Heat shock protein 90 ( HSP90 ) represents a suite of highly conserved and multi-functional molecular chaperone proteins that play an important role in cellular stress responses. In order to better understand the expression of HSP90 in mollusks, a full-length complementary DNA (cDNA) of HSP90 ( HcHSP90 ) was identified in Hyriopsis cumingii . HcHSP90 cDNA was 2659bp in length, consisting of 3′ and 5′-untranslated regions and an open reading frame of 2187bp, that encoded a 728amino acid protein. Homology analyses showed that the HcHSP90 protein was highly conserved and had five well-conserved family signatures of HSP90 proteins. HcHSP90 mRNA expressed in various tissues of Hyriopsis cumingii . The expression... More
Heat shock protein 90 ( HSP90 ) represents a suite of highly conserved and multi-functional molecular chaperone proteins that play an important role in cellular stress responses. In order to better understand the expression of HSP90 in mollusks, a full-length complementary DNA (cDNA) of HSP90 ( HcHSP90 ) was identified in Hyriopsis cumingii . HcHSP90 cDNA was 2659bp in length, consisting of 3′ and 5′-untranslated regions and an open reading frame of 2187bp, that encoded a 728amino acid protein. Homology analyses showed that the HcHSP90 protein was highly conserved and had five well-conserved family signatures of HSP90 proteins. HcHSP90 mRNA expressed in various tissues of Hyriopsis cumingii . The expression level of HcHSP90 was highest in the digestive gland. In all tissues, with the exception of the digestive gland where it was down-regulated, HcHSP90 mRNA expression was significantly induced by temperature treatments (0, 5, 25, and 35°C) relative to the control (15°C). Exposure of H.cumingii to different concentrations of cadmium (50, 100, and 200μg/L), up-regulated HcHSP90 mRNA in the haemolymph and gill but without an obvious dose-dependent response. When H.cumingii were infected with Aeromonas hydrophila , HcHSP90 mRNA expression in the haemolymph was up-regulated and peaked 36h post-infection, while in the gills it was significantly up-regulated 3h post-infection in the gills, then remained constant until returning to pre-challenge expression levels at 36h post-infection. The results show that HcHSP90 expression can be significantly regulated by changes in temperature, cadmium exposure and bacterial infection. We deduced that HSP90 may play an important role in helping H.cumingii to cope with environmental stress.
