Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone.

ABSTRACT:

Background

In eukaryotes, histone arginine methylation associates with both active and repressed chromatin states depending on the residues involved and the status of methylation. Even when the amino-terminus of Entamoeba histolytica histones diverge from metazoan sequences, these regions contain arginine residues that are potential targets for methylation. However, histone arginine methylation as well as the activity of arginine methyltransferases (PRMTs) has not been studied in this parasite. The aim of this work was to examine the dimethylation of arginine 3 of H4 histone (H4R3me2) and to identify the parasite PRMT that could be responsible for this modification (EhPRMT1).

Methods

To examine the presence of H4R3me2 in E histolytica, we performed Western blot and immunoflu

SUBMITTER: Borbolla-Vazquez J 

PROVIDER: S-EPMC4393863 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature