Research Article

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

Published: August 06, 2012
Genet. Mol. Res. 11 (3) : 2122-2129 DOI: https://doi.org/10.4238/2012.August.6.15
Cite this Article:
R.A. Campos, M.L. da Silva, G.V. da Costa, P.M. Bisch, J.M. Peralta, R. Silva, E. Rondinelli, T.P. Ürményi (2012). Gene expression and molecular modeling of the HSP104 chaperone of Trypanosoma cruzi. Genet. Mol. Res. 11(3): 2122-2129. https://doi.org/10.4238/2012.August.6.15
2,199 views

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.

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.