Molecular characterization of heat-shock protein 90 gene and its expression in Gobiocypris rarus juveniles exposed to pentachlorophenol.

Heat-shock protein 90 (HSP90) is an abundant and highly conserved molecular chaperone, and it fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity, and proper regulation of a subset of cytosolic proteins. In this study, the full-length 2693-bp cDNA of HSP90 was cloned by rapid amplification of cDNA ends (RACE) technique from the liver of rare minnow (Gobiocypris rarus) for the first time, designated as GrHSP90. The complete coding sequence of GrHSP90 is 2181 bp in length, which encodes a polypeptide of 726 amino acids with a predicted molecular mass of 83.4 kDa and a theoretical isoelectric point of 4.90. Phylogenetic tree analysis indicated that deduced protein GrHSP90 had extensive sequence similarities to other fish HSP90s. Tissue distribution showed that GrHSP90 was constitutively expressed in a wide range of tissues including gill, blood, brain, fin, gonad, heart, intestine, kidney, liver, muscle, spleen, skin, and swim bladder. The highest expression was found in the gonad. Furthermore, significant increase in GrHSP90 mRNA in the liver was observed after exposure to pentachlorophenol ≥8 µg/L (p < 0.05). Our results suggest that GrHSP90 is indeed an ortholog of the HSP90 family and may be act as a biomarker to assess the effect of environmental contaminant.