SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

@article{Akita1990SecAIW,
  title={SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.},
  author={Masahiko Akita and Sei Sasaki and Shigemi Matsuyama and Shoji Mizushima},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 14},
  pages={8164-9}
}
SecA is an acidic, peripheral membrane protein involved in the translocation of secretory proteins across the cytoplasmic membrane. The direct interaction of SecA with secretory proteins was demonstrated by means of chemical cross-linking with 1-ethyl-3-(3-dimethylaminoprophyl)carbodiimide. OmpF-Lpp, a model secretory protein, carries either an uncleavable or cleavable signal peptide, and mutant secretory proteins derived from uncleavable OmpF-Lpp were used as translocation substrates. The… CONTINUE READING
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