Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli.

@article{Ghrayeb1984NineAA,
  title={Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli.},
  author={John Ghrayeb and M. Inouye},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 1},
  pages={463-7}
}
We have examined the structural requirements at the NH2-terminal region of the lipoprotein for its assembly in the outer membrane of Escherichia coli by constructing a hybrid protein consisting of an NH2-terminal portion of the prolipoprotein, consisting of the signal peptide and 9 amino acid residues of lipoprotein, and the entire beta-lactamase sequence. The results from this study indicate that the hybrid protein is modified with glyceride, processed in a globomycin-sensitive step, and… CONTINUE READING