Reference : Direct interactions between the secreted effector and the T2SS components GspL and Gs...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/233227
Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion
English
Michel-Souzy, S. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France]
Douzi, B. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France, CNRS, Aix Marseille Université, IMM, Laboratoire de Chimie Bactérienne (LCB)/UMR7283, Marseille, 13009, France]
Cadoret, F. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France]
Raynaud, C. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France, CNRS, Aix Marseille Université, IMM, Laboratoire de Chimie Bactérienne (LCB)/UMR7283, Marseille, 13009, France]
Quinton, Loïc mailto [Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique >]
Ball, G. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France, CNRS, Aix Marseille Université, IMM, Laboratoire de Chimie Bactérienne (LCB)/UMR7283, Marseille, 13009, France]
Voulhoux, R. [CNRS, Aix Marseille Université, Institut de Microbiologie de la Méditerranée (IMM), Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM)/UMR7255, Marseille, 13009, France, CNRS, Aix Marseille Université, IMM, Laboratoire de Chimie Bactérienne (LCB)/UMR7283, Marseille, 13009, France]
2018
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology Inc.
293
50
19441-19450
Yes (verified by ORBi)
International
00219258
[en] Bacteria ; Hybrid systems ; Proteins ; Direct interactions ; Effector binding ; Gram-negative bacteria ; Homodimerization ; Protein interaction networks ; Pseudomonas aeruginosa ; Secretion systems ; Two-hybrid system ; Physiology ; Pseudomonas aeruginosa
[en] 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, XcpYL and XcpZM, of the T2SS assembly platform (AP) in the opportunistic pathogen Pseudomonas aeruginosa. Competition experiments indicated that CbpD binding to XcpYL is XcpZM-dependent, suggesting sequential recruitment of the effector by the periplasmic domains of these AP components. Using a 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 XcpZM homodimerization and increases the affinity between XcpYL and XcpZM. 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. © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.
http://hdl.handle.net/2268/233227
10.1074/jbc.RA117.001127

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