Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion
| Autor: | Frédéric Cadoret, Loïc Quinton, Badreddine Douzi, Sandra Michel-Souzy, Geneviève Ball, Romé Voulhoux, Claire Raynaud |
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| Přispěvatelé: | Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie bactérienne (LCB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Spectrométrie de Masse, Université de Liège, ANR-14-CE09-0027,4D-SECRETION,Exploration multidimensionnelle du transport et de la sécrétion des éxoprotéines par la voie de type II(2014), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), LEROI, Delphine, Appel à projets générique - Exploration multidimensionnelle du transport et de la sécrétion des éxoprotéines par la voie de type II - - 4D-SECRETION2014 - ANR-14-CE09-0027 - Appel à projets générique - VALID |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Type 2 Secretion infectious disease [SDV]Life Sciences [q-bio] Virulence medicine.disease_cause Microbiology Biochemistry Interactome Protein–protein interaction 03 medical and health sciences Bacterial Proteins Protein Domains Type II Secretion Systems Protein targeting medicine Secretion Protein Structure Quaternary Molecular Biology effector recognition Gsp Chemistry Effector Protein Secretion Cell Biology Periplasmic space CbpD Cell biology [SDV] Life Sciences [q-bio] virulence 030104 developmental biology Secretory protein Periplasm Pseudomonas aeruginosa Xcp Protein Multimerization Protein Binding T2SS |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, 2018, 293 (50), pp.19441-19450. ⟨10.1074/jbc.RA117.001127⟩ Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (50), pp.19441-19450. ⟨10.1074/jbc.RA117.001127⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.RA117.001127⟩ |
| Popis: | International audience; In many Gram-negative bacteria, the type 2 secretion system (T2SS) plays an important role in virulence because of its capacity to deliver a large amount of fully folded protein effectors to the extracellular milieu. Despite our knowledge of most T2SS components, the mechanisms underlying effector recruitment and secretion by the T2SS remain enigmatic. Using complementary biophysical and biochemical approaches, we identified here two direct interactions between the secreted effector CbpD and two components, XcpY L and XcpZ M , of the T2SS assembly platform (AP) in the opportunistic pathogen Pseudomonas aeruginosa. Competition experiments indicated that CbpD binding to XcpY L is XcpZ M-dependent, suggesting sequential recruitment of the effector by the periplasmic domains of these AP components. Using the bacterial two-hybrid system, we then tested the influence of the effector on the AP protein-protein interaction network. Our findings revealed that the presence of the effector modifies the AP interactome and, in particular, induces XcpZ M homodimerization and increases the affinity between XcpY L and XcpZ M. The observed direct relationship between effector binding and T2SS dynamics suggests an additional synchronizing step during the type 2 secretion process, where the activation of the AP of the T2SS nanomachine is triggered by effector binding. |
| Databáze: | OpenAIRE |
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