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Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects


van Teeffelen, Sven et al. (2020), Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects, Dryad, Dataset,


Cell shape and cell-envelope integrity of bacteria are determined by the peptidoglycan cell wall. In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex and the class-A penicillin-binding proteins (aPBPs). While the Rod complex governs rod-like cell shape, aPBP function is less well understood. aPBPs were previously hypothesized to either work in concert with the Rod complex or to independently repair cell-wall defects. First, we demonstrate through modulation of enzyme levels that aPBPs do not contribute to rod-like cell shape but are required for mechanical stability, supporting their independent activity. By combining measurements of cell-wall stiffness, cell-wall insertion, and PBP1b motion at the single-molecule level, we then present evidence that PBP1b, the major aPBP, contributes to cell-wall integrity by repairing cell wall defects.

Usage Notes

- Tracking dataset: Each file is a csv (tab-separated) file with the X and Y positions of the particles, and the unique particle ID for each track. See ReadMe file.

- SDS Page raw images. See ReadMe file.



H2020 European Research Council, Award: 679980

H2020 European Research Council, Award: 677823

Agence Nationale de la Recherche, Award: ANR-10-LABX-62-IBEID

Volkswagen Foundation

Knut och Alice Wallenbergs Stiftelse



Mairie de Paris, Award: Emergence(s)

Laboratory for Molecular Infection Medicine Sweden