Identification and Characterization of Protein Arginine Methyltransferase 1 in Acanthamoeba castellanii.
10.3347/kjp.2017.55.2.109
- Author:
Eun Kyung MOON
1
;
Hyun Hee KONG
;
Yeonchul HONG
;
Hae Ahm LEE
;
Fu Shi QUAN
Author Information
1. Department of Medical Zoology, Kyung Hee University School of Medicine, Seoul 02447, Korea. fquan01@gmail.com
- Publication Type:Original Article
- Keywords:
Acanthamoeba castellanii;
characterization;
encystation;
protein arginine methyltransferase 1
- MeSH:
Acanthamoeba castellanii*;
Acanthamoeba*;
Amino Acids;
Clone Cells;
Cytoplasm;
DNA, Complementary;
Epigenomics;
Eukaryotic Cells;
Protein-Arginine N-Methyltransferases*;
RNA, Small Interfering
- From:The Korean Journal of Parasitology
2017;55(2):109-114
- CountryRepublic of Korea
- Language:English
-
Abstract:
Protein arginine methyltransferase (PRMT) is an important epigenetic regulator in eukaryotic cells. During encystation, an essential process for Acanthamoeba survival, the expression of a lot of genes involved in the encystation process has to be regulated in order to be induced or inhibited. However, the regulation mechanism of these genes is yet unknown. In this study, the full-length 1,059 bp cDNA sequence of Acanthamoeba castellanii PRMT1 (AcPRMT1) was cloned for the first time. The AcPRMT1 protein comprised of 352 amino acids with a SAM-dependent methyltransferase PRMT-type domain. The expression level of AcPRMT1 was highly increased during encystation of A. castellanii. The EGFP-AcPRMT1 fusion protein was distributed over the cytoplasm, but it was mainly localized in the nucleus of Acanthamoeba. Knock down of AcPRMT1 by synthetic siRNA with a complementary sequence failed to form mature cysts. These findings suggested that AcPRMT1 plays a critical role in the regulation of encystation of A. castellanii. The target gene of AcPRMT1 regulation and the detailed mechanisms need to be investigated by further studies.
