Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: cleavage of the nascent protein and addition of the PI-G moiety depend on the size of the COOH-terminal signal peptide.

@article{Kodukula1992BiosynthesisOP,
  title={Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: cleavage of the nascent protein and addition of the PI-G moiety depend on the size of the COOH-terminal signal peptide.},
  author={Krishna Kodukula and Douglas B Cines and Rodolfo Amthauer and Louise Diekmann Gerber and Sidney Udenfriend},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 4},
  pages={
          1350-3
        }
}
Nascent translation products of PI-G-anchored membrane proteins contain both NH2- and COOH-terminal signal sequences of approximately 15-30 residues that are removed during processing. Removal of the latter occurs concomitant with the addition of the PI-G moiety to the newly formed COOH terminus. In human placental alkaline phosphatase (PLAP) the COOH-terminal signal peptide contains 29 residues. An engineered form of PLAP, miniPLAP 208, containing the same NH2- and COOH-terminal signal… CONTINUE READING