Title Cloning, Expression, and Functional Characterization of the Dunaliella salina 5-enolpyruvylshikimate-3-phosphate Synthase Gene in Escherichia coli
Author Yi Yi1, Dairong Qiao1,2, Linhan Bai1,2, Hui Xu1, Ya Li1, Xiaolin Wang1, and Yi Cao1,2*
Address 1Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, College of Life Sciences, Sichuan University, Sichuan 610064, P. R. China, 2Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan 610064, P. R. China
Bibliography Journal of Microbiology, 45(2),153-157, 2007,
DOI
Key Words Dunaliella salina, EPSP synthase, glyphosate tolerant
Abstract 5-enolpyruvylshikimate-3-phosphate synthase (EPSP synthase, EC 2.5.1.19) is the sixth enzyme in the shikimate pathway which is essential for the synthesis of aromatic amino acids and many secondary metabolites. The enzyme is widely involved in glyphosate tolerant transgenic plants because it is the primary target of the nonselective herbicide glyphosate. In this study, the Dunaliella salina EPSP synthase gene was cloned by RT-PCR approach. It contains an open reading frame encoding a protein of 514 amino acids with a calculated molecular weight of 54.6 KDa. The derived amino acid sequence showed high homology with other EPSP synthases. The Dunaliella salina EPSP synthase gene was expressed in Escherichia coli and the recombinant EPSP synthase were identified by functional complementation assay.
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