Identification and Characterization of HSP90 Gene Family Reveals Involvement of HSP90, GRP94 and Not TRAP1 in Heat Stress Response in Chlamys farreri

Abstract

Heat shock proteins 90 (HSP90s) are a class of ubiquitous, highly conserved, and multi-functional molecular chaperones present in all living organisms. They assist protein folding processes to form functional proteins. In the present study, three HSP90 genes, CfHSP90, CfGRP94 and CfTRAP1, were successfully identified in the genome of Chlamys farreri. The length of CfHSP90, CfGRP94 and CfTRAP1 were 7211 bp, 26457 bp, and 28699 bp, each containing an open reading frame (ORF) of 2181 bp, 2397 bp, and 2181bp, and encoding proteins of 726, 798, and 726 amino acids, respectively. A transcriptomic database demonstrated that CfHSP90 and CfGRP94 were the primary functional executors with high expression during larval development and in adult tissues, while CfTRAP1 expression was low. Furthermore, all of the three CfHSP90s showed higher expression in gonads and ganglia as compared with other tissues, which indicated their probable involvement in gametogenesis and nerve signal transmission in C. farreri. In addition, under heat stress, the expressions of CfHSP90 and CfGRP94 were significantly up-regulated in the mantle, gill, and blood, but not in the heart. Nevertheless, the expression of CfTRAP1 did not change significantly in the four tested tissues. Taken together, in coping with heat stress, CfHSP90 and CfGRP94 could help correct protein folding or salvage damaged proteins for cell homeostasis in C. farreri. Collectively, a comprehensive analysis of CfHSP90s in C. farreri was conducted. The study indicates the functional diversity of CfHSP90s in growth, development, and environmental response, and our findings may have implications for the subsequent in-depth exploration of HSP90s in invertebrates.

Genomic Survey of Heat Shock Proteins in Liriodendron chinense Provides Insight into Evolution, Characterization, and Functional Diversities

“…Particularly, the HSP90 class encompasses the heat shock proteins that are highly conserved and widely distributed in the cytoplasm, chloroplast, mitochondria, and endoplasmic reticulum, accounting for 1–2% of total cellular proteins. It exists mainly as a homodimer, containing a 12 kDa N-terminal domain of the ATP-binding site, the 35 kDa intermediate domain, and a 25 kDa C-terminal substrate-binding domain [ 13 , 14 ]. The HSP70 class is one of the most widely distributed and studied heat shock proteins, comprising of a 44 kDa N-terminal ATP binding domain (NBD), 15 kDa substrate binding domain, and about 10 kDa C-terminal domain [ 15 , 16 ].…”

Tissue-Specific and Time-Dependent Expressions of PC4s in Bay Scallop (Argopecten irradians irradians) Reveal Function Allocation in Thermal Response

“…As expected, the cardiac performance investigations in scallops reported that, with the increase of ambient seawater temperature, the heart rate and heart amplitude of scallops increased gradually before Arrhenius break temperature, and the results of which generally supported our hypothesis [ 53 ], whereas obvious down-regulations occurred in Arg0193880.1 at nearly all time points during high-temperature stimulation, indicating that transcriptional function inhibition was blocked by some protein synthesis [ 101 ]. A similar phenomenon of gene family member tissue-specific and time-dependent expression was also observed in Mitogen-activated protein kinase ( MAPK ) [ 106 ] and HSP90 genes in Zhikong scallops [ 107 ], providing implications for flexible regulation of bivalve gene families in response to heat stress. Collectively, our results showed a significant and flexible regulation profile (up-/down-regulated, tissue-specific, time-dependent) of these AiPC4s and possibly suggested a strong adaptation model under temperature stress.…”

Regulation of GeCu/Zn-SOD, GeMn-SOD, GeHsp90, and GeMT in Gymnocypris eckloni in Response to Copper and Lead Ion Challenges

“…Heat shock proteins (HSPs) have been widely found to play an important role in protecting organisms from heat stress through combining heat shock factor 1 (HSF1) with heat shock elements (HSEs) to upregulate HSP90 [44,45]. Meanwhile, the expression of HSP90 is regulated by salinity, reduced oxygen level, food scarcity, and heavy metals [44][45][46]. Interestingly, according to earlier research, HSP90 expression showed a time and concentration dependence under stress conditions.…”