Kim Meesun, Ahn In-Young, Kim Hakjun, Cheon Jina, Park Hyun
Korea Polar Research Institute, Korea Ocean Research and Development Institute (KORDI), Incheon, South Korea.
Cell Stress Chaperones. 2009 Jul;14(4):363-70. doi: 10.1007/s12192-008-0090-9. Epub 2008 Nov 6.
Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays a key role in protein synthesis, folding, denaturation prevention, and signal transduction. We cloned the complete complementary DNA (cDNA) sequence of the Laternula elliptica HSP90. The full-length cDNA was 2,823 bp in size and contained an open reading frame of 2,190 bp that was translated into 729 amino acids with a calculated molecular weight of 83.4 kDa. The deduced amino acid sequence of HSP90 showed the highest homology to Haliotis tuberculata HSP90 (83%). Reverse-transcriptase polymerase chain reaction analysis revealed the presence of HSP90 transcripts in all of the tissues examined. We also studied the transcriptional expression pattern of HSP90 exposed to thermal stress with real-time polymerase chain reaction. The relative expression level of HSP90 messenger RNA was upregulated and peaked at 12 h in the digestive gland and at 24 h in the gills, then dropped progressively.
热休克蛋白90（HSP90）是一种高度保守的分子伴侣，在蛋白质合成、折叠、防止变性和信号转导中起关键作用。我们克隆了椭圆海笋HSP90的完整互补DNA（cDNA）序列。全长cDNA大小为2823 bp，包含一个2190 bp的开放阅读框，该阅读框被翻译成729个氨基酸，计算分子量为83.4 kDa。HSP90推导的氨基酸序列与瘤珠母贝HSP90的同源性最高（83%）。逆转录聚合酶链反应分析显示，在所检测的所有组织中均存在HSP90转录本。我们还通过实时聚合酶链反应研究了热应激下HSP90的转录表达模式。HSP90信使核糖核酸的相对表达水平上调，在消化腺中于12小时达到峰值，在鳃中于24小时达到峰值，然后逐渐下降。
