Korea
- Language:English
-
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.
