TY - JOUR
T1 - Membrane topology of three Xcp proteins involved in exoprotein transport by Pseudomonas aeruginosa
AU - Bleves, Sophie
AU - Lazdunski, Andrée
AU - Filloux, Alain
PY - 1996
Y1 - 1996
N2 - 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.
AB - 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.
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U2 - 10.1128/jb.178.14.4297-4300.1996
DO - 10.1128/jb.178.14.4297-4300.1996
M3 - Article
C2 - 8763961
AN - SCOPUS:0030013762
SN - 0021-9193
VL - 178
SP - 4297
EP - 4300
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 14
ER -