Both a short hydrophobic domain and a carboxyl-terminal hydrophilic region are important for signal function in the Escherichia coli leader peptidase.

@article{Zhu1989BothAS,
  title={Both a short hydrophobic domain and a carboxyl-terminal hydrophilic region are important for signal function in the Escherichia coli leader peptidase.},
  author={Hong Yin Zhu and Ross E. Dalbey},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 20},
  pages={11833-8}
}
Leader peptidase, typical of inner membrane proteins of Escherichia coli, does not have an amino-terminal leader sequence. This protein contains an internal signal peptide, residues 51-83, which is essential for assembly and remains as a membrane anchor domain. We have employed site-directed mutagenesis techniques to either delete residues within this… CONTINUE READING