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 | |
| State | Published - Jan 1 2005 |
| Externally published | Yes |
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Keywords
- Cytosine-5 DNA methyltransferase
- DNA methylation
- Entamoeba
- Scaffold/matrix attachment region
ASJC Scopus subject areas
- Parasitology
- Molecular Biology
Cite this
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; Ankri, Serge.
In: Molecular and Biochemical Parasitology, Vol. 139, No. 1, 01.01.2005, p. 91-97.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Entamoeba histolytica DNA methyltransferase (Ehmeth) is a nuclear matrix protein that binds EhMRS2, a DNA that includes a scaffold/matrix attachment region (S/MAR)
AU - Banerjee, Sulagna
AU - Fisher, Ohad
AU - Lohia, Anuradha
AU - Ankri, Serge
PY - 2005/1/1
Y1 - 2005/1/1
N2 - 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.
AB - 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.
KW - Cytosine-5 DNA methyltransferase
KW - DNA methylation
KW - Entamoeba
KW - Scaffold/matrix attachment region
UR - http://www.scopus.com/inward/record.url?scp=11144321640&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11144321640&partnerID=8YFLogxK
U2 - 10.1016/j.molbiopara.2004.10.003
DO - 10.1016/j.molbiopara.2004.10.003
M3 - Article
C2 - 15610823
AN - SCOPUS:11144321640
VL - 139
SP - 91
EP - 97
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
SN - 0166-6851
IS - 1
ER -