Molecular cloning of the heat shock protein 20 gene from Paphia textile and its expression in response to heat shock

Jiakai Li; Xiangwei Wu; Jing Tan; Ruixiang Zhao; Lingwei Deng; Xiande Liu

doi:10.1007/s00343-015-4223-6

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Molecular cloning of the heat shock protein 20 gene from Paphia textile and its expression in response to heat shock

Updated：2023-05-16

- Molecular cloning of the heat shock protein 20 gene from Paphia textile and its expression in response to heat shock
- Journal of Oceanology and Limnology Vol. 33, Issue 4, Pages: 919-927(2015)
- Affiliations：
  
  1. Key Laboratory of Mariculture in the East China Sea Ministry of Agriculture of China
  2. Fisheries College Jimei University
  3. Animal Science and Technology College Yunnan Agricultural University
  4. Rice Molecular Breeding in Northern Chinese Academy of Sciences Joint Research Center
- Author bio：
- Funds：
- DOI：10.1007/s00343-015-4223-6
  CLC：
- Online First：26 April 2015，
  
  Published：2015
- Accepted：
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Li, J., Wu, X., Tan, J. et al. Molecular cloning of the heat shock protein 20 gene from Paphia textile and its expression in response to heat shock., Chin. J. Ocean. Limnol. 33, 919–927 (2015). https://doi.org/10.1007/s00343-015-4223-6
DOI：

Li, J., Wu, X., Tan, J. et al. Molecular cloning of the heat shock protein 20 gene from Paphia textile and its expression in response to heat shock., Chin. J. Ocean. Limnol. 33, 919–927 (2015). https://doi.org/10.1007/s00343-015-4223-6 DOI：

摘要

Abstract

P. textile is an important aquaculture species in China and is mainly distributed in Fujian

Guangdong

and Guangxi Provinces. In this study

an HSP20 cDNA designated PtHSP20 was cloned from P. textile. The full-length cDNA of PtHSP20 is 1 090 bp long and contains a 5′ untranslated region (UTR) of 93 bp

a 3′ UTR of 475 bp

and an open reading frame (ORF) of 522 bp. The PtHSP20 cDNA encodes 173 amino acid residues and has a molecular mass of 20.22 kDa and an isoelectric point of 6.2. Its predicted amino acid sequence shows that PtHSP20 contains a typical α-crystallin domain (residues 77–171) and three polyadenylation signal-sequences at the C-terminus. According to an amino acid sequence alignment

PtHSP20 shows moderate homology to other mollusk sHSPs. PtHSP20 mRNA was present in all of the test tissues including the heart

digestive gland

adductor muscle

gonad

gill

and mantle

with the highest concentration found in the gonad. Under the stress of high temperature

the expression of PtHSP20 mRNA was down-regulated in all of the tissues except the adductor muscle and gonad.

关键词

Keywords

references

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