Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF)
| Autor: | Mohammed El Khattabi, Margot Koster, Geneviève Ball, Alain Filloux, Jan Tommassen, Jorik Arts, Arjan de Groot, Eric Durand |
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| Rok vydání: | 2007 |
| Předmět: |
Recombination
Genetic chemistry.chemical_classification biology Pseudomonas putida Pseudomonas aeruginosa Membrane Proteins Membrane Transport Proteins medicine.disease_cause biology.organism_classification Microbiology Protein Structure Tertiary Protein Transport Enzyme Bacterial Proteins Biochemistry chemistry Cytoplasm Protein Interaction Mapping Pseudomonadales medicine Extracellular Secretion Pseudomonadaceae |
| Zdroj: | Microbiology. 153:1582-1592 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/mic.0.2006/002840-0 |
| Popis: | Pseudomonas aeruginosa is an opportunistic pathogen, which secretes a wide variety of enzymes and toxins into the extracellular medium. Most exoproteins are exported by the type II secretion machinery, the Xcp system, which encompasses 12 different proteins. One of the core components of the Xcp system is the inner-membrane protein XcpS (GspF), homologues of which can be identified in type II secretion machineries as well as in type IV piliation systems. In this study, XcpS was shown to be stabilized by co-expression of the XcpR (GspE) and XcpY (GspL) components of the machinery, demonstrating an interaction between these three proteins. By replacing segments of P. aeruginosa XcpS with the corresponding parts of its Pseudomonas putida counterpart, XcpS domains were identified that are important for species-specific functioning and thus represent putative interaction domains. The cytoplasmic loop of XcpS was found to be involved in the stabilization by XcpR and XcpY. |
| Databáze: | OpenAIRE |
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