Cotranslational integration of soybean (Glycine max) oil body membrane protein oleosin into microsomal membranes

Storage triglycerides in oil seeds are sequestered in discrete organelles termed oil bodies. They are bounded by a monolayer of phospholipids in which a few distinct proteins (oleosins) are embedded. Synthesis of soybean (Glycine max) 24-kD oleosin was analyzed by in vitro transcription and translation in reticulocyte lysate in the presence of canine microsomes. Our results show that 24-kD oleosin is cotranslationally integrated into microsomal membranes. We demonstrate that oleosin is integrated into a bilayer membrane in preference to the oil body monolayer membrane, indicating that oleosin is synthesized on the endoplasmic reticulum (ER). A new model of oil body assembly involving a conformational change through initial association with the ER membrane is proposed.