Identification of XcpZ domains required for assembly of the secreton of Pseudomonas aeruginosa.
J Bacteriol
; 184(6): 1779-82, 2002 Mar.
Article
en En
| MEDLINE
| ID: mdl-11872731
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Pseudomonas aeruginosa
/
Proteínas Bacterianas
/
Proteínas de la Membrana
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
J Bacteriol
Año:
2002
Tipo del documento:
Article
País de afiliación:
Francia