Abstract
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.