Physiological effect of mild thermal stress and its induction of gene expression in the common cutworm, Spodoptera litura

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• 作者：Ying Shen ; Yan-Jun Gong ; Jun Gu ; Li-Hua Huang ; Qi-Li Feng
• 关键词：Heat shock protein ; EcR ; Trade-off ; Co-immunoprecipitation ; Subcellular localization
• 刊名：Journal of Insect Physiology
• 出版年：February, 2014
• 年：2014
• 卷：61
• 期：Complete
• 页码：34-41
• 全文大小：1153 K

文摘

Heat shock protein (Hsp) and its cognate protein (Hsc) play important roles in helping insects survive extreme temperatures. However, high level of Hsp expression usually brings negative physiological effects on organisms. The mechanism of this trade-off is unclear. In this study, a lepidopteran insect, the common cutworm Spodoptera litura, was stressed at different temperatures, and the impact on both thermotolerance and fecundity was examined. The mRNA levels of four Hsp/Hscs (Hsp90, Hsc90, Hsp70 and Hsc70) and two ecdysone receptors (EcRs, EcRA and EcRB1) in different stresses and during the larval-pupal metamorphosis were determined. The results revealed that the pre-acclamation at mild stress increased the thermotolerance but decreased the egg production in adults. During the stress process, the mRNA levels of all the Hsp/Hsc and ecdysone receptor genes were significantly up-regulated. The two Hsp/Hsc70s and EcRs revealed consistent expression profiles with each other during the larval-pupal metamorphosis. Co-immunoprecipitation and Western blotting analysis indicated that Hsp/Hsc70 interacted with EcRs. RNAi of Hsc70 decreased the mRNA levels of two 20E-induced genes such as E74B and E75. Hsp70 transferred from the cytoplasm to nucleus in response to cold stress. These data together suggest that Hsp/Hsc70 might be involved in the regulation of 20E signaling, and the protein-protein interaction between Hsp/Hsc70 and EcRs probably act as a bridge mediating the trade-off between high thermotolerance and physiological defects.