Isolation of a FAD-GPDH gene encoding a mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase from Dunaliella salina
✍ Scribed by Wanggui Yang; Yi Cao; Xiaofei Sun; Fei Huang; Qinghua He; Dairong Qiao; Linhan Bai
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 936 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
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)