Abstract
As one crucial member of heat shock proteins (HSPs) family, HSP70s play many important roles in a large amount of physiological processes including immune response. However, information regarding HSP70 in ark shell Scapharca broughtonii is still rather limited. Here the full-length cDNA of HSP70 gene (named SbHSP70) of S. broughtonii was identified by using reverse transcription PCR (RT-PCR) and rapid amplification ends (RACE) methods. The SbHSP70 cDNA was 2423 bp in length containing a 5′ untranslated region (UTR) of 131 bp, 3′-UTR of 330 bp, and an open reading frame (ORF) of 1962 bp which encodes a peptide of 653 amino acids.The multiple alignment and phylogeny analysis showed that the SbHSP70 shared high homology sequence with other mollusk species, and clustered together with gastropods to form a sister group. The mRNA expression profiles of SbHSP70 in tissues of foot, gill, mantle, adductor muscle, haemocytes and hepatopancreas analyzed by quantitative real-time PCR (qRT-PCR) suggested the mRNA transcripts of SbHSP70 distributed in all the examined tissues, and the highest expression level was observed in foot, and a significant difference could be detected between gill and adductor muscle (p<0.05), no significant difference among the gill, mantle and hemocytes (p > 0.05). Its dynamic change during the early stage of larvae showed that it could be transferred from parent and may be involved in some key developmental process. What’s more, Vibrio anguillarum challenge resulted in regular change of expression of SbHSP70 mRNA, indicating SbHSP70 actively participated in the immune response process.
Highlights
Heat shock proteins (HSPs), with a highly conserved polypeptide of structure and widely existing in prokaryotic and eukaryotic cells, acted as molecular chaperons to maintain the proper folding or refolding protein, which playing lots of important roles in normal condition and in the continuation of life under stress
A nucleotide sequence with final length of 2423bp representing for the complete cDNA sequence of SbHSP70 gene was obtained by assembling all the amplified partial fragments amplified by reverse transcription PCR (RT-PCR) and RACRE
The full-length sequence of SbHSP70 cDNA contained a 5′-untranslated region (UTR) of 131 bp, a 3′-UTR of 330 bp with a canonical polyadenylation signal sequences AATAAA and a poly (A) tail, and an open reading frame (ORF) of 1962 bp encoding a polypeptide of 653 amino acids with the predicted molecular mass of 71.33 kDa and theoretical isoelectric point of 5.36
Summary
Heat shock proteins (HSPs), with a highly conserved polypeptide of structure and widely existing in prokaryotic and eukaryotic cells, acted as molecular chaperons to maintain the proper folding or refolding protein, which playing lots of important roles in normal condition and in the continuation of life under stress. When facing the stress condition, organisms would massively produce HSPs to prevent from the accumulation of denatured proteins, transport immature proteins to target organelles and improve the stress tolerance to protect organisms from damaging (Mayer & Bukau, 2005; Tanaka et al, 2007) Because of their important biological functions, HSPs have been becoming more and more popular research objects in many fields. To our knowledge, information about HSP70 in the ark shell Scapharca broughtonii is extremely limited
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