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

van Teeffelen, Sven1, 2; Vigouroux, Antoine1, 2; Cordier, Baptiste2; Aristov, Andrey2; Alvarez, Laura3; Özbaykal, Gizem2; Chaze, Thibault4; Oldewurtel, Enno Rainer2; Matondo, Mariette4; Cava, Felipe3; Bikard, David5

Published Jan 06, 2020 on Dryad. https://doi.org/10.5061/dryad.m37pvmcxq

Data files

Jan 07, 2020 version files 408.80 MB
Jan 06, 2020 version files 280.37 MB

Abstract

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.