| Tolerance to environmental stress in plants is controlled by several internal factors and environmental signals. In this study, we have focused on phosphatidylinositol-specific phospholipase C (TaPI-PLC) and phosphoglycerol-specific phospholipase C (TaPG-PLC) in wheat, Triticum aestivum . Three homologs of TaPG-PLCs were identified as cDNA with high sequence similarity to rice and Arabidopsis PG-PLC1. TaPG-PLC3 was mapped on the distal part of the long arm of chromosome 5A, whereas TaPG-PLC1 and TaPG-PLC2 like genes appear to be duplicated in two of hexploid wheat 3 three genomes. A TaPG-PLC1::Green fluorescent protein (GFP)-fusion was localized on endoplasmic reticulum (ER), golgi and plasma membrane (PM). Important protein-protein interactions were found for wheat PI-PLCs. The PI-PLCI::GFP fusion was localized on ER-and PM. In vivo interactions between TaPI-PLC1 and two classes of G-proteins, the heterotrimeric G protein subunit TaGa and a non-canonicat G-protein J822, were detected using Bimolecular Fluorescent Complementation (BiFC). The interactions were detected in both the ER and PM. In contrast, TaPI-PLC2::GFP fusion was localized only on PM and was not found to interact with TaGalpha or J822 . Since both TaPI-PLC 1 and J822 are up-regulated by cold stress and it is possible that they play an important role in signaling during cold acclimation. |
