Membrane topology of three Xcp proteins involved in exoprotein transport by Pseudomonas aeruginosa

J Bacteriol. 1996 Jul;178(14):4297-300. doi: 10.1128/jb.178.14.4297-4300.1996.

Abstract

Xcp proteins constitute the secretory apparatus of Pseudomonas aeruginosa. Deduced amino acid sequence of xcp genes, expression, and subcellular localization revealed unexpected features. Indeed, most Xcp proteins are found in the cytoplasmic membrane although xcp mutations lead to periplasmic accumulation of exoproteins, indicating that the limiting step is translocation across the outer membrane. To understand the mechanism by which the machinery functions and the interactions between its components, it is valuable to know their membrane organization. We report data demonstrating the N(in)-C(out) topologies of three general secretion pathway components, the XcpP, -Y, and -Z proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / ultrastructure*
  • Base Sequence
  • Biological Transport
  • Membrane Proteins / analysis
  • Membrane Proteins / metabolism
  • Membrane Proteins / ultrastructure*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Pseudomonas aeruginosa / metabolism
  • Pseudomonas aeruginosa / ultrastructure*
  • Recombinant Fusion Proteins
  • Subcellular Fractions / chemistry

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Recombinant Fusion Proteins
  • XcpP protein, Pseudomonas aeruginosa
  • xcpY protein, Pseudomonas aeruginosa
  • xcpZ protein, Pseudomonas aeruginosa
  • Alkaline Phosphatase