Substrate specificity of the SecB chaperone.

@article{Knoblauch1999SubstrateSO,
  title={Substrate specificity of the SecB chaperone.},
  author={Nicola T M Knoblauch and Stefan R{\"u}diger and H J Schoenfeld and Arnold J M Driessen and Jens Schneider-Mergener and Bernd Bukau},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 48},
  pages={34219-25}
}
The bacterial chaperone SecB assists translocation of proteins across the inner membrane. The mechanism by which it differentiates between secretory and cytosolic proteins is poorly understood. To identify its binding motif, we screened 2688 peptides covering sequences of 23 proteins for SecB binding. The motif is approximately 9 residues long and is enriched in aromatic and basic residues, whereas acidic residues are disfavored. Its identification allows the prediction of binding regions… CONTINUE READING