Gene expression and molecular modeling of the HSP104 chaperone of Trypanosoma cruzi

Abstract

ABSTRACT. Heat shock protein (HSP) 104 is a highly conserved molecular chaperone that catalyzes protein unfolding, disaggregation and degradation under stress conditions. We characterized HSP104 gene structure and expression in Trypanosoma cruzi, a protozoan parasite that causes Chagas' disease. The T. cruzi HSP104 is an 869 amino-acid protein encoded by a single-copy gene that has the highest sequence similarity (76%) with that of T. brucei and the lowest (23%) with that of the human protein. HSP104 transcripts were detected at room temperature, and levels increased after incubation at 37° or 40°C. The HSP104 protein was found at low levels in non-heat-shocked cells, and accumulated continuously up to 24 h at elevated temperatures. We developed a predicted structural model of hexameric T. cruzi HSP104, which showed some conserved features.

Dealing with environmental challenges: Mechanisms of adaptation in Trypanosoma cruzi

“…HSP104 mRNA and protein levels [16] as well as transcript abundance for the small chaperonins HSP10 and HSP16, are also increased by thermal stress [17, 18]. Two-dimensional gel electrophoresis and proteomic analysis of 24 differential spots obtained from epimastigotes incubated at 42°C showed an increase in a relatively small number of stress-related proteins, including HSP70 and HSP40, but no large changes in protein expression were observed under this conditions [7].…”

The Heat Shock Proteins of Trypanosoma cruzi

“…With the gene sequence available as a starting point, a member of the HSP104 family has been recently characterized in T . cruzi (Campos et al 2012 ). A single copy gene is present in the genome, and the primary sequence of 869 amino acid residues contains the characteristic N-terminal domain and the Walker A-and B-type NBD domains.…”