In vitro translational translocation of precursor ribose binding protein across inverted membrane vesicles and its binding to model membranes

Abstract

All proteins are synthesized in cytoplasm and transfered to their final location. Translocation across plasma membrane is very important phenomena to understand the mechanism of protein export. Precursor ribose binding protein is synthesized by in vitro translation and mixed with inverted membrane vesicles. $[^{35}S]$-Met-pRBP is translocated and processed to $[^{35}S]$-Met-mRBP. mRBP is seperated by SDS-PAGE and detected by autoradiogram. From above result we can say that pRBP is translocated across INV and is not affected by completely folded precursor form. From the binding patterns of RBP to INV and MLV, we can say that signal sequence is important to bind to MLV and hydrophobic interaction is a major force. Now we can say that in order to bind to INV, pRBP must be make a complex with unknown soluble factor and this factor has a dual function for targeting and antifolding.