Characterization of 13 glycerophosphodiester phosphodiesterase in rice
2016
Oane, R.H. | Enriquez, B.A. | Mendoza, E.M.T. | Kohli, A.
Glycerophosphodiester phosphodiesterase (GDPD) belongs to a class of hydrolase enzymes that catalyzes the breakdown of a broad range of glycerophosphodiesters into sn-glycerol-3-phosphate and alcohol. These substrates include glycerophosphocholine, glycerophospho ethanolamine, glycerophosphoserine, glycerophosphoglycerol and glycerophosphoinositol. There are many articles published GDPD from Escherichia coli to human but very few studies were reported on the importance of GDPD in plants especially in rice. Recent studies on Arabidopsis showed that GDPD were shown to be highly expressed in siligues and this gene is said to be important in plant P homeostasis. To shed light into the role played by GDPD in rice, the 13 identified GDPD isoforms were characterized. The genomic organization, chromosomal location, nucleotide and protein sequence were analyzed. Results showed that the rice OsGDPD genes can be classified into two groups based on the presence of glycerophosphodiester (GP PDE) domain. The group (Type 1) with one domain consists of no more than 400 amino acid while group with 2 protein domain (Type 2) consists of 700-780 amino acid. Phylogenetic analysis showed that 4 of rice GDPDs belong to the same clade as E. coli and Arabidopsis GDPD1. Analysis of gene expression showed that 7 of OsGDPD are expressed in calli, root, shoot, peduncle, flagleaf and spikelets but highest expression was observed in spikelets in 5/13 of the OsGDPD tested. When further analyzed, OsGDPD sub 12.1 showed the strongest expression in anther, ovule, stigma, filament and lodicules of rice florets. The gene expression results showed that OsGDPD may play an important role in different events in rice flowering.
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