| The heat shock proteins (Hsps) exist in almost all forms of life. They can restore denatured proteins, prevent aggregation of non-native proteins, and play crucial roles in protein quality control. In addition, Hsps have a closely relationship with autophagy. sHSPs and HSP10are belong to the heat shock protein family. They can act as molecular chaperones。The cotton aphid, Aphis gossypii Glover, the major insect pest for the cotton seeding, is widely distribution in the world. There is no information about Hsps in cotton aphid. In this paper, fluorescence quantitative and prokaryotic expressions were used to study Hsps. Our lab previously obtained two cotton aphid transcriptomes at different growth stages of cotton, seedling and summer. Now, we focus on cotton aphid and select four Hsps from cotton aphid transcriptome date:Agoshsp22.9, Agoshsp21.8, Agoshspll.2and Agoshspll. These Hsps were analyzed with Bioinformatics and expressed in Escherichia coli. We also detected the expressions of these Hsps by Quantitative real-time PCR in different developmental stages and temperatures. The results as follows:1. The Alignment of amino acid sequences indicate that Agoshsp22.9and Agoshsp21.8are belong to the sHSP family, Agoshsp11.2and Agoshspll are belong to HSP family.2. Predict the molecular weight sizes through biology software and name the four hsps based on this.3. The results of Quantitative real-time PCR indicate that the four hsps are expressed in all forms of cotton aphid. The expression of Agoshsp22.9, Agoshsp21.8and Agoshsp11.2are increased under the temperature stress and has a close relation with time. However, there is no obvious increase expression of Agoshsp11.4. The purification of proteins showed that the protein size consistent with predicted results.5. All four hsps can protect the E. coli against the high temperature in different degrees. |
