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Epigenetic and classical activation of Entamoeba histolytica heat shock protein 100 (EHsp100) expression
Author(s) -
Bernes Sabina,
Siman-Tov Rama,
Ankri Serge
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.101
Subject(s) - microbiology and biotechnology , dna methylation , biology , dna methyltransferase , heat shock protein , hspa14 , hspa12a , entamoeba histolytica , histone , demethylation , hsp70 , methylation , methyltransferase , dna , biochemistry , gene expression , genetics , gene
The protozoan parasite Entamoeba histolytica expresses 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, the 5′ region of E. histolytica heat shock protein 100 (5′ EHsp100 ) was isolated by affinity chromatography with 5‐methylcytosine antibodies as ligand. The methylation status of 5′ EHsp100 was confirmed by sodium bisulfite sequencing. We showed that the expression of EHsp100 was induced by heat shock, 5‐azacytidine (5‐AzaC), an inhibitor of DNA methyltransferase and Trichostatin A (TSA), an inhibitor of histone deacetylase. The effect of TSA on EHsp100 expression was rapidly reversed by removing the drug from the culture. In contrast, EHsp100 expression was still detectable one month after removing 5‐AzaC from the media. Whereas 5‐AzaC and TSA caused demethylation in the promoter region of EHsp100 , no demethylation was observed following heat shock. Remarkably, DNA that includes three putative heat shock elements identified in the promoter region of EHsp100 bound to a protein of 37 kDa present in the nuclear fraction of heat‐shocked trophozoites but absent in the nuclear fraction of 5‐AzaC and TSA treated trophozoites. Our data suggest that EHsp100 expression can be regulated by both a classical and an epigenetic mechanism.