Isolation and characterization of the trehalose-6-phosphate synthase gene from Locusta migratoria manilensis

作     者：Shu-Yan Cui Yu-Xian Xia 2008-09-16 

作者机构：School of Bioengineering Chongqing University Chongqing Engineering Research Center for Fungal Insecticide The Key Laboratory of Gene Function and Expression Regulation Chongqing China 

出 版 物：《Insect Science》 (昆虫科学（英文版）)

年 卷 期：2009年第16卷第4期

页      面：287-295页

核心收录：

学科分类：0832[工学-食品科学与工程（可授工学、农学学位）] 081703[工学-生物化工] 08[工学] 0817[工学-化学工程与技术] 0836[工学-生物工程] 082203[工学-发酵工程] 0822[工学-轻工技术与工程] 083203[工学-农产品加工及贮藏工程] 

基　　金：supported by grants from the National High Technology Research and Development Program Project 863’of China (No.2006AA10A212) the Program for New Century Excellent Talents in University Ministry of Education of P.R.China (No.NCET-NCET-04-851) 

主　　题：cloning Locusta migratoria-manilensis trehalose-6-phosphate synthase,RT-PCR 

摘      要：Trehalose plays an important role in protecting organisms from various stresses. Trehalose-6-phosphate synthase （TPS） is the key enzyme in trehalose synthesis, but in insects only a few TPS genes have been identified and their function has not been well characterized. To better understand the function of TPS in insects, a complete TPS complementary DNA （eDNA） clone was obtained from the fat body of the locust Locusta migratoria manilensis （GenBank accession number： EU131894）. The full-length cDNA is 2 806 bp, including an open reading frame of 2 442 bp, which encodes an 813 amino acids protein with a calculated molecular weight of 91 976 Daltons and an isoelectric point of 6.14. The deduced amino acid sequence is highly similar to other published insect TPS and its C-terminal also has a region homologous to trehalose phosphate phsophatase （TPP）. Semi-quantitative analysis indicated that the TPS transcript was expressed not only in fat body, but also in gut, hemolymph and leg muscle. These data may facilitate studies of TPS function in insects and improve our understanding of trehalose metabolism.