Abstract
BackgroundPhospholipases hydrolyze glycerophospholipids and generate diverse lipid-derived molecules with secondary messenger activity. Out of these, phospholipase C (PLC) specifically cleaves the phospholipids at ester linkages and yields diacylglycerol (DAG) and phosphorylated head groups. PLCs are classified further as phosphatidylinositol-specific PLCs (PI-PLCs) and non-specific PLCs with biased specificity for phosphatidylcholine (NPC/PC-PLC). ResultsIn the present report, we identified and characterized PLC genes in the genomes of three orchids, Phalaenopsis equestris (seven PePLCs), Dendrobium catenatum (eight DcPLCs), and Apostasia shenzhenica (seven AsPLCs). Multiple sequence alignment analysis confirmed the presence of conserved X and Y catalytic domains, calcium/lipid-binding domain (C2 domain) at the C terminal region, and EF-hand at the N-terminal region in PI-PLC proteins and esterase domain in PC-PLC. Systematic phylogenetic analysis established the relationship of the PLC protein sequences and clustered them into two groups (PI-PLC and PC-PLC) along with those of Arabidopsis thaliana and Oryza sativa. Gene architecture studies showed the presence of nine exons in all PI-PLC genes while the number varied from one to five in PC-PLCs. RNA-seq-based spatio-temporal expression profile for PLC genes was generated, which showed that PePC-PLC1, PePC-PLC2A, DcPC-PLC1A, DcPC-PLC1B, DcPC-PLC2, DcPC-PLC1B, and AsPC-PLC1 had significant expression in all reproductive and vegetative tissues. The expression profile is matched to their upstream cis-regulatory promoter elements, which indicates that PLC genes have a role in various growth and development processes and during stress responses. ConclusionsThe present study unwrapped the opportunity for functional characterization of selected PLC genes in planta for plant improvement.
Highlights
Phospholipases hydrolyze glycerophospholipids and generate diverse lipid-derived molecules with secondary messenger activity
Members of both sub-groups of phospholipase C (PLC) have their own specific signature domains: phosphatidylinositol-specific PLCs (PI-PLCs) group consists of X and Y catalytic domains, which leads to the formation of the TIM barrel-like structure essential for the phosphoesterase activity, a calcium/lipid-binding domain (C2 domain) at the C terminal region, and EFhand at N-terminal region to guide the binding of the enzyme to a membrane and PC-PLC contains only esterase domain
The PLC gene family in all three plants could be successfully divided into two major groups, phosphatidylinositol-specific PLC (PI-PLCs) and nonspecific phospholipase C with specific catalytic activity for phosphatidylcholine (PC-PLC/NPC)
Summary
Phospholipases hydrolyze glycerophospholipids and generate diverse lipid-derived molecules with secondary messenger activity. Phospholipase C is considered one of the essential lipid-hydrolyzing enzymes; it cleaves the ester linkage of phospholipid molecule of the plasma membrane and yields a watersoluble phospholipid head group and diacylglycerol (DAG) [3]. [20], Avena sativa [21], Lilium daviddi [22], Zea mays [23], and Physcomitrella patens [24, 25] Members of both sub-groups of PLC have their own specific signature domains: PI-PLC group consists of X and Y catalytic domains, which leads to the formation of the TIM (triphosphate isomerase) barrel-like structure essential for the phosphoesterase activity, a calcium/lipid-binding domain (C2 domain) at the C terminal region, and EFhand at N-terminal region to guide the binding of the enzyme to a membrane and PC-PLC contains only esterase domain
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