Gene expression and molecular modeling of the HSP104 chaperone of Trypanosoma cruzi
| Autor: | Peralta Jm, Edson Rondinelli, R. Silva, Campos Ra, da Costa Gv, da Silva Ml, Bisch Pm, Turán P. Ürményi |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Trypanosoma cruzi Molecular Sequence Data Protozoan Proteins Biology Protein Structure Secondary HSPA4 Heat shock protein parasitic diseases HSPA2 Genetics Humans Amino Acid Sequence Molecular Biology Heat-Shock Proteins HSPA9 HSPA14 General Medicine biology.organism_classification Molecular biology Biochemistry Gene Expression Regulation Chaperone (protein) AKT1S1 biology.protein Sequence Alignment Molecular Chaperones |
| Zdroj: | Genetics and molecular research : GMR. 11(3) |
| ISSN: | 1676-5680 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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