In silico Analysis of Post Translational Modifications on the EhHSTF7 factor in Entamoeba histolytica

The heat shock transcription factors (HSTFs) are gene regulatory proteins involved in heat stress response. Post-translational modifications have been essential in the functioning of HSTFs in eukaryotic organisms. Phosphorylation, methylation, acetylation, sumoylation, and ubiquitination are part of the regulatory processes of HSTF factors. In the protozoan parasite Entamoeba histolytica, the causal agent of amoebiasis, little is known about post-translational modifications and the molecules involved in heat stress. Particularly, this parasite presents an HSTF that is overexpressed in trophozoites growth on heat shock stress or with emetine, an antiamebian drug. In this article, we identified and characterized by potential bioinformatics tools, the posttranslational modifications, such as phosphorylation, sumoylation, and acetylation sites in the HSTF factor of Entamoeba histolytica. The results showed the presence of fourteen potential phosphorylation sites, five sumoylation sites, and two acetylation sites in the HSTF. These results suggest that the functions of the HSTF maybe being regulated by these post-translational modifications when the amoeba is exposed or not in stressful situations.