Gupta S.M.,Defence Institute of Bio Energy Research DIBER DRDO |
Pandey P.,Defence Institute of Bio Energy Research DIBER DRDO |
Grover A.,Defence Institute of Bio Energy Research DIBER DRDO |
Patade V.Y.,Defence Institute of Bio Energy Research DIBER DRDO |
And 2 more authors.
Molecular Biology Reports | Year: 2013
Glycerol-3-phosphate acyltransferase (GPAT) catalyzes first and the rate limiting step in glycerolipid synthesis pathway, which in turn contribute to stabilization of plasma membrane structure and oil lipid synthesis in plant cells. Here, we report cloning and characterization of GPAT gene from Lepidium latifolium (LlaGPAT). The cDNA sequence (1,615 bp) of LlaGPAT gene consisted of 1,113 bp ORF encoding a protein of 370 aa residues, with deduced mass of 41.2 kDa and four acyltransferase (AT) motifs having role in catalysis and in glycerol-3-phosphate binding. Southern blot analysis suggested presence of a single copy of the gene in the genome. Tissue specific expression of the gene was seen more abundantly in aerial parts, compared to the roots. Quantitative real-time PCR indicated down-regulation of the gene by cold (4 C), drought (PEG6000), salt (300 mM NaCl) and ABA (100 μM) treatments. Considering the vitality of the function of encoded enzyme, LlaGPAT can be considered a potential candidate gene for genetic engineering of oil yields and abiotic stress management in food as well as fuel crops. © 2013 Springer Science+Business Media Dordrecht.