Entamoeba histolytica DNA methyltransferase (Ehmeth) is a nuclear matrix protein that binds EhMRS2, a DNA that includes a scaffold/matrix attachment region (S/MAR)

Sulagna Banerjee, Ohad Fisher, Anuradha Lohia, Serge Ankri

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

The protozoan parasite Entamoeba histolytica express a cytosine-5 DNA methyltransferase (Ehmeth) that belongs to the DNMT2 protein family. The biological function of members of this DNMT2 family is unknown. In the present study, we have demonstrated that Ehmeth is a nuclear matrix protein. Indeed, we showed by south-western analysis and yeast one-hybrid system that Ehmeth binds to EhMRS2, a DNA element which contains the eukaryotic consensus scaffold/matrix attachment regions (S/MAR) bipartite recognition sequences. S/MARs have been implicated in a variety of important functions, such as genome organization and gene expression. The methylation status of cytosine located within EhMRS2 was analyzed by bisulfite genomic sequencing. We observed the presence of methylated cytosine within the 3′-end of EhMRS2. These data provide the first evidence that a member of the DNMT2 family interacts with a S/MAR containing DNA element.

Original languageEnglish (US)
Pages (from-to)91-97
Number of pages7
JournalMolecular and Biochemical Parasitology
Volume139
Issue number1
DOIs
StatePublished - Jan 1 2005
Externally publishedYes

Keywords

  • Cytosine-5 DNA methyltransferase
  • DNA methylation
  • Entamoeba
  • Scaffold/matrix attachment region

ASJC Scopus subject areas

  • Parasitology
  • Molecular Biology

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