Cloning of a heat shock protein 90 (HSP90) gene and expression analysis in the ridgetail white prawn Exopalaemon carinicauda
- 作者：Jitao Li ; Junying Han ; Ping Chen ; Zhiqiang Chang ; Yuying He ; Ping Liu ; Qingyin Wang ; Jian Li ; lijian@ysfri.ac.cn
- 关键词：Exopalaemon carinicauda ; Heat shock protein 90 (HSP90) ; Cloning ; Expression
- 刊名：Fish & Shellfish Immunology
- 出版年：2012
- 期刊代码：115_10504648
- 类别：abs
- 出版时间：June, 2012
- 卷：32
- 期：6
- 页码：1191-1197
- 文件大小：2226 K
摘要
Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. In this study, a heat shock protein 90 cDNA named EcHSP90 was cloned from the hepatopancreas of ridgetail white prawn Exopalaemon carinicauda by reverse transcription polymerase chain reaction (RT-PCR) coupled with rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of EcHSP90 was of 2695 bp, including an open reading frame (ORF) of 2163 bp encoding a polypeptide of 720 amino acids with an estimated molecular mass of 82.73聽kDa and an estimated isoelectric point of 4.83. BLAST analysis revealed that the EcHSP90 shared high similarity (87.6%-75.24%) with other known HSP90s. The 铿乿e conserved amino acid blocks de铿乶ed as HSP90 protein family signatures were also identi铿乪d in EcHSP90, which indicated that EcHSP90 should be a cytosolic member of the HSP90 family. Quantitative real-time RT-PCR analysis revealed that EcHSP90 transcript could be detected in all the tested tissues, and strongly expressed in ovary of E. carinicauda. The transcript of EcHSP90 in hepatopancreas of E. carinicauda showed different expression profiles after pH and ammonia-N stresses. The results indicated that EcHSP90 was a constitutive and inducible expressed protein and could be induced by various stresses from environment.