Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba.
Korean J Parasitol
; 54(2): 133-8, 2016 Apr.
Article
in En
| MEDLINE
| ID: mdl-27180570
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein-Arginine N-Methyltransferases
/
Protozoan Proteins
/
Epigenesis, Genetic
/
Acanthamoeba castellanii
/
Parasite Encystment
Type of study:
Diagnostic_studies
/
Prognostic_studies
Language:
En
Journal:
Korean J Parasitol
Journal subject:
PARASITOLOGIA
Year:
2016
Document type:
Article