Abstract
The HSTF is a master molecule involved in the transcriptional control of several genes during different types of stress. This transcription factor is a very conserved protein identified in different organisms from bacterial to human. Entamoeba histolytica is the protozoan responsible for the human amoebiasis. This parasite is exposed to different kind of stress as changes in the pH, temperature, drugs, all that situations in where the parasite needs survive. Here we identified and isolated a novel gene family of HSTFs in the protozoan parasite E. histolytica. Three members that we called Ehhstf1, Ehhstf2 and Ehhstf3 compose this family. Amino acid alignments and domain architecture analysis revealed that the EhHSTFs presents a conserved DNA-binding domain composed of approximately 25 residues. Interestingly this domain is shorter than the domain of the human, mouse and yeast HSTFs. Heterologous antibodies recognized four peptides of 73, 66, 47 and 23 kDa in total extracts from trophozoites growth under normal conditions. The 73, 47 and 23 kDa peptides increased their intensity when the cells were growth at 42°C by 2 h. All results together demonstrate that the amoeba present HSTFs, which may be, controlled the gene expression of this parasite under different stress situations.
Highlights
All the organisms respond to chemical, environmental or physiological stress through a transient arrest of the cell cycle that is accompanied by widespread changes in macromolecular synthesis, degradation, trafficking, overall cellular metabolism and signal transduction pathways to cope with stressful conditions until more favourable conditions are encountered [1].The termic stress in any organism may provoke different changes, since expression and/or repression of different molecules, the destabilization of protein conformation, leading to protein unfolding and aggregation, until severe or prolonged stresses can lead irreversible protein damage provoking the cell die [2]
The heat shock transcription factors (HSTF) is a central regulator for the expression of different proteins during the heat shock response and to exposition to a variety of chemical and physiological stresses
In E. histolytica have been described the presence of heat shock proteins (Hsps) [31] and recently have been identified a putative heat shock element (HSE) in the promoters of some genes of this parasite ‘unpublished data’ suggesting that the amoeba presents a HSTF in their genome
Summary
All the organisms respond to chemical, environmental or physiological stress through a transient arrest of the cell cycle that is accompanied by widespread changes in macromolecular synthesis, degradation, trafficking, overall cellular metabolism and signal transduction pathways to cope with stressful conditions until more favourable conditions are encountered [1].The termic stress in any organism may provoke different changes, since expression and/or repression of different molecules, the destabilization of protein conformation, leading to protein unfolding and aggregation, until severe or prolonged stresses can lead irreversible protein damage provoking the cell die [2]. A very knows group of proteins have been completely related to this event: the heat shock proteins (Hsps) These proteins are chaperones involved in the folding, trafficking, maturation and degradation of proteins [3]. Other important proteins involved in the heat shock response are the heat shock transcription factors (HSTF), which rapidly activate and bind to the heat shock element (HSE) present in the Hsp promoters. This factor induces the Hsps gene expression whose products ensure the survival of the cell during stressful conditions by providing defense against general protein damage [4]
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