We are excited to share two recent studies that reveal how E. coli bacteria remodel their cell envelope architecture and fortify it during cell division.
In our latest bioRxiv preprint, we uncovered a specialized role for the cell wall synthase PBP1b in reinforcing the E. coli division site. Using in situ cryo-electron tomography (cryo-ET), atomic force microscopy, and live-cell imaging, we show that PBP1b forms a wedge-shaped peptidoglycan structure that helps prevent osmotic rupture, acting independently of its usual activator LpoB. This reveals a new, specialized function of PBP1b and suggests similar mechanisms might be at work in other bacteria.
👉 Read the preprint here!
In another exciting project published in PNAS, we combined theoretical modeling and cryo-ET to demonstrate how mechanical stress guides E. coli division. Our lab contributed critical in situ cryo-ET data that helped visualize how stress and growth patterns shape cellular architecture during cell division.
👉 Read the paper here!
These studies highlight the power of interdisciplinary approaches, merging structural biology, physics, and microbiology, to uncover fundamental mechanisms of bacterial cell division.