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Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia

机译:猪鞭草胞质热休克蛋白90(FcHSP90)的克隆及其对热休克和缺氧的表达反应

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摘要

Heat shock protein 90 (HSP90) works as a multi-functional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.
机译:热休克蛋白90(HSP90)可作为多功能伴侣,并参与许多重要细胞途径的调控。在这项研究中,我们已经从中国虾对虾Fenneropenaeus chinensis中鉴定了HSP90(FcHSP90)的全长互补DNA(cDNA)。 FcHSP90全长cDNA包含2552 bp,包括2181 bp的开放阅读框,编码726个氨基酸。使用与先前鉴定的HSP90和系统进化树的比对进行的两个同源性分析表明,FcHSP90是细胞质HSP90。实时逆转录聚合酶链反应分析表明,FcHSP90在所有检查的组织中普遍表达,但在中华小子的卵巢中表达最高。 FcHSP90 mRNA水平由热休克(从25°C到35°C)敏感地诱导,并在热休克治疗期间的6小时达到最大值。在缺氧条件下,在缺氧应激过程中,血细胞和g中的FcHSP90 mRNA水平在2小时被诱导,而在8小时被压低。对热休克和缺氧胁迫下FcHSP90 mRNA水平的评估表明,FcHSP90的转录对热休克和缺氧非常敏感,因此我们推断FcHSP90可能对虾应对环境胁迫起着非常重要的作用。

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