Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.

@article{Bageshwar2009InterconvertibilityOL,
  title={Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI.},
  author={Umesh K. Bageshwar and Neal Whitaker and F Q Liang and Siegfried M Musser},
  journal={Molecular microbiology},
  year={2009},
  volume={74 1},
  pages={
          209-226
        }
}
Signal peptides target protein cargos for secretion from the bacterial cytoplasm. These signal peptides contain a tri-partite structure consisting of a central hydrophobic domain (h-domain), and two flanking polar domains. Using a recently developed in vitro transport assay, we report here that a central h-domain position (C17) of the twin arginine translocation (Tat) substrate pre-SufI is especially sensitive to amino acid hydrophobicity. The C17I mutant is transported more efficiently than… CONTINUE READING

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