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
N1 - 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.
PY - 2005/1
Y1 - 2005/1
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 -