TY - JOUR
T1 - Identification of XcpZ domains required for assembly of the secreton of Pseudomonas aeruginosa
AU - Robert, Viviane
AU - Hayes, Finbarr
AU - Lazdunski, Andrée
AU - Michel, Gérard P F
PY - 2002
Y1 - 2002
N2 - Most of the exoproteins secreted by Pseudomonas aeruginosa are transported via the type II secretion system. This machinery, which is widely conserved in gram-negative bacteria, consists of 12 Xcp proteins organized as a multiprotein complex, also called the secreton. We previously reported that the mutual stabilization of XcpZ and XcpY plays an important role in the assembly of the secreton. In this study, we engineered variant XcpZ proteins by using linker insertion mutagenesis. We identified three distinct regions of XcpZ required for both the stabilization of XcpY and the functionality of the secreton. Interestingly, we also demonstrated that another component of the machinery, XcpP, can modulate the stabilizing activity of XcpZ on XcpY.
AB - Most of the exoproteins secreted by Pseudomonas aeruginosa are transported via the type II secretion system. This machinery, which is widely conserved in gram-negative bacteria, consists of 12 Xcp proteins organized as a multiprotein complex, also called the secreton. We previously reported that the mutual stabilization of XcpZ and XcpY plays an important role in the assembly of the secreton. In this study, we engineered variant XcpZ proteins by using linker insertion mutagenesis. We identified three distinct regions of XcpZ required for both the stabilization of XcpY and the functionality of the secreton. Interestingly, we also demonstrated that another component of the machinery, XcpP, can modulate the stabilizing activity of XcpZ on XcpY.
U2 - 10.1128/JB.184.6.1779-1782.2002
DO - 10.1128/JB.184.6.1779-1782.2002
M3 - Article
SN - 0021-9193
VL - 184
SP - 1779
EP - 1782
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 6
ER -