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Molecular cloning, sequence characterization and expression analysis of HSP90β from ayu (Plecoglossus altivelis)

  

  1. School of Marine Sciences, Ningbo University, Ningbo 315211, China
  • Online:2018-02-18 Published:2018-02-18

Abstract: Heat shock proteins (HSPs) are one type of molecular chaperones, and have a wide range of biological activities. The full-length cDNA sequence of ayu HSP90β gene (PaHSP90β) was obtained from the liver tissue cDNA library of ayu (Plecoglossus altivelis). The cDNA sequence of PaHSP90β was 2726 nucleotides, containing a 2175 bp open reading frame that encoded a protein of 724 amino acids with a deduced molecular weight (MW) of 83.30 ku and a isoelectric point (pI) of 4.83. Multiple sequence alignment of complete amino acid sequences showed that PaHSP90β contained five conserved HSP90 family signatures, and a typical HATPase (histidine kinase-like ATPases) domain, which was located at positions 34 to 188. PaHSP90β shared the highest amino acid sequence identity (95.8%) with that of European whitefish (Coregonus lavaretus). Quantitative real-time PCR (qPCR) analysis showed that PaHSP90β mRNA had the highest expressional level in ayu liver, followed by the spleen. Upon Cd exposure, PaHSP90β transcripts were significantly up-regulated in liver, spleen, kidney, intestine and gill of ayu. After the salinity stress, PaHSP90β mRNA expression was significantly up-regulated in all the tissues except the intestine. In summary, PaHSP90β had a close relationship with heavy metal and salinity stress, and may be involved in physiological processes against environmental stresses in fish.
   

Key words: Plecoglossus altivelis, HSP90β, cadmium stress, salinity stress, quantitative real-time PCR