Journal
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 139, Issue 1, Pages 91-97Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2004.10.003
Keywords
Entamoeba; DNA methylation; cytosine-5 DNA methyltransferase; scaffold/matrix attachment region
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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/inatrix 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. (C) 2004 Elsevier B.V. All rights reserved.
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