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Characterization of the elongasome core PBP2 : MreC complex of Helicobacter pylori

Meriem El Ghachi 1, 2 Pierre-Jean Matteï 3 Chantal Ecobichon 1, 2 Alexandre Martins 3 Sylviane Hoos 4 Christine Schmitt 5 Frédéric Colland 6 Christine Ebel 3 Marie-Christine Prévost 5 Frank Gabel 3 Patrick England 7, 4 Andréa Dessen 3, * Ivo Boneca 1, 2, *
* Corresponding author
1 BGPB - Biologie et Génétique de la Paroi bactérienne - Biology and Genetics of Bacterial Cell Wall
2 INSERM - Institut National de la Santé et de la Recherche Médicale
3 IBSM - Institut de biologie structurale et microbiologie
4 Biophysique des Macromolécules et de leurs Interactions
5 Microscopie ultrastructurale (plate-forme)
6 Hybrigenics [Paris]
7 Institut Pasteur [Paris]
Abstract : The definition of bacterial cell shape is a complex process requiring the participation of multiple components of an intricate macromolecular machinery. We aimed at characterizing the determinants involved in cell shape of the helical bacterium Helicobacter pylori. Using a yeast two-hybrid screen with the key cell elongation protein PBP2 as bait, we identified an interaction between PBP2 and MreC. The minimal region of MreC required for this interaction ranges from amino acids 116 to 226. Using recombinant proteins, we showed by affinity and size exclusion chromatographies and surface plasmon resonance that PBP2 and MreC form a stable complex. In vivo, the two proteins display a similar spatial localization and their complex has an apparent 1:1 stoichiometry; these results were confirmed in vitro by analytical ultracentrifugation and chemical cross-linking. Small angle X-ray scattering analyses of the PBP2 : MreC complex suggest that MreC interacts directly with the C-terminal region of PBP2. Depletion of either PBP2 or MreC leads to transition into spherical cells that lose viability. Finally, the specific expression in trans of the minimal interacting domain of MreC with PBP2 in the periplasmic space leads to cell rounding, suggesting that the PBP2/MreC complex formation in vivo is essential for cell morphology.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-03525624
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Submitted on : Friday, January 14, 2022 - 12:22:36 AM
Last modification on : Thursday, April 7, 2022 - 10:10:43 AM

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Meriem El Ghachi, Pierre-Jean Matteï, Chantal Ecobichon, Alexandre Martins, Sylviane Hoos, et al.. Characterization of the elongasome core PBP2 : MreC complex of Helicobacter pylori. Molecular Microbiology, Wiley, 2011, 82 (1), pp.68 - 86. ⟨10.1111/j.1365-2958.2011.07791.x⟩. ⟨pasteur-03525624⟩

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