Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus.

@article{Dedent2008SignalPD,
  title={Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus.},
  author={Andrea C Dedent and Taeok Bae and Dominique Missiakas and Olaf Schneewind},
  journal={The EMBO journal},
  year={2008},
  volume={27 20},
  pages={
          2656-68
        }
}
Surface proteins of Gram-positive bacteria are covalently linked to the cell wall envelope by a mechanism requiring an N-terminal signal peptide and a C-terminal LPXTG motif sorting signal. We show here that surface proteins of Staphylococcus aureus arrive at two distinct destinations in the bacterial envelope, either distributed as a ring surrounding each cell or as discrete assembly sites. Proteins with ring-like distribution (clumping factor A (ClfA), Spa, fibronectin-binding protein B… CONTINUE READING
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