A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery

• DOI: 10.1371/journal.pgen.1007726
• Publication Date: 2018-10-18T17:30:51Z
• Authors: Patricia D. A. Rohs; Jackson Buss; Sue I. Sim; Georgia R. Squyres; Veerasak Srisuknimit; Mandy Smith; Hongbaek Cho; Megan Sjodt; Andrew C. Kruse; Ethan C. Garner; Suzanne Walker; Daniel E. Kahne; Thomas G. Bernhardt
• Keywords: 0301 basic medicine; Escherichia coli Proteins; Cell Cycle; Membrane Proteins; Peptidoglycan; QH426-470; Actins; Polymerization; 3. Good health; 03 medical and health sciences; Bacterial Proteins; Cell Wall; Polysaccharides; Genetics; Escherichia coli; Morphogenesis; Penicillin-Binding Proteins; Cytoskeleton; Research Article; Cytokinesis

Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system function when essential accessory components of the machinery are inactivated. This PBP2 variant hyperactivates cell wall synthesis in vivo and stimulates the activity of RodA-PBP2 complexes in vitro. Cells with the activated synthase also exhibited enhanced polymerization of the actin-like MreB component of the Rod system. Our results define an activation pathway governing Rod system function in which PBP2 conformation plays a central role in stimulating both glycan polymerization by its partner RodA and the formation of cytoskeletal filaments of MreB to orient cell wall assembly. In light of these results, previously isolated mutations that activate cytokinesis suggest that an analogous pathway may also control cell wall synthesis by the division machinery.