Five small heat shock protein genes from Chilo suppressalis: characteristics of gene, genomic organization, structural analysis, and transcription profiles
Five small heat shock protein genes from Chilo suppressalis: characteristics of gene, genomic organization, structural analysis, and transcription profiles
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DOI：
10.1007/s12192-013-0437-8
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发表时间：
2014-01-01
影响因子：
3.8
通讯作者：
Du, Yu-Zhou
中科院分区：
文献类型：
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作者：
Lu, Ming-Xing;Hua, Jin;Du, Yu-Zhou
小热休克蛋白 (sHSP) 是最多样化但也是最鲜为人知的分子伴侣家族，它们在各种生物过程中发挥着重要作用。条纹螟二化螟（昆虫纲：鳞翅目：螟科）是水稻最严重的害虫之一，造成广泛的损害和产量损失。在本研究中，我们从二化螟中分离并鉴定了 sHSP 家族的五个成员 - Cshsp19.8、Cshsp21.4、Cshsp21.5、Cshsp21.7a 和 Cshsp21.7b。这些基因的cDNA编码177、187、191、191和191个氨基酸的蛋白质，等电点分别为7.0、5.6、6.1、6.3和6.3。 Cshsp19.8、Cshsp21.5 和 Cshsp21.7b 没有内含子，而 Cshsp21.4 和 Cshsp21.7a 分别含有 1 个和 2 个内含子。结构分析表明，所有 5 个 Cshsp 均具有保守的精氨酸和 V/IXI/V 基序，这与 sHSP 的疏水特性有关。五种热休克蛋白可分为两大类：直系同源类型（Cshsp21.4 和 Cshsp21.7a）和物种特异性类型（Cshsp19.8、Cshsp21.5 和 Cshsp21.7b）。实时定量PCR分析显示，Cshsp19.8、Cshsp21.5、Cshsp21.7a和Cshsp21.7b均在马氏小管或后肠中表现出最高的表达水平，而Cshsp21.4的这种水平在头部中发现。 Csshsps在不同发育阶段的表达表明，Cshsp19.8、Cshsp21.4、Cshsp21.5和Cshsp21.7b的mRNA水平在成虫中达到峰值，而Cshsp21.7a在一龄幼虫中观察到最高水平。 Cshsp19.8和Cshsp21.7b均因热和冷而显着上调，而Cshsp21.5可被冷应激诱导。 Cshsp21.4 和 Cshsp21.7a 都对热或冷没有反应。这些结果表明不同的Csshsps在二化螟生理活动的调节中发挥着独特的作用。
Small heat shock proteins (sHSPs) are the most diverse but also the most poorly known family of molecular chaperones, and they play essential roles in various biological processes. The striped stem borer, Chilo suppressalis (Insecta: Lepidoptera: Pyralidae), is one of the most serious pests of rice, causing extensive damage and yield loss. In this study, we isolated and characterized five members of the sHSPs family-Cshsp19.8, Cshsp21.4, Cshsp21.5, Cshsp21.7a, and Cshsp21.7b-from C. suppressalis. The cDNAs of these genes encoded proteins of 177, 187, 191, 191, and 191 amino acids with isoelectric points of 7.0, 5.6, 6.1, 6.3, and 6.3, respectively. While Cshsp19.8, Cshsp21.5, and Cshsp21.7b had no introns, Cshsp21.4 and Cshsp21.7a contained one and two introns, respectively. Structural analysis indicated that all five Cshsps possessed conserved arginine and a V/IXI/V motif, which is related to hydrophobic characteristics of sHSPs. The five heat shock proteins can be classified into two main groups: an orthologous type (Cshsp21.4 and Cshsp21.7a) and a species-specific type (Cshsp19.8, Cshsp21.5, and Cshsp21.7b). Real-time quantitative PCR analyses revealed that Cshsp19.8, Cshsp21.5, Cshsp21.7a, and Cshsp21.7b all exhibited their highest expression levels within Malpighian tubules or the hindgut, while such levels were found in the head for Cshsp21.4. The expression of Csshsps at different developmental stages revealed that the mRNA levels of Cshsp19.8, Cshsp21.4, Cshsp21.5, and Cshsp21.7b peaked in adults, whereas the highest level of Cshsp21.7a was observed in first instar larvae. Cshsp19.8 and Cshsp21.7b were both upregulated dramatically by heat and cold, and Cshsp21.5 could be induced by cold stress. Neither Cshsp21.4 nor Cshsp21.7a responded to heat or cold. These results demonstrated that different Csshsps play distinctive roles in the regulation of the physiological activities in C. suppressalis.