TY - JOUR TI - The transpeptidase PBP2 governs initial localization and activity of the major cell-wall synthesis machinery in E. coli AU - Özbaykal, Gizem AU - Wollrab, Eva AU - Simon, Francois AU - Vigouroux, Antoine AU - Cordier, Baptiste AU - Aristov, Andrey AU - Chaze, Thibault AU - Matondo, Mariette AU - van Teeffelen, Sven A2 - Mignot, Tâm A2 - Storz, Gisela VL - 9 PY - 2020 DA - 2020/02/20 SP - e50629 C1 - eLife 2020;9:e50629 DO - 10.7554/eLife.50629 UR - https://doi.org/10.7554/eLife.50629 AB - 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. Using single-particle tracking of the transpeptidase and Rod-complex component PBP2, we found that PBP2 binds to a substrate different from MreB. Depletion and localization experiments of other putative Rod-complex components provide evidence that none of those provide the sole rate-limiting substrate for PBP2 binding. Consistently, we found only weak correlations between MreB and envelope curvature in the cylindrical part of cells. Residual correlations do not require curvature-based Rod-complex initiation but can be attributed to persistent rotational motion. We therefore speculate that the local cell-wall architecture provides the cue for Rod-complex initiation, either through direct binding by PBP2 or through an unknown intermediate. KW - cell-wall insertion KW - single-enzyme dynamics KW - MreB cytoskeleton KW - bacterial morphogenesis KW - Rod complex JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -