Pheromone-gland-specific fatty-acyl reductase in the adzuki bean borer,Ostrinia scapulalis (Lepidoptera: Crambidae) |
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| Authors: | Binu Antony Takeshi Fujii Ken'ichi Moto Shogo Matsumoto Mai Fukuzawa Ryo Nakano Sadahiro Tatsuki Yukio Ishikawa |
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| Institution: | 1. Laboratory of Applied Entomology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan;2. Molecular Entomology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama 351-0198, Japan;1. Ministry of Education Engineering Research Center of Starch & Protein Processing, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China;2. Key Laboratory of Environment Correlative Dietology (Ministry of Education), College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China;1. Graduate School of Science and Engineering, University of Toyama, Toyama, Toyama 930-8555, Japan;2. National Institute of Agrobiological Sciences, Ohwashi 1-2, Tsukuba, Ibaraki 305-8634, Japan;3. Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan;1. Department of Zoology, College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China;2. Department of Zoology, University of Melbourne, Parkville, Melbourne, Victoria 3010, Australia |
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| Abstract: | The adzuki bean borer moth, Ostrinia scapulalis, uses a mixture of (E)-11- and (Z)-11-tetradecenyl acetates as a sex pheromone. At a step in the pheromone biosynthetic pathway, fatty-acyl precursors are converted to corresponding alcohols by an enzyme, fatty-acyl reductase (FAR). Here we report the cloning of FAR-like genes expressed in the pheromone gland of female O. scapulalis, and the characterization of a single pheromone-gland-specific FAR (pgFAR) and its functional assay using an insect cell expression system. As many as thirteen FAR-like genes (FAR-I–FAR-XIII) were expressed in the pheromone gland of O. scapulalis; however, only one (FAR-XIII) was pheromone-gland-specific. The deduced amino acid sequence of FAR-XIII predicted a 462-aa protein with a conserved NAD(P)H-binding motif in the N-terminal region, showing overall identity of 34% with the pgFAR of Bombyx mori. A functional assay using Sf9 cells transfected with an expression vector containing the open reading frame of the FAR-XIII gene has proven that FAR-XIII protein has the ability to convert a natural substrate, (Z)-11-tetradecenoic acid, to a corresponding alcohol, (Z)-11-tetradecenol. |
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