The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions.

@article{Hardie1996TheSC,
  title={The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions.},
  author={Kim Rachael Hardie and A. Seydel and Ingrid Guilvout and Anthony P. Pugsley},
  journal={Molecular microbiology},
  year={1996},
  volume={22 5},
  pages={967-76}
}
The chaperone-like protein of the main terminal branch of the general secretory pathway from Klebsiella oxytoca, the outer membrane lipoprotein PulS, protects the multimeric secretin PulD from degradation and promotes its correct localization to the outer membrane. To determine whether these are separable functions, or whether resistance to proteolysis results simply from correct localization of PulD, we replaced the lipoprotein-type signal peptide of PulS by the signal peptide of periplasmic… CONTINUE READING
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