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

doi:10.1016/j.molbiopara.2004.10.003

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 journal › Article › peer-review

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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 language	English (US)
Pages (from-to)	91-97
Number of pages	7
Journal	Molecular and Biochemical Parasitology
Volume	139
Issue number	1
DOIs	https://doi.org/10.1016/j.molbiopara.2004.10.003
State	Published - Jan 2005
Externally published	Yes

Bibliographical note

Funding Information:
This study was supported by grants from the Israel Science Foundation, Center for the study of Emerging diseases and Israeli Ministry of Health to S. Ankri and grants from DBT and ICMR, Govt of India to A. Lohia. We thank A. Meijer and P.R.F. Ouwerkerk for the yeast one-hybrid vectors and strains.

Keywords

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

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10.1016/j.molbiopara.2004.10.003

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Entamoeba histolytica DNA methyltransferase (Ehmeth) is a nuclear matrix protein that binds EhMRS2, a DNA that includes a scaffold/matrix attachment region (S/MAR). / Banerjee, Sulagna; Fisher, Ohad; Lohia, Anuradha et al.
In: Molecular and Biochemical Parasitology, Vol. 139, No. 1, 01.2005, p. 91-97.

Research output: Contribution to journal › Article › peer-review

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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.",

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

Abstract

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