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Transpeptidase PBP2 governs initial localization and activity of major cell-wall synthesis machinery in Escherichia coli

Eva Wollrab, View ORCID ProfileGizem Özbaykal, View ORCID ProfileAntoine Vigouroux, View ORCID ProfileBaptiste Cordier, View ORCID ProfileFrancois Simon, Thibault Chaze, View ORCID ProfileMariette Matondo, View ORCID ProfileSven van Teeffelen
doi: https://doi.org/10.1101/716407
Eva Wollrab
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
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Gizem Özbaykal
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
2Université Paris Diderot, Sorbonne-Paris-Cité, Paris, France
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  • ORCID record for Gizem Özbaykal
Antoine Vigouroux
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
3Synthetic Biology Lab, Institut Pasteur, Paris, France
4Université Paris Descartes, Sorbonne-Paris-Cité, Paris, France
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  • ORCID record for Antoine Vigouroux
Baptiste Cordier
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
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Francois Simon
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
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Thibault Chaze
5Proteomics Platform, Institut Pasteur, Paris, France
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Mariette Matondo
5Proteomics Platform, Institut Pasteur, Paris, France
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  • ORCID record for Mariette Matondo
Sven van Teeffelen
1Morphogenesis and Microbial Growth Lab, Institut Pasteur, Paris, France
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  • ORCID record for Sven van Teeffelen
  • For correspondence: sven.vanteeffelen@gmail.com
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Abstract

Bacterial shape is physically determined by the peptidoglycan cell wall. The cell-wall-synthesis machinery responsible for rod shape in Escherichia coli is the processive ‘Rod complex’. Previously, cytoplasmic MreB filaments were thought to govern formation and localization of Rod complexes based on local cell-envelope curvature. However, using single-particle tracking of the transpeptidase PBP2, we found strong evidence that PBP2 initiates new Rod complexes by binding to a substrate different from MreB or any known Rod-complex component. This substrate is likely the cell wall. Consistently, we found only weak correlations between MreB and envelope curvature in the cylindrical part of cells. Residual correlations do not require any curvature-based Rod-complex initiation but can be attributed to persistent rotational motion. Therefore, local cell-wall architecture likely provides the cue for PBP2 binding and subsequent Rod-complex initiation. We also found that PBP2 has a limiting role for Rod-complex activity, thus supporting its central role.

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Posted July 28, 2019.
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Transpeptidase PBP2 governs initial localization and activity of major cell-wall synthesis machinery in Escherichia coli
Eva Wollrab, Gizem Özbaykal, Antoine Vigouroux, Baptiste Cordier, Francois Simon, Thibault Chaze, Mariette Matondo, Sven van Teeffelen
bioRxiv 716407; doi: https://doi.org/10.1101/716407
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Transpeptidase PBP2 governs initial localization and activity of major cell-wall synthesis machinery in Escherichia coli
Eva Wollrab, Gizem Özbaykal, Antoine Vigouroux, Baptiste Cordier, Francois Simon, Thibault Chaze, Mariette Matondo, Sven van Teeffelen
bioRxiv 716407; doi: https://doi.org/10.1101/716407

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