Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases.

@article{Szab2007IdentificationOD,
  title={Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases.},
  author={Zal{\'a}n Szab{\'o} and Adriana Oliveira Stahl and Sonja-Verena Albers and Jessica C. Kissinger and Arnold J M Driessen and Mechthild Pohlschr{\"o}der},
  journal={Journal of bacteriology},
  year={2007},
  volume={189 3},
  pages={772-8}
}
Most secreted archaeal proteins are targeted to the membrane via a tripartite signal composed of a charged N terminus and a hydrophobic domain, followed by a signal peptidase-processing site. Signal peptides of archaeal flagellins, similar to class III signal peptides of bacterial type IV pilins, are distinct in that their processing sites precede the hydrophobic domain, which is crucial for assembly of these extracytoplasmic structures. To identify the complement of archaeal proteins with… CONTINUE READING
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