Gene expression  and molecular modeling of the HSP104 chaperone of Trypanosoma cruzi.
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.
Programa de Biologia Molecular e Estrutural, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
R A
RA
Campos
M L
ML
da Silva
G V
GV
da Costa
P M
PM
Bisch
J M
JM
Peralta
R
R
Silva
E
E
Rondinelli
T P
TP
Urményi
D000595:Amino Acid Sequence; D005786:Gene Expression Regulation; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D014349:Trypanosoma cruzi / Q000235:genetics*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D015800:Protozoan Proteins