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

• Published in: Genetics and molecular research 2012-01, Vol.11 (3), p.2122-2129
• Main Authors: Campos, R A, da Silva, M L, da Costa, G V, Bisch, P M, Peralta, J M, Silva, R, Rondinelli, E, Urményi, T P
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Gene Expression Regulation; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Humans; Models, Molecular; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Sequence Data; Protein Structure, Secondary; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; Protozoan Proteins - metabolism; Sequence Alignment; Trypanosoma cruzi - genetics
• ISSN: 1676-5680; 1676-5680
• DOI: 10.4238/2012.August.6.15

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.