Specificity of signal peptide recognition in tat-dependent bacterial protein translocation.

@article{Blaudeck2001SpecificityOS,
  title={Specificity of signal peptide recognition in tat-dependent bacterial protein translocation.},
  author={Natascha Blaudeck and Georg A. Sprenger and Roland Freudl and Thomas Wiegert},
  journal={Journal of bacteriology},
  year={2001},
  volume={183 2},
  pages={604-10}
}
The bacterial twin arginine translocation (Tat) pathway translocates across the cytoplasmic membrane folded proteins which, in most cases, contain a tightly bound cofactor. Specific amino-terminal signal peptides that exhibit a conserved amino acid consensus motif, S/T-R-R-X-F-L-K, direct these proteins to the Tat translocon. The glucose-fructose oxidoreductase (GFOR) of Zymomonas mobilis is a periplasmic enzyme with tightly bound NADP as a cofactor. It is synthesized as a cytoplasmic precursor… CONTINUE READING

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