Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa.

@article{Bleves1999StructurefunctionAO,
  title={Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa.},
  author={Sophie Bleves and Manon G{\'e}rard-Vincent and Andr{\'e}e M. Lazdunski and Alain Filloux},
  journal={Journal of bacteriology},
  year={1999},
  volume={181 13},
  pages={4012-9}
}
The general secretory pathway of Pseudomonas aeruginosa is required for the transport of signal peptide-containing exoproteins across the cell envelope. After completion of the Sec-dependent translocation of exoproteins across the inner membrane and cleavage of the signal peptide, the Xcp machinery mediates translocation across the outer membrane. This machinery consists of 12 components, of which XcpQ (GspD) is the sole outer membrane protein. XcpQ forms a multimeric ring-shaped structure… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 25 extracted citations

Similar Papers

Loading similar papers…