Phosphatidylglycerophosphate synthases from Arabidopsis thaliana
Related Experiment Video
Updated: Oct 3, 2026

Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography (TLC) Coupled with Gas-Liquid Chromatography (GLC)
Published on: March 18, 2011
1RWTH Aachen, Institut für Biologie I, Spezielle Botanik, Worringer Weg 1, 52056, Aachen, Germany.
Abstract:
Two Arabidopsis thaliana genes were shown to encode phosphatidylglycerophosphate synthases (PGPS) of 25.4 and 32.2 kDa, respectively. Apart from their N-terminal regions, the two proteins exhibit high sequence similarity. Functional expression studies in yeast provided evidence that the 25.4 kDa protein is a microsomal PGPS while the 32.2 kDa protein represents a preprotein which can be imported into yeast mitochondria and processed to a mature PGPS. The two isozymes were solubilized and purified as fusion proteins carrying a His tag at their C-terminus. Enzyme assays with both membrane fractions and purified enzyme fractions revealed that the two A. thaliana isozymes have similar properties but differ in their CDP-diacylglycerol species specificity.
Related Concept Videos
ATP Synthase: Structure
IP3/DAG Signaling Pathway
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Cell Signaling in Plants
Synthesis of Phosphatidylcholine in the ER Membrane
The major components of all eukaryotic cell...
Protein Transport to the Inner Chloroplast Membrane

