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Isolation of a FAD-GPDH gene encoding a mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase from Dunaliella salina

Authors

  • Wanggui Yang,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Yi Cao,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Xiaofei Sun,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Fei Huang,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Qinghua He,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Dairong Qiao,

    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
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  • Linhan Bai Dr.

    Corresponding author
    1. College of Life Science, Sichuan University, Sichuan Public Experimental Platform of Bioinformatics and Metabolic Engineering, Sichuan, P. R. China
    • Phone: +86 028 85412842, Fax: +86 028 85411099
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Abstract

The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase (FAD-GPDH), recently reported in plants, has been detailed in yeast and animal systems. It oxidizes glycerol-3-phosphate (G-3-P) to dihydroxyacetone phosphate (DHAP) on the outer surface of mitochondrial inner membrane. A cDNA encoding the Dunaliella salina mitochondrial glycerol-3-phosphate dehydrogenase (DsFAD-GPDH) has been cloned and sequenced. The full length cDNA is 2791 bp, with an open reading frame (ORF) encoding 650 predicted amino acids, which show strong homology to reported FAD-GPDHs and have an apparent mitochondrial targeting sequence in the N-terminal. The sequence has been submitted to the GenBank database under Accession No. DQ916107. Results of Real-Time Quantitative PCR and enzymatic assays show that expression of DsFAD-GPDH is enhanced at first by salt treatment, and repressed by oxygen deficiency and cold stress. (© 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)

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